AUTHOR INDEX VOLUME 145 A Benz, EJ., Jr. Sec Mattagajasingh, Huang, Hartenstein. Snyder. Marches!, and Benz. Adams. I.R., and Kilmartin, J.V. Localization of core spindle pole Bergeron. JJ.M. See Dominguez. Fazel. Dahan, Lovell, Hermo, body (SPB) components during SPB duplication in Saccharoniy- Claude. Melan^on. and Bergeron. ces cerevisiae. 809. Berrueta, L. See Tirnauer, O'Toole, Berrueta, Bierer, and Peilman. Ahmad. FJ., Yu. W., McNally, FJ., and Baas. P.W. An essential role Berthold, C.-H, See Pekny, Johansson, Eliasson, Stakeberg. Wallen. for katanin in severing microtubules in the neuron. 305. Perlmann, Lendahl, Betsholtz. Berthold, and Frisen. Akanbi. K. See French. Smith, Akanbi, Sanford. Hecht. Farach- Betsholtz, C. See Pekny, Johansson, Eliasson. Stakeberg, Wallen, Carson. and Carson. Perlmann, Lendahl, Betsholtz, Berthold, and Frisen. Albar, J.P. See Puertollano, Martm-Belmonte, Millan, del Carmen de Bevis, B.J. See Rossanese. Soderholm. Bevis. Sears. O'Connor. Marco, Albar, Kremer, and Alonso. Williamson, and Glick. Albayya, F.P. See Michele, Albayya, and Metzger. Beyaert, R. See Heyninck, De Valck, Vanden Berghe, Van Albus, A. See Koch. Olson, Albus. Jin, Hunter. Brunken, Burgeson. Criekinge, Contreras. Fiers, Haegeman, and Beyaert. and Champliaud. Bhakta. S. See Bistrup, Bhakta, Lee, Belov, Gunn, Zuo, Huang, Allison, D.C., and Nestor, A.L. Evidence for a relatively random Kannagi, Rosen, and Hemmerich. array of human chromosomes on the mitotic ring. 1. Bickmorc, W.A. See Croft. Bridger, Boyle, Perry, Teague, and Alonso, M.A. See Puertollano, Martm-Belmonte, Millan, del Carmen Bickmore. de Marco. Albar, Kremer, and Alonso. Bierer, B.E. See Tirnauer, O'Toole, Berrueta. Bierer, and Peilman. Amberg, D.C. See Rodal. Tetreault, Lappalainen, Drubin, and Bijlmakers. M.-JJ.E., and Marsh, M. Trafficking of an acylated cyto¬ Amberg. solic protein: Newly synthesized p56'‘* travels to the plasma Anderson, HJ. See Sauve, Anderson, Ray. James, and Roberge. membrane via the exocytic pathway. 457. Andjelkovic. A.V., Spencer, D.I)., and Pachter, J.S. Visualization of Birge, R.B. See Oktay, Wary, Dans. Birge, and Giancotti. chemokine binding sites on human brain microvessels. 403. BischofT, F.R. See Paraskeva. Izaurralde, Bischoff, Huber, Kutay, Antony, C. See Mallard, Antony, Tenza, Salamero, Goud. and Hartmann, Luhrmann, and Gorlich. Johannes. Bistrup, A.. Bhakta, S., Lee, J.K., Belov, Y.Y., Gunn, M.D., Zuo, Aoki, J. See Takahashi, Nakanishi. Miyahara, Mandai. Satoh, Satoh. F.-R., Huang, C.-C., Kannagi. R., Rosen, S.D., and Hemmerich, Nishioka, Aoki, Nomoto. Mizoguchi. and Takai. S. Sulfotransferases of two specificities function in the recon¬ Aono, S., Nakagana, S., Reynolds, A.B., and Takeichi, M. pi20^'" struction of high endothelial cell ligands for L-selectin. 899. acts as an inhibitory regulator of cadherin function in colon car¬ Blackburn, E.H. See Smith and Blackburn. cinoma cells. 551. Blagoveshchenskaya, A.D., Hewitt. E.W., and Cutler, D.F. A com¬ Astier, M. See Fremion. Astier, Zaffran, Guillen, Homburger. and plex web of signal-dependent trafficking underlies the trior- Semeriva. ganellar distribution of P-selectin in neuroendocrine PC 12 cells. Astoul, E., Watton, S., and Cantrell, D. The dynamics of protein ki¬ 1419. nase B regulation during B cell antigen receptor engagement. Blobel. G. See Pemberton, Rosenblum, and Blobel. 1511. Blystone, S.D., Slater, S.E., Williams, M.P., Crow, M.T., and Brown, E J. A molecular mechanism of integrin crosstalk: a.p, Suppres¬ sion of calcium/calmodulin-dependent protein kinase 11 regu¬ lates a^Pi function. 889. Boitier, E., Rea, R., and Duchen, M.R. Mitochondria exert a negative B feedback on the propagation of intracellular Ca-" waves in rat cortical astrocytes. 795. Baart, E. See Woods. Hodges. Baart, Baker, Liskay, and Hunt. Bonifacino, J.S., and Dell'Angelica, E.C. Molecular bases for the rec¬ Baas, P.W. See Ahmad, Yu. McNally, and Baas. ognition of tyrosine-based sorting signals. 923. Bachorik, J.L. See Kataoka. Bachorik, and Dreyfuss. Bonini, S. See Pellegrini, Golisano, Paterna. Lambiase, Bonini. Bacick, I. See Tortorella. Story, Huppa, Wiertz, Jones, Bacik. Bennink, Rama, and De Luca. Yewdell, and Ploegh. Boonstra. J. See Keresztes and Boonstra. Bagrodia, S. See Turner, Brown, Perrotta. Riedy. Nikolopoulos. Borisy, G.G. See Svitkina and Borisy. McDonald. Bagrodia, Thomas, and Leventhal. Bornens, M. See Infante, Ramos-Morales. Fedriani, Bornens. and Baillie, D.L. See Ono, Baillie, and Benian. Rios. Bailly, M., Macaluso, F., Cammer, M., Chan, A., Segall, J.E., and Boyd, J.T. See Sells. Boyd, and Chernoff. Condeelis, J.S. Relationship between Arp2/3 complex and the Boyle, S. See Croft, Bridger, Boyle, Perry, Teague, and Bickmore. barbed ends of actin filaments at the leading edge of carcinoma Boyle, WJ. See Burgess, Qian. Kaufman. Ring. Van, Capparelli. cells after epidermal growth factor stimulation. 331. Kelley, Hsu, Boyle. Dunstan. Hu, and Lacey. Baird, B. See Sheets, Holowka. and Baird. Bray, P.G., Janneh, O., Raynes, KJ., Mungthin, M., Ginsburg, H., Baker, S.M. See Woods, Hodges. Baart. Baker, Liskay, and Hunt. and Ward, S.A. Cellular uptake of chloroquine is dependent on Baumgartner, S. See Martin, Zusman, Li, Williams, Khare, DaRocha, binding to ferriprotoporphyrin IX and is independent of NHE Chiquet-Ehrismann, and Baumgartner. activity in Plasmodium falciparum. 363. Beatty, W.L., Meresse, S., Gounun, P., Davuust, J., Mounier, J., Bridger, J.M, See Croft. Bridger. Boyle, Perry, Teague, and Bickmore. Sansunetti, PJ., and Gorvel, J.-P. Trafficking of Shigella li- Brown, E J, See Blystone. Slater, Williams. Crow, and Brown. popolysaccharide in polarized intestinal epithelial cells. 689. Brown, M.C. See Turner, Brown. Perrotta, Riedy, Nikolopoulos, Belmont, A.S. See Tumbar, Sudlow, and Belmont. McDonald, Bagrodia, Thomas, and Leventhal. Belov, Y.Y. See Bistrup, Bhakta, Lee, Belov, Gunn, Zuo, Huang, Briimmendorf, T. See Marg. Sirim, Spaltmann, Plagge, Kauselmann, Kannagi, Rosen, and Hemmerich. Buck. Rathjen. and Briimmendorf. Benian, G.M. See Ono, Baillie, and Benian. Brunken, WJ. See KtKh. Olson. Albus, Jin, Hunter, Brunken. Burgeson. Bennett, V. See Fukata, Oshiro, Kinoshita. Kawano, Matsuoka. and Champliaud. Bennett, Matsuura, and Kaibuchi. Buck. F. See Marg. Sirim, Spaltmann. Plagge. Kauselmann. Buck, Bennink, J.R. See Tortorelia, Story, Huppa. Wiertz. Jones. Bacik. Rathjen. and Briimmendorf. Bennink, Yewdell, and Ploegh. Burgeson, R.E. See KcKh. Olson, Albus, Jin, Hunter, Brunken, Bentley, D. See Lau, Zucker, and Bentley. Burgeson. and Champliaud. Author Index 1525 Burgess, T.L„ Qian. Y.-x., Kaufman, S„ Ring, B.I),, Van, G„ Capparelli, DaRocha. S. See Marlin, Zusman. Li. Williams. Khare. DaRocha. C., Kelley, M., Hsu, H., Boyle, WJ., Uunstan, C.R., Hu, S., and Chiquet-Ehrismann, and Baumgartner. Lacey, D.L. The ligand for osteoprotegerin (OPGL) directly ac¬ Davidson. L.A. See Murray. Davidson. Chapkin, Gustafson. Schat- tivates mature osteoclasts. 527. tenberg. and Fields. Buxbaum, R.E. See Heidemann. Kaech, Buxbaum. and Matus. Davoust, J. See Beatty. Meresse. Gounon. Davoust, Mounicr. Sansonetti. and Gorvel. Dawe, R.K. See Yu, Muszynski. and Dawe. Dechampesme, .V.-M., Koroleva, O., Leger-Silvestre, I., Gas, N., »nd C Camier, S. Assembly of 5S ribosomal RNA is required at a spe¬ cific step of the pre-rRNA processing pathway. 1.369. Deerinck, TJ, See Huang. Wang. Ma. Durick. Perkins, Deerinck, Caldwell, H. See Millward-Sadler, Wright. Lee. Nishida. Caldwell. Ellisman. and Taylor. Nuki. and Salter. Delamarre, L. See Rosenberg. Delamarre. Pique, Le Blanc. Griffith, Camier, S. See Dechampesme. Koroleva. Leger-Silvestre. Gas. and and Dokhelar. Camier. del Carmen de Marco, M. See Puertollano. Martm-Belmonte. Millan, Cammer, M. See Bailly. Macaluso. Cammer. Chan. Scgall. and del Carmen de Marco, Albar. Kremer. and Alonso. Condeelis. Dell'Angelica, E.C. See Bonifacino and Dell'Angelica. Campbell. K.P. See Crosbie, Lebakken. Holt. Venzke. Straub. Lee. De Luca, M. See Pellegrini. Golisano. Palerna. Lambiase. Bonini. Grady. Chamberlain. Sanes. and Campbell. Rama, and De Luca. Cantrell, 1). See Astoul. Watton. and Cantrell. DcMartino. G.N. .See Wigley. Fabunmi, Lee. Marino. Muallem. Capparelli. C. See Burgess. Qian. Kaufman. Ring. Van, Capparelli. DeMartino. and Thomas. Kelley. Hsu. Boyle, Dunstan. Hu. and Lacey. Dembo, M. See Oliver, Dembo. and Jacobson. Carbonetlo. S. See Montanaro. Lindenbaum. and Carbonetto. De Valck, D. See Heyninck. De Valck, Vanden Berghe, Van Carozzi, A. See Luetterforst, Stang. Zorzi. Carozzi. Way. and Parton. Criekinge. Contreras. Fiers. Haegeman. and Beyaert. Carpenter, C. See Kost. Lemichez, Spielhofer. Hong, Tolias. Carpenter, Dickmanns, A. See Kehlenbach. Dickmanns. Kehlenbach, Guan. and and Chua. Gerace. Carson. D.I). See French, Smith. Akanbi. Sanford, Hecht. Farach- Dimitrov, S. See Houchmandzadeh and Dimitrov. Carson. and Carson. Dokhelar, M.-C. See Rosenberg. Delamarre, Pique, Le Blanc, Griffith, Carter, W.G. See Ryan, Lee. Miyashita. and Carter. and Dokhelar. Chamberlain, J.S. See Crosbie. Lebakken, Holt. Venzke. Straub. Lee, Dominguez, M., Fazel, A., Dahan, S., Lovell, J., Hermo, L.. Claude, Grady, Chamberlain. Sanes. and Campbell. A., Melan^on, P., and Bergeron, JJ.M. Fusogenic domains of Champliaud, M.-F. See Koch. Olson. Albus. Jin, Hunter, Brunken, Golgi membranes are sequestered into specialized regions of the Burgeson. and Champliaud. Chan. A. See Bailly, Macaluso. Cammer. Chan, Segall, and Condeelis. stack that can be released by mechanical fragmentation. 673. Dreyfuss, G. See Kataoka. Bachorik, and Dreyfuss. Chan, C.S.M. See Kim, Kang, and Chan. Drubin, D.G. See Rcxlal. Tetreault. Lappalainen. Drubin. and Amberg. Chao. M.V. See Osterhout. Wolven, Wolf. Resh. and Chao. Duchen, M.R. See Boitier, Rea, and Duchen. Chapkin, R.S. See Murray. Davidson. Chapkin. Gustafson, Schat- tenberg. and Fields. Dunstan. C.R. See Burgess, Qian, Kaufman. Ring. Van. Capparelli, Kelley. Hsu, Boyle, Dunstan. Hu, and Lacey. Chen. J. See Taooka. Chen. Yednock. and Sheppard. Chernoff, J. See Sells. Boyd, and Chernoff. Duran, A. See Trilla, Duran, and Roncero. Durick, K. See Huang. Wang, Ma. Durick. Perkins, Deerinck. Ellisman. Chi, M.M.-Y. See Hughes. Chi. Lowry, and Gundersen. and Taylor. Chiquet-Ehrismann, R. See Martin. Zusman. Li. Williams. Khare. DaRocha. Chiquet-Ehrismann. and Baumgartner. Dyck, J.A. See Yeakley. Tronchere. Olesen, Dyck, Wang, and Fu. — See Oohashi. Zhou. Feng. Richter. Morgelin. Perez. Su, Chiquet- Ehrismann, Rauch, and Fassler. Chua. N.-H. See Kost. Lemichez. Spielhofer, Hong, Tolias. Carpenter, and Chua. E Chun, J. See Marszalek. Weiner. Farlow. Chun, and Goldstein. Claude, A. See Dominguez. Fazel. Dahan. Lovell, Hermo. Claude, Melan(;on. and Bergeron. Eferl, R., Sibilia, M., Hilbcrg, F., Fuchsbichicr, A., Kufferath, L, Colognato, H., Winkclmann, I).A., and Yurchenco, P.I). Laminin (lUertl. B., Zenz, R.. Wagner, E.F., and Zatloukal, K. Functions polymerization induces a receptor-cytoskeleton network. 619. of c-Jun in liver and heart development. 1049. Condeelis. J.S. See Bailly. Macaluso. Cammer. Chan. Segall, and Eichinger, L. See Karakesisoglou. Janssen. Eichinger. Noegel. and Condeelis. Schleicher. Contreras, R. See Heyninck. De Valck. Vanden Berghe. Van Eliasson, C. See Pekny. Johansson, Eliasson, Slakeberg. Wallen, Criekinge. Contreras. Fiers, Haegeman. and Beyaert. Perlmann. Lendahl, Betshollz. Berthold, and Frisen. Costantini, F. See Fagotto. Jho, Zeng. Kurth. Joos. Kaufmann. and Ellisman, M.H. See Huang, Wang. Ma, Durick, Perkins, Deerinck. Constantini. Ellisman, and Taylor. Cowan, N J. See Hansen, Cowan, and Welch. Espenshade, P. See Roberg, Crotwell. Espenshade. Gimeno. and Kaiser. Cox, A.I). See Keely. Rusyn. Cox. and Parise. Croft, J.A- Bridger, J.M., Boyle, S., Perry, P., Teague, P., and Bickmore, W'.A. Differences in the localization and morphology of chro¬ mosomes in the human nucleus. 1119. F Crosbie, R.H., Lebakken, C.S., Holt, K.H.. Venzke, l).P., Straub, V., Lee, J.C.. Grady, R.M.. Chamberlain. J.S., Sanes, J.R., and Campbell. K.P. Membrane targeting and stabilization of sar- Fabunmi, R.P. See Wigley, Fabunmi. Lee, Marino. Muallem, cospan is mediated by the sarcoglycan subcomplex. 153. DeMartino. and Thomas. Crotwell, M. See Roberg. Crotwell, Espenshade, Gimeno, and Kaiser. Fagotto, F., Jho, E.-h., Zeng, L., Kurth, T., Joos, T., Kaufmann, C., Crow, M.T. See Blystone. Slater. Williams, Crow, and Brown. and Costantini, F. Domains of Axin involved in protein-protein Cutler, D.F. See Blagoveshchenskaya. Hewitt, and Cutler. interactions. Wnt pathway inhibition, and intracellular localiza¬ tion. 741. Farach-Carson, M.C. See French, Smith. Akanbi. Sanford. Hecht. Farach-Carson. and Carson. Farlow, SJ. See Marszalek, Weiner, Farlow, Chun, and Goldstein. I) Farquhar, M.(L .See Lin, Yao, Hofmeister, Tsien, and Farquhar. Fassler, R. See Oohashi, Zhou, Feng. Richter, Morgelin. Perez. Su, Dahan. S. See Dominguez. Fazel, Dahan, Lovell. Hermo, Claude. Chiquet-Ehrismann. Rauch, and Fassler. Melan^on, and Bergeron. Fazel, A. See Dominguez. Fazel, Dahan, Lovell. Hermo. Claude, Dahlin, K. See Nishiyama. Dahlin. Prince, Johnstone, and Stallcup. Melan(;on. and Bergeron. Dans, M. See Oktay. Wary. Dans, Birge. and Giancotti. Fedriani, C. .See Infante, Ramos-Morales, Fedriani, Bornens, and Daro, E.A. See Sheff. Daro, Hull, and Mellman. Rios. The Journal of Cell Biology, Volume 14.5, 1999 1526 Feng, K. See Oohashi. Zhou. Feng. Richter. Morgelin. Perez. Su. Griiter, P. See Kramer. Griiter, Groning. and Kastner. Chiquet-Ehrismann. Rauch, and Fassler. Guan, T. See Kehlenbach, Dickmanns. Kehlenbach. Guan, and Gerace. Fields. A.P. See Murray. Davidson. Chapkin. Gustafson. Schat- Guertl, B. See Eferl. Sibilia, Hilberg. Fuchsbichler, Kufferath. Guertl, tenberg. and Fields. Zenz, Wagner, and Zatloukal. Fiers, W. 5t't' Heyninck. De Valck. Vanden Berghe. Van Criekinge. Guillen, A. See Fremion, Astier, Zaffran, Guillen. Homburger, and Contreras. Fiers. Haegeman. and Beyaert. Semeriva. Filippini, A. See Tripiciano. Peluso. Morena. Palombi. Stefanini. Gundersen, K. See Hughes. Chi, Lowry, and Gundersen. Ziparo. Yanagisawa. and Filippini. Gunn, M.D. See Bistrup, Bhakta. Lee. Belov, Gunn, Zuo, Huang. Finnegan, C.IM. See Tuma. Finnegan. Yi. and Hubbard. Kannagi. Rosen, and Hemmerich. Fischer von Mollard, G. See Ungermann. Fischer von Mollard. Gustafson, W.C. See Murray, Davidson, Chapkin. Gustafson, Schat- Jensen. Margolis. Stevens, and Wickner. tenberg. and Fields. Fisk, H.A., and Yaffe. M.P. A role for ubiquitination in mitochon¬ drial inheritance in Saccharomyces cerevisiae. 1199. Formenti, E. See Fraschini. Formenti. Lucchini, and Piatti. Fornerod. M. See Pritchard, Fornerod, Kasper, and van Deursen. H Fraschini, R.. Formenti, E., Lucchini, G., and Piatti, S. Budding yeast Bub2 is localized at spindle pole bodies and activates the mitotic Haegeman, G. See Heyninck, De Valck, Vanden Berghe, Van checkpoint via a different pathway from Mad2. 979. Criekinge. Contreras, Fiers, Haegeman. and Beyaert. Fremion, F., Astier, M., ZafTran, S., Guillen. .A., Homburger, V., and Hall, R.A., Premont, R.T., and Lefkowitz, RJ. Heptahelical receptor Semeriva, IM. The heterotrimeric protein G„ is required for the signaling: Beyond the G protein paradigm. 927. formation of heart epithelium in Drosophila. 1063. Hannun, Y.A. See Zhang, Reedy, Hannun, and Obeid. French, M.M., Smith. S.E., Akanbi, K., Sanford. T., Hecht, J., Farach- Hansen, WJ., Cowan, NJ., and Welch, WJ. Prefolding-nascent Carson, M.C., and Carson, Expression of the heparan sul¬ chain complexes in the folding of cytoskeleton proteins. 265. fate proteoglycan perlecan. during mouse embryogenesis and Hardisson, C. See Miguelez, Hardisson, and Manzanal. perlecan chondrogenic activity in vitro. 1103. Hartenstein, J.S. See Mattagajasingh, Huang. Hartenstein, Snyder. Frisen, J. See Pekny, Johansson, Eliasson. Stakeberg, Wallen, Marchesi. and Benz. Perlmann, Lendahl, Betsholtz. Berthold. and Frisen. Hartmann, E. See Paraskeva. Izaurralde. Bischoff, Huber. Kutay, Froehner, S.C. See Kachinsky. Froehner, and Milgram. Hartmann. Liihrmann, and Gorlich. Frdhiich, E. See Madeo. Frohlich, Ligr. Grey. Sigrist, Wolf, and Hayashi, K., Takahashi, IV1., Kimura, K., Nishida, W., Saga, H., and Frohlich. Sobue, K. Changes in the balance of phosphoinositide 3-kinase/ Friihlich, K.-U. See Madeo. Frohlich. Ligr. Grey. Sigrist. Wolf, and protein kinase B (Akt) and the mitogen-activated protein ki¬ Frohlich. nases (ERK/p38MAPK) determine a phenotype of visceral and Fu, X.-I). See Yeakley, Tronchere. Olesen, Dyck. Wang, and Fu. vascular smooth muscle cells. 727. Fuchsbichler, A. See Eferl, Sibilia, Hilberg, Fuchsbichler, Kufferath. Hecht, J. See French, Smith, Akanbi, Sanford, Hecht. Farach-Carson, Guertl, Zenz, Wagner, and Zatloukal. and Carson. Fujimoto, K. See Morita. Sasaki, Fujimoto. Furuse, and Tsukita. Heidemann, S.R., Kaech, S., Buxbaum, R.E., and Matus, A. Direct Fukata, Y., Oshiro, N., Kinoshita, N., Kawano, Y., IVlatsuoka, Y., observations of the mechanical behaviors of the cytoskeleton in Bennett, V., Matsuura, Y., and Kaibuchi, K. Phosphorylation of living fibroblasts. 109. adducin by Rho-kinase plays a crucial role in cell motility. 347. Helenius, A. See Kann, Sodeik, Vlachou, Gerlich. and Helenius. Furuse, M. Sec Morita. Sasaki, Fujimoto, Furuse. and Tsukita. Hemmerich, S. See Bistrup, Bhakta. Lee, Belov. Gunn, Zuo. Huang. Kannagi. Rosen, and Hemmerich. Hermo, L. See Dominguez, Fazel. Dahan, Lovell. Hermo. Claude. C, Melanqon, and Bergeron. Herskowitz, i. See Sanders, Gentzsch. Tanner, and Herskowitz. Hewitt. E.W, See Blagoveshchenskaya. Hewitt, and Cutler. (las, N. See Dechampesme. Koroleva. Leger-Silvestre, Gas, and Heyninck, K.. De Valck, D., Vanden Berghe. W., Van Criekinge, W., Camier. Contreras, R.. Fiers, W., Haegeman. G., and Beyaert, R. The (ient/sch, L. See Sanders. Gentzsch, Tanner, and Herskowitz. zinc finger protein A2() inhibits TNF-induced NF-KB-dependent (ierace, L. See Kehlenbach, Dickmanns, Kehlenbach. Guan. and gene expression by interfering with an RIP- or TRAF2-medi- Gerace. ated transactivation signal and directly binds to a novel NF-kB- (•erlich, W.H. See Kann. Sodeik, Vlachou. Gerlich, and Helenius. inhibiting protein ABIN. 1471. Ghitescu, L. See Stan, Ghitescu. Jacobson, and Palade. Hieter, P. See Hyland. Kingsbury. Koshland, and Hieter. (iiancotti, F.G. See Oktay. Wary. Dans, Birge. and Giancotti. Hilberg, F. See Eferl, Sibilia. Hilberg. Fuchsbichler, Kufferath, Ciijdn. M.A., Spencer, D.M., Kaiser, A.L., and Leslie, C.C. Role of Guertl. Zenz. Wagner, and Zatloukal. phosphorylation sites and the C2 domain in regulation of cyto¬ Hiraoka, Y. See Yamamoto, West. McIntosh, and Hiraoka. solic phospholipase Ai. 1219. Hirokawa, N. See Takeda. Yonekawa, Tanaka. Okada, Nonaka, and Gimenu, R. See Roberg, Crotwell, Espenshade. Gimeno. and Kaiser, Hirokawa. (iinsburg, H. See Bray. Janneh. Raynes, Mungthin. Ginsburg, and — See Terada. Tsujimoto. Takei. Takahashi, and Hirokawa. Ward. Hodges, C.A. See Woods. Hodges. Baart. Baker, Liskay. and Hunt. Glick, B.S. See Rossanese. Soderholm, Bevis, Sears, O'Connor, Hofmeister, R. See Lin, Yao, Hofmeister. Tsien, and Farquhar. Williamson, and Glick. Holowka, D. See Sheets, Holowka. and Baird. Cioldstein, L.S.B. See Marszalek. Weiner. Farlow. Chun, and Goldstein, Holt, K.H. See Crosbie. Lebakken, Holt, Venzke, Straub. Lee. (lolisano, (). See Pellegrini, Golisano. Paterna. Lambiase, Bonini, Grady. Chamberlain. Sanes, and Campbell. Rama, and De Luca. Homburger, V. See Fremion, Astier. Zaffran, Guillen, Homburger, (idriich, I), See Paraskeva, Izaurralde. Bischoff, Huber. Kutay, and Semeriva. Hartmann, Liihrmann. and Gbrlich. Hong, Y, See Kost. Lemichez, Spielhofer. Hong. Tolias. Carpenter, (iurvel, J.-P. See Beatty. Meresse. Gounon, Davoust, Mounier. and Chua. Sansonetti, and Gorvel. Houchmandzadeh, B., and Dimitrov, S. Elasticity measurements (lOud, B. See Mallard, Antony. Tenza. Salamero. Goud. and Johannes, show the existence of thin rigid cores inside mitotic chromo¬ (iuunon, P. See Beatty, Meresse. Gounon, Davoust. Mounier, San¬ somes. 215. sonetti, and Gorvel. Hsu, H. See Burgess. Qian. Kaufman. Ring. Van. Capparelli, Kelley. (irady, R.M. See Crosbie. Lebakken. Holt, Venzke. Straub. Lee. Hsu. Boyle. Dunstan. Hu, and Lacey. Grady. Chamberlain. Sanes, and Campbell. Hu, S. See Burgess. Oian. Kaufman. Ring, Van. Capparelli. Kelley, Grancell, A.S. See Russell. Grancell, and Sorger. Hsu, Boyle, Dunstan. Hu. and Lacey. (ireenwald, I. See Wen and Greenwald. Huang, C,-C. See Bistrup, Bhakta. Lee. Belov. Gunn. Zuo, Huang. (irey, M. See Madeo, Frohlich. Ligr, Grey. Sigrist, Wolf, and Kannagi, Rosen, and Hemmerich. Frohlich. Huang, LJ., Wang, L., Ma, Y., Durick, K., Perkins, G., Deerinck, TJ., (■riffith. (i. See Rosenberg, Delamarre, Pique. Le Blanc. Griffith, and Ellisman, M.H., and Taylor, S.S. NH2-terminal targeting motifs Dokhelar. direct dual specificity A-kinase-anchoring protein 1 (D-AKAPl) (>r<ining, K. See Kramer, Grutcr, Grdning. and Kastner. to either mitochondria or endoplasmic reticulum. 951. Author liule.x 1527 Huang. S.-C. See Mattagajasingh. Huang, Hartenstein, Snyder. Karaplis, A. See Serra, Karaplis. and Sohn. Marchesi. and Benz. Kasper, L.H. See Pritchard, Fornerod. Kasper, and van Deursen. Hubbard. A.L. See Tuma. Finnegan, Yi, and Hubbard. Kastner, B. See Kramer. Gruter. Grdning, and Kastner. Huber, J. See Paraskeva. Izaurralde, Bischoff, Huber. Kutay. Hart¬ Kataoka. N., Bachorik, J.L., and Dreyfuss, G. Transportin-SR. A nu¬ mann, LUhrmann, and Gdriich. clear import receptor for SR proteins. 1145. Hughes. S.IV1., Chi. IVI.M.-Y., Lowry, O.H., and Gundersen, K. Myo- Kaufman, S. See Burgess, Qian, Kaufman. Ring. Van. Capparelli, genin induces a shift of enzyme activity from glycolytic to oxida¬ Kelley. Hsu, Boyle. Dunstan. Hu, and Lacey. tive metabolism in muscles of transgenic mice. 633. Kaufmann, C. See Fagotto, Jho, Zeng. Kurth, Joos, Kaufmann, and Hull. M. See Sheff, Daro, Hull, and Mellman. Constantini. Hunt. P.A. See Woods. Hodges, Baart. Baker. Liskay. and Hunt. Kauselmann, G. See Marg, Sirim, Spaltmann. Plagge. Kauselmann. Hunter, D.D. See Kwh, Olson, Albus. Jin. Hunter, Brunken, Burgeson, Buck. Rathjen. and Brummendorf. and Champliaud. Kawano. Y. See Fukata, Oshiro, Kinoshita. Kawano, Matsuoka, Huppa, J.B. See Tortorella, Story. Huppa. Wiertz. Jones. Bacik. Bennett. Matsuura, and Kaibuchi. Bennink. Yewdell, and Ploegh. Kay, S.A. See Yamaguchi, Nakamura, Mochizuki, Kay, and Nagatani. Hyland, K.M., Kingsbury, J., Koshland, I)., and Hieter, P. Ctfl9p: A Keely, PJ., Rusyn, E.V„ Cox, A.D., and Parise, L.V. R-Ras signals novel kinetochore protein in Saccfuiromyces cerevisiae and a po¬ through specific integrin a cytoplasmic domains to promote tential link between the kinetochore and mitotic spindle. 15. migration and invasion of breast epithelial cells. 1077. Kehlenbach, A. Set* Kehlenbach, Dickmanns. Kehlenbach, Guan, and Gerace. Kehlenbach, R.H, Dickmanns, A., Kehlenbach, A., Guan. T., and 1 Gerace, L. A role for RanBPl in the release of CRMl from the nuclear pore complex in a terminal step of nuclear export. 645. Infante, C., Ramos-Morales, F., Fedriani, C., Bornens, M., and Rios, Kelley, M. See Burgess, Qian, Kaufman, Ring, Van, Capparelli, R.M. GMAP-21(). A cis-Golgi network-associated protein, is a Kelley, Hsu. Boyle. Dunstan. Hu, and Lacey. minus end microtubule-binding protein. 83. Keresztes, M., and Boonstra, J. Import(ance) of growth factors in(to) Izaurralde, E. See Paraskeva. Izaurralde. Bischoff, Huber. Kutay. the nucleus. 421. Hartmann. LUhrmann. and Gorlich. Khare, N. See Martin. Zusman, Li, Williams, Khare. DaRocha, Chiquet-Ehrismann, and Baumgartner. Kilmartin. J.V. See Adams and Kilmartin. Kim, J.-h., Kang, J.-s., and Chan, C.S.M. Slil5 associates with the Ipll J protein kinase to promote proper chromosome segregation in Saccharomyces cerevisiae. 1381. Jacobson, B.S. See Stan, Ghitescu, Jacobson, and Palade. Kimura, K. See Hayashi. Takahashi. Kimura. Nishida. Saga, and Sobue. Jacobson, K. See Oliver, Dembo, and Jacobson. Kingsbury, J. See Hyland, Kingsbury, Koshland, and Hieter. James. W.M. See Sauve. Anderson, Ray. James, and Roberge. Kinoshita, N. See Fukata, Oshiro, Kinoshita, Kawano. Matsuoka, Janicki. S.M. See Stabler, Ostrowski, Janicki, and Monteiro. Bennett. Matsuura, and Kaibuchi. Janneh, O. See Bray, Janneh. Ravnes. Mungthin, Ginsburg. and Koch, M., Olson, P.F., Albus, A., Jin, W., Hunter, D.D., Brunken, Ward. W,J., Burgeson, R.E., and Champliaud, M.-F. Characterization Janssen, K.-P. See Karakesisoglou. Janssen, Eichinger, Noegel, and and expression of the laminin ^3 chain: A novel, non-basement Schleicher. membrane-associated, laminin chain. 605. Jensen, O.N. See Ungermann. Fischer von Mollard, Jensen. Margolis, Koroleva, O. See Dechampesme. Koroleva. Leger-Silvestre, Gas, and Stevens, and Wickner. Camier. Jho, E.-h. See Fagotto. Jho. Zeng, Kurth. Joos, Kaufmann. and Koshland, D. See Hyland, Kingsbury, Koshland, and Hieter. Constantini. Kost, B., Lemichez, E., Spielhofer, P., Hong, Y., Tolias, K., Carpenter, Jin, W, See Koch, Olson, Albus. Jin. Hunter. Brunken, Burgeson. and C., and Chua, N.-H, Rac homologues and compartmentalized Champliaud. phosphatidylinositol 4,5-bisphosphate act in a common pathway Johannes, L. See Mallard, Antony, Tenza. Salamero. Goud. and to regulate polar pollen tube growth. 317. Johannes. Kramer, A., Gruter, P., Griming, K., and Kastner, B. Combined bio¬ Johansson, C.B. See Pekny. Johansson. Eliasson, Stakeberg, Wallen, chemical and electron microscopic analyses reveal the architec¬ Perlmann, Lendahl, Betsholtz. Berthold. and Frisen. ture of the mammalian U2 snRNP. 13.55. Johnstone, S. See Nishiyama. Dahlin, Prince, Johnstone, and Stallcup. Kremer, L. See Puertollano, Martin-Belmonte, Millan, del Carmen Jolly, C., Vourc’h, C., Robert-Nicoud, M., and Morimoto, R,l. de Marco. Albar. Kremer. and Alonso. Intron-independent association of splicing factors with active Kufferath, 1. See Eferl, Sibilia, Hilberg, Fuchsbichler, Kufferath. genes. 1133. GuertI, Zenz. Wagner, and Zatloukal. Jones T.R. See Tortorella. Story, Huppa. Wiertz, Jones, Bacik, Bennink, Kurth, T. See Fagotto. Jho, Zeng. Kurth. Joos. Kaufmann, and Yewdell. and Ploegh. Constantini. Joos, T. See Fagotto. Jho, Zeng. Kurth. Joos, Kaufmann, and Kutay, U. See Paraskeva. Izaurralde. Bischoff, Huber. Kutay, Hart¬ Constantini. mann, LUhrmann. and Gdriich. K L Kachinsky, A.M., Froehner, S.C., and Milgram, S.L. A PDZ-contain- ing scaffold related to the dystrophin complex at the basolateral Lacey, D.L, See Burgess, Qian. Kaufman, Ring. Van, Capparelli, membrane of epithelial cells. 391. Kelley, Hsu, Boyle, Dunstan, Hu, and Lacey. Kaech, S. See Heidemann, Kaech. Buxbaum. and Matus. Lambiase, A. See Pellegrini. Golisano, Paterna. Lambiase, Bonini, Kaibuchi, K. See Fukata, Oshiro. Kinoshita. Kawano, Matsuoka, Rama, and De Luca. Bennett, Matsuura, and Kaibuchi. Lappalainen, P. See Rodal, Tetreault, Lappalainen, Drubin, and Kaiser, A.L. See Gijdn. Spencer. Kaiser, and Leslie. Amberg. Kaiser, C.A. See Roberg, Crotwell. Espenshade, Gimeno, and Kaiser. Larsson, C, See Zeidman, Ldfgren, PShlman, and Larsson. Kang, J.-s. See Kim. Kang, and Chan. Lau, P., Zucker, R.S., and Bentley, D. Induction of filopodia by di¬ Kann, M., Sodeik, B., V'lachou, A., Gerlich, W.H., and Helenius, A. rect local elevation of intracellular calcium ion concentration. Phosphorylation-dependent binding of hepatitis B virus core 1265. particles to the nuclear pore complex. 45. Lebakken, C,S. See Crosbie, Lebakken, Holt, Venzke, Straub, Lee, Kannagi, R. See Bistrup, Bhakta, Lee, Belov, Gunn, Zuo, Huang. Grady, Chamberlain, Sanes. and Campbell. Kannagi, Rosen, and Hemmerich. Le Blanc, 1. See Rosenberg, Delamarre, Pique, Le Blanc, Griffith, Karakesisoglou, I., Janssen, K.-P,, Eichinger, L., Noegel, A.A., and and Dokhelar. Schleicher, M, Identification of a suppressor of the Dictyostelium Lee, H.-S. See Millward-Sadler, Wright, Lee, Nishida, Caldwell, profilin-minus phenotype as a CD36/L1MP-1I homologue. 167. Nuki, and Salter. The Journal of Cell Biology, Volume 145, 1999 1528 Lee, J.C. See Crosbie, Lebakken, Holt, Venzke, Straub, Lee, Grady, Matsuura, Y. See Fukata, Oshiro, Kinoshita, Kawano, Matsuoka, Chamberlain, Sanes, and Campbell. Bennett, Matsuura, and Kaibuchi. Lee, J.K. See Bistrup, Bhakta, Lee, Belov, Gunn, Zuo, Huang, Mattagajasingh, S.N., Huang, S.-C., Hartenstein, J.S., Snyder, M., Kannagi, Rosen, and Hemmerich. Marches!, V.T., and Benz, EJ., Jr. A nonerythroid isoform of Lee, K. See Ryan, Lee, Miyashita, and Carter. protein 4.1 R interacts with the nuclear mitotic apparatus Lee, M.G. See Wigley, Fabunmi, Lee, Marino, Muallem, DeMartino, (NuMA) protein. 29. and Thomas. Matus, A. See Heidemann, Kaech, Buxbaum, and Matus. Lefkowitz, R J. See Hall. Fremont, and Lefkowitz. McDonald, A.R. See Turner, Brown, Perrotta, Riedy, Nikolopoulos, Leger-Silvestre, 1. See Dechampesme, Koroleva, Leger-Silvestre, McDonald, Bagrodia. Thomas, and Leventhal. Gas, and Camier. McIntosh, J.R. See Yamamoto, West, McIntosh, and Hiraoka. Lemichez, E. See Kost, Lemichez, Spielhofer, Hong, Tolias, Carpenter, McNally, FJ. See Ahmad, Yu, McNally, and Baas. and Chua. Meeusen, S., Tieu, Q., Wong, E., Weiss, E., Schieltz, D., Yates, J.R., Lendahl, G. See Pekny, Johansson, Eliasson, Stakeberg, Wallen, and Nunnari, J. MgmlOlp is a novel component of the mito¬ Perlmann, Lendahl, Betsholtz, Berthold. and Frisen. chondrial nucleoid that binds DNA and is required for the re¬ Leslie, C.C. See Gijon, Spencer, Kaiser, and Leslie. pair of oxidatively damaged mitochondrial DNA. 291. Leventhal, P.S. See Turner, Brown, Perrotta, Riedy, Nikolopoulos, Meijer, M. See Merlin, Voos, Maarse, Meijer, Pfanner, and Rassow. McDonald, Bagrodia. Thomas, and Leventhal. Melangon, P. See Dominguez, Fazel, Dahan, Lovell, Hermo, Claude, Li, X. See Martin, Zusman, Li, Williams, Khare, DaRocha, Chiquet- Melanqon, and Bergeron. Ehrismann, and Baumgartner. Mellman, I. See Sheff, Daro, Hull, and Mellman. Ligr, iVl. See Madeo, Frohlich, Ligr, Grey, Sigrist, Wolf, and Frohlich. Meresse, S. See Beatty, Meresse, Gounon, Davoust, Mounier, Lin, P., Yao, Y., Hofmeister, R., Tsien, R.Y., and Farquhar, M.G. Sansonetti, and Gorvel. Overexpression of CALNUC (nucleobindin) increases agonist Merlin, A., Voos, W., Maarse, A.C., Meijer, M., Pfanner, N., and and thapsigargin releasable Ca^^ storage in the Golgi. 279. Rassow, J. The J-related segment of Tim44 is essential for cell Lindenbaum, M. See Montanaro, Lindenbaum, and Carbonetto. viability: A mutant Tim44 remains in the mitochondrial import Liskay, M. See Woods, Hodges, Baart, Baker, Liskay, and Hunt. site, but inefficiently recruits mtHsp70 and impairs protein Lofgren, B. See Zeidman, Ldfgren, Pdhlman, and Larsson. translocation. 961. Lovell, J. See Dominguez, Fazel, Dahan, Lovell, Hermo, Claude, Metzger, J.M. See Michele, Albayya, and Metzger. Melan^on, and Bergeron. Michele, D.E., Albayya, F.P,, and Metzger, J.M. Thin filament pro¬ Lowry, O.H. See Hughes. Chi, Lowry, and Gundersen. tein dynamics in fully differentiated adult cardiac myocytes; Lucchini, G. See Fraschini, Formenti, Lucchini, and Piatti. Toward a model of sarcomere maintenance. 1483. Luetterforst, R., Stang, E., Zorzi, N>, Carozzi, A., Way, M., and Parton, Miguelez, E.M., Hardisson, C., and Manzanal, M.B. Hyphal death R.G. Molecular characterization of caveolin association with the during colony development in Streptomyces antibioticus: Mor¬ Golgi complex; Identification of a cis-Golgi targeting domain in phological evidence for the existence of a process of cell deletion the caveolin molecule. 1443. in a multicellular prokaryote. 515. Liihrmann, R. See Paraskeva, Izaurralde, Bischoff, Huber, Kutay, Milgram, S.L. See Kachinsky, Froehner, and Milgram. Hartmann, Liihrmann, and Gorlich. Millan, J. See Puertollano, Martin-Belmonte, Millan, del Carmen de Marco, Albar, Kremer, and Alonso. Millward-Sadler, SJ., Wright, M.O., Lee, H.-S., Nishida, K., Caldwell, H., Nuki, G., and Salter, D.M. Integrin-regulated secretion of in¬ M terleukin 4: A novel pathway of mechanotransduction in human articular chondrocytes. 183. Ma, Y. See Huang, Wang, Ma, Durick, Perkins, Deerinck, Ellisman, Miyahara, M. See Takahashi, Nakanishi, Miyahara, Mandai. Satoh, and Taylor. Satoh, Nishioka, Aoki, Nomoto, Mizoguchi, and Takai. Maarse, A.C. See Merlin. Voos, Maarse, Meijer, Pfanner, and Miyashita, Y. See Ryan, Lee, Miyashita, and Carter. Rassow. Mizoguchi, A. See Takahashi, Nakanishi, Miyahara. Mandai, Satoh, Macaluso, F. See Bailly, Macaluso, Cammer, Chan, Segall, and Satoh, Nishioka, Aoki, Nomoto, Mizoguchi, and Takai. Condeelis. Mochizuki, N. See Yamaguchi, Nakamura, Mochizuki, Kay, and Madeo, F., Frohlich, E., Ligr, M., Grey, M., Sigrist, SJ., Wolf, D.H., Nagatani. and Frohlich, K.-G. Oxygen stress: A regulator of apoptosis in Montanaro, F., Lindenbaum, M., and Carbonetto, S. a-Dystroglycan yeast. 757. is a laminin receptor involved in extracellular matrix assembly Mallard, F., Antony, C., Tenza, D., Salamero, J., Goud, B., and on myotubes and muscle cell viability. 1325. Johannes, L. Direct pathway from early/recycling endosomes to Monteiro, M J. See Stabler, Ostrowski, Janicki, and Monteiro. the golgi apparatus revealed through the study of Shiga toxin Morena, A.R. See Tripiciano, Peluso, Morena, Palombi, Stefanini, B-fragment transport [143(4):973]: Correction. 1521. Ziparo, Yanagisawa, and Filippini. Mandai, K. See Takahashi, Nakanishi, Miyahara, Mandai. Satoh, Morgelin, M. See Oohashi, Zhou, Feng, Richter, Morgelin, Perez, Su, Satoh, Nishioka, Aoki, Nomoto, Mizoguchi, and Takai. Chiquet-Ehrismann, Rauch, and Fassler. Manzanal, M.B. See Miguelez, Hardisson, and Manzanal. Morimoto, R.I. See Jolly, Vourc’h, Robert-Nicoud, and Morimoto. Marches!, V.T. See Mattagajasingh, Huang, Hartenstein, Snyder, Morita, K., Sasaki, H., Fujimoto, K., Furuse, M., and Tsukita, S. Marches!, and Benz. Claudin-ll/OSP-based tight junctions of myelin sheaths in brain Marg, A., Sirim, P., Spaltmann, F., Plagge, A., Kauselmann, G., and Sertoli cells in testis. 579. Buck, F., Rathjen, F.G., and Briimmendorf, T. Neurotractin, A Mounier, J. See Beatty, Meresse, Gounon, Davoust, Mounier, novel neurite outgrowth-promoting Ig-like protein that interacts Sansonetti, and Gorvel. with CEPG-1 and LAMP. 865. Muallem, S. See Wigley, Fabunmi, Lee, Marino, Muallem. DeMartino, Margolis, N. See Gngermann, Fischer von Mollard, Jensen, Margolis, and Thomas. Stevens, and Wickner. Mungthin, M. See Bray, Janneh, Raynes, Mungthin, Ginsburg, and Marino, C.R. See Wigley, Fabunmi, Lee, Marino, Muallem, DeMartino, Ward. and Thomas. Murray, N.R., Davidson, L.A., Chapkin, R.S., Gustafson, W.C., Marsh, M, See Bijlmakers and Marsh. Schattenberg, D.G., and Fields, A.P. Overexpression of protein Marszalek, J.R., Weiner, J.A., Farlow, SJ., Chun, J., and Goldstein, kinase C Pn induces colonic hyperproliferation and increased L.S.B. Novel dendritic kinesin sorting identified by different sensitivity to colon carcinogenesis. 699. process targeting of two related kinesins: KIF21A and KIF21B. Muszynski, M.G. See Yu, Muszynski, and Dawe. 469. Martin, D., Zusman, S., Li, X., Williams, E.L., Khare, N., DaRocha, S., Chiquet-Ehrismann, R., and Baumgartner, S. wing blister, A new Drosophila laminin a chain required for cell adhesion and N migration during embryonic and imaginal development. 191. Martin-Belmonte, F. See Puertollano, Martm-Belmonte, Millan, del Nagatani, A. See Yamaguchi, Nakaniura, Mochizuki, Kay, and Nagatani. Carmen de Marco, Albar, Kremer, and Alonso Nakagawa, S. See Aono, Nakagawa, Reynolds, and Takeichi. Matsuoka, Y. See Fukata, Oshiro, Kinoshita, Kawano, Matsuoka, Nakamura, M, See Yamaguchi, Nakamura, Mochizuki. Kay, and Bennett, Matsuura. and Kaibuchi. Nagatani. Author Index 1529 Nakanishi, H. See Takahashi, Nakanishi, Miyahara, Mandai. Satoh. Pellegrini, G., Golisano, O., Paterna. P., Lambiase, A., Bonini, S., Satoh. Nishioka, Aoki. Nomoto. Mizoguchi. and Takai. Rama, P., and l)e Luca, IV1. Location and clonal analysis of stem Nestor, A.L. See Allison and Nestor. cells and their differentiated progeny in the human ocular sur¬ Nikolopoulos, S.N. Turner, Brown. Perrotta. Riedy. Nikolopoulos. face. 769. McDonald, Bagrodia, Thomas, and Leventhal. Pellman, I). See Tirnauer. O'Toole. Berrueta. Bierer. and Pellman. Nishida, K. See Millward-Sadler. Wright. Lee. Nishida, Caldwell. Peluso, C. See Tripiciano. Peluso. Morena. Palombi, Stefanini, Nuki. and Salter. Ziparo. Yanagisawa. and Filippini. Nishida, W. See Hayashi. Takahashi, Kimura, Nishida. Saga, and Sobue. Pemberton, L.F., Rosenblum, J.S., and Blobel, G. Nuclear import of Nishioka. H. See Takahashi, Nakanishi. Miyahara, Mandai, Satoh. the TATA-binding protein; Mediation by the karyopherin Satoh. Nishioka. Aoki, Nomoto, Mizoguchi, and Takai. Kapil4p and a possible mechanism for intranuclear targeting. Nishiyama. A., Dahlin, K., Prince. J., Johnstone, S., and Stallcup. 1407. W.B. The primary' structure of NG2, a novel membrane-spanning Peng, H.B., Xie, H., Rossi, S.G., and Rotundo, R.L. Acetylcholine¬ proteoglycan [114(5):3.S9]: Correction. 1117. sterase clustering at the neuromuscular junction involves perle- Noegel, A.A. See Karakesisoglou. Janssen. Eichinger, Noegel, and can and dystroglycan. 911. Schleicher. Perez, M.T. See Oohashi, Zhou, Feng. Richter. Morgelin. Perez. Su. Nomoto, A. See Takahashi. Nakanishi, Miyahara. Mandai. Satoh. Chiquet-Ehrismann. Rauch, and Fassler. Satoh. Nishioka, Aoki. Nomoto. Mizoguchi, and Takai. Perkins G. See Huang, Wang. Ma. Durick. Perkins. Deerinck. Ellisman. Nonaka, S. See Takeda. Yonekawa. Tanaka. Okada. Nonaka, and and Taylor. Hirokawa. Perlmann, T. See Pekny. Johansson, Eliasson, Stakeberg. Wallen, Nuki. G. See Millward-Sadler. Wright. Lee. Nishida. Caldwell, Nuki. Perlmann. Lendahl. Betsholtz, Berthold, and Frisen. and Salter. Perrotta, J.A. See Turner. Brown. Perrotta. Riedy. Nikolopoulos. Nunnari, J. See Meeusen. Tieu. Wong. Weiss. Schieltz, Yates, and McDonald. Bagrodia. Thomas, and Leventhal. Nunnari. Perry, P. See Croft, Bridget. Boyle, Perry, Teague, and Bickmore. Pfanner, N. See Merlin. Voos, Maarse, Meijer, Pfanner. and Rassow. Piatti, S. See Fraschini. Formenti. Lucchini. and Piatti. O Pique. C. See Rosenberg. Delamarre, Pique. Le Blanc. Griffith, and Dokhelar. Plagge, A. See Marg. Sirim. Spaltmann. Plagge. Kauselmann, Buck. Obcid, L.M. See Zhang. Reedy. Hannun. and Obeid. Rathjen. and Briimmendorf. O'Connor, J. 5cc Rossanese, Soderholm, Bevis, Sears, O’Connor. Ploegh, H.L. See Tortorella. Story. Huppa, Wiertz. Jones. Bacik. Williamson, and Glick. Bennink. Yewdell. and Ploegh. Okada, Y. See Takeda, Yonekawa, Tanaka, Okada. Nonaka. and Premont, R.T. See Hall. Premont, and Lefkowitz. Hirokawa. Prince. J. See Nishiyama. Dahlin. Prince, Johnstone, and Stallcup. Oktay, M., Wary, K.K., Dans, M., Birge, R.B., and Giancotti, F.G. Pritchard. C.EJ., Fornerod, IM., Kasper, L.H., and van Deursen, integrin-mediated activation of focal adhesion kinase is required J.M.A. RAEI is a shuttling mRNA export factor that binds to a for signaling to Jun NHi-terminal kinase and progression GLEBS-like NUP98 motif at the nuclear pore complex through through the G1 phase of the cell cycle. 1461. multiple domains. 237. Olcscn, J. See Yeakley. Tronchere, Olesen. Dyck. Wang, and Fu. Puertollano, R., IMartm-Belmonte, F., IMillan, J., del Carmen de Oliver, T., Dembo. M„ and Jacobson. K. Separation of propulsive Marco, M., Albar, J.P., Kremer, L., and Alonso, M.A. The M AL and adhesive traction stresses in locomoting keratocytes. .389. proteolipid is necessary for normal apical transport and accurate Olson, P.F. See Koch. Olson, Albus. Jin. Hunter. Brunken. Burgeson, sorting of the influenza virus hemagglutinin in Madin-Darby ca¬ and Champliaud. nine kidney cells. 141. Ono, S., Baillie, D.L., and Benian, G.M. L'NC-6()B. an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhahditis elegans body wall muscle. 491. Oohashi, T., Zhou, X.-H., Feng. K., Richter, B., Morgelin, M.. Perez, Q M.T., Su, W.-D., Chiquet-Ehrismann, R., Rauch, O., and Fassler, R. Mouse Ten-m/Odz is a new family of dimeric type II Qian, Y.-x. See Burgess. Qian. Kaufman, Ring. Van, Capparelli, transmembrane proteins expressed in many tissues.^ 563. Kelley. Hsu, Boyle. Dunstan, Hu, and Lacey. Oshiro, N. See Fukata, Oshiro. Kinoshita, Kawano, Matsuoka. Bennett, Matsuura. and Kaibuchi. Osterhout, DJ., W’olven, A.. Wolf, R.M., Resh, M.D., and Chao, M.V. Morphological differentiation of oligodendrocytes re¬ R quires activation of Fyn tyrosine kinase. 1209. Ostrowski, L.L. See Stabler, Ostrowski. Janicki, and Monteiro. Rama. P. See Pellegrini, Golisano. Paterna. Lambiase, Bonini. Rama, O'Toole, E. See Tirnauer. O'Toole, Berrueta, Bierer. and Pellman. and De Luca. Ramos-Morales, F. See Infante. Ramos-Morales, Fedriani. Bornens, and Rios. P Rassow, J. See Merlin. Voos. Maarse. Meijer. Pfanner. and Rassow. Rathjen, F.G. 5£'<’ Marg. Sirim. Spaltmann, Plagge. Kauselmann. Pachter, J.S, See Andjelkovic. Spencer, and Pachter. Buck. Rathjen. and Briimmendorf. Pahiman. S. See Zeidman, Ldfgren, PShlman. and Larsson. Rauch, U. See Oohashi, Zhou. Feng, Richter. Morgelin. Perez. Su. Palade. G.E. See Stan, Ghitescu. Jacobson, and Palade. Chiquet-Ehrismann. Rauch, and Fassler. Palombi. F. See Tripiciano, Peluso, Morena. Palombi, Stefanini. Ray, J.M. Sec Sauve. Anderson. Ray, James, and Roberge. Ziparo. Yanagisawa, and Filippini. Ravnes, KJ. See Bray. Janneh. Ravnes. Mungthin. Ginsburg, and Paraskeva, E., Izaurralde, E., Bischoff, F.R., Huber, J., Kutay, U., Ward. Hartmann. E., Liihrmann, R., and Gorlich, 1). CRM 1-mediated Rea, R, See Boitier. Rea, and Duchen. recycling of snurportin 1 to the cytoplasm. 255. Reedy, M.C. See Zhang. Reedy, Hannun. and Obeid. Parise, L.V. See Keely, Rusyn, Cox. and Parise. Resh. M.D. See Osterhout. Wolven, Wolf, Resh, and Chao. Parton. R.G. See Luetterforst. Stang, Zorzi, Carozzi. Way, and Parton. — See van’t Hof and Resh. Paterna, P, See Pellegrini. Golisano. Paterna. Lambiase, Bonini. Reynolds, A.B. See Aono. Nakagawa. Reynolds, and Takeichi. Rama, and De Luca. Richter, B. See Oohashi. Zhou. Feng. Richter, Morgelin. Perez. Su. Pekny, M., Johansson. C.B., Eliasson, C., Stakeberg, J., Wallen, A., Chiquet-Ehrismann. Rauch, and Fassler. Perlmann, T., Lendahl, U., Betsholtz, C., Berthold, C.-H., and Ridley, AJ. See Wojciak-Stothard. Williams, and Ridley. Frisen, J. Abnormal reaction to central nervous system injury in Riedy, M.C. See Turner, Brown, Perrotta. Riedy. Nikolopoulos. mice lacking glial fibrillary acidic protein and vimentin. 503. McDonald, Bagrodia, Thomas, and Leventhal. Ring. B.D. See Burgess. Qian, Kaufman. Ring. Van, Capparelli. Kelley, Hsu, Boyle, Dunstan. Hu, and Lacey. Rios, R.M. See Infante, Ramos-Morales, Fedriani, Bornens. and ® The online version of this article contains supplemental material. Rios. The Journal of Cell Biology, Volume 145, 1999 15.30 Rober{>. KJ^ Crotwell, Espenshade, Gimeno, and Kaiser, Sheff, D.R., Daro, E.A., Hull, M., and Mellman, I. The receptor recy¬ C.A. LST! is a SEC24 homologuc used for selective export of the cling pathway contains two distinct populations of early endo- plasma membrane ATPase from the endoplasmic reticulum. 659. somes with different sorting functions. 123. Roberge, M. See Sauve. Anderson. Ray. James, and Roberge. Sheppard. D. See Taooka, Chen. Yednock. and Sheppard. Robert-Nicoud, M. See Jolly. Vourc'h. Robert-Nicoud, and Morimoto. Shore, G.C. See Schleiff, Silvius. and Shore. Rodal, A..\., Tetreault, J.W., Lappalainen. P., Drubin, D.G., and Sibilia, M. See Eferl. Sibilia, Hilberg, Fuchsbichler, Kufferath. Guertl. .4mberg, O.C. Aiplp interacts with cofilin to disassemble actin Zenz, Wagner, and Zatloukal. filaments. 1251. Sigrist, SJ. See Madeo. Frbhlich. Ligr. Grey, Sigrist. Wolf, and Roncero, C. See Trilla. Duran, and Roncero. Frdhiich. Rosen, S.D, See Cistrup. Bhakta. Lee. Belov. Gunn. Zuo. Huang. Silvius, J.R. See Schleiff, Silvius, and Shore. Kannagi. Rosen, and Hemmerich. Sirim, P. 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Takahashi. Kimura, Nishida, Saga, and Sobue. Rotundo, R.L. See Peng. Xie. Rossi, and Rotundo. Sodeik, B. See Kann. Sodeik, Vlachou, Gerlich. and Helenius. Russell, 1.1)., Grancell, A.S., and Sorger, P.K. The unstable F-box Soderholm, J. See Rossanese, Soderholm. Bevis. Sears, O'Connor. protein p.58-Ctfl3 forms the structural core of the CBF3 kineto- Williamson, and Glick. chore complex. 933. Sohn, P. See Serra. Karaplis. and Sohn. Rusyn, E.V, See Keely. Rusyn. Cox. and Parise. Sorger, P.K. See Russell, Grancell, and Sorger. Ryan, IM.C., Lee, K., Miyashita, Y., and Carter, W.G. Targeted dis¬ Spaltmann, F. See Marg. Sirim. Spaltmann. Plagge. Kauselmann, ruption of the LAM A3 gene in mice reveals abnormalities in Buck. Rathjen. and Briimmendorf. survival and late stage differentiation of epithelial cells. 1309. Spencer, D.D, See Andjelkovic. Spencer, and Pachter. Spencer, D.M. See Gijon. Spencer, Kaiser, and Leslie. Spielhofer, P, See Kost. Lemichez. Spielhofer, Hong. 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See Luetterforst. Stang, Zorzi, Carozzi, Way. and Parton. Sanes, J.R. See Crosbie. Lebakken. Holt. Venzke. Straub, Lee. Stefanini, M. See Tripiciano, Peluso. Morena. Palombi. Stefanini. Grady. Chamberlain, Sanes, and Campbell. Ziparo, Yanagisawa. and Filippini. Sanford. T. See French. Smith, Akanbi, Sanford, Hecht, Farach- Stevens, T.H. See Ungermann. Fischer von Mollard, Jensen. Carson. and Carson. Margolis. Stevens, and Wickner. Sansonetti, PJ. See Beatty. Meresse. Gounon. Davoust, Mounier. Story, C.M. See Tortorella, Story, Huppa, Wiertz, Jones. Bacik, Sansonetti. and Gorvel. Bennink, Yewdell. and Ploegh. Sasaki, H. See Morita, Sasaki. Fujimoto. Furuse, and Tsukita. Straub, V. See Crosbie, Lebakken. Holt, Venzke. Straub. Lee, Grady. Satoh, A. See Takahashi, Nakanishi, Miyahara, Mandai, Satoh, Satoh. Chamberlain. Sanes. and Campbell. Nishioka. Aoki. Nomoto. Mizoguchi. and Takai. Su, W.-D. See Oohashi. Zhou. Feng. Richter, Morgelin. Perez, Su, Satoh. K. See Takahashi. Nakanishi. 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Left-right asymmetry and kinesin superfamily Serra, R., Karaplis, and Sohn, P. Parathyroid hormone-related protein K1F3A: New insights in determination of laterality and peptide (PTHrP)-dependent and -independent effects of trans¬ mesoderm induction by ki/3A mice analysis. 825. forming growth factor p (TGF-P) on endochondral bone forma¬ Takei, Y. See Terada. Tsujimoto, Takei, Takahashi. and Hirokawa. tion. 783. Takeichi, M. See Aono. Nakagawa. Reynolds, and Takeichi. Sheets, E.D., Holowka, I)., and Baird, B. Critical role for cholesterol Tanaka, Y. See Takeda, Yonekawa, Tanaka. Okada, Nonaka, and in Lyn-mediated tyrosine phosphorylation of FCeRl and their Hirokawa. association with detergent-resistant membranes. 877. Tanner, W. See Sanders. Gentzsch. Tanner, and Herskowitz. Author hide.x 1531 Taooka, Chen, J., Yednock, T,, and Sheppard, D, The integrin Voos, W, See Merlin. Voos, Maarse, Meijer, Planner, and Rassow. a9pi mediates adhesion to activated endothelial cells and Vourc’h, C. 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Wojciak-Stothard, B., Williams, L., and Ridley, A J. Monocyte adhe¬ — See Yonemura, Tsukita, and Tsukita. sion and spreading on human endothelial cells is dependent on Tuma, P.L., Finnegan, C,M., Yi, and Hubbard, A.L. Evidence Rho-regulated receptor clustering. 1293. for apical endocytosis in polarized hepatic cells; Phosphoinosi- Wolf, D.H. See Madeo, Frbhlich, Ligr, Grey, Sigrist, Wolf, and tide 3-kinase inhibitors lead to the lysosomal accumulation of Frohlich. resident apical plasma membrane proteins. 1089. Wolf, R.M. See Osterhout, Wolven, Wolf, Resh, and Chao. Tumbar, T,, Sudlow, G„ and Belmont, A.S. Large-scale chromatin Wolven, A. See Osterhout, Wolven, Wolf, Resh. and Chao. unfolding and remodeling induced by VP16 acidic activation do¬ Wong, E. See Meeusen, Tieu. Wong, Weiss. Schieltz, Yates, and main. 1341. Nunnari. Turner, C.E,, Brown, M.C,, Perrotta, J.A., Riedy, M.C,, Nikolopoulos, Woods, L.M., Hodges, C.A., Baart. E., Baker, S.M., Liskay, M., and S.N,, McDonald, A.R., Bagrodia, S., Thomas, S., and Leventhal, Hunt, P.A. Chromosomal influence on meiotic spindle assem¬ P.S, Paxillin LD4 motif binds PAK and PIX through a novel 95- bly: Abnormal meiosis I in female Mlhl mutant mice. 1395. kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal Wright, M.O. See Millward-Sadler, Wright, Lee, Nishida, Caldwell, remodeling. 851. Correction. 1523. Nuki. and Salter. U X Ungermann, C,, Fischer von Mollard, G., Jensen, O.N., Margolis, N., Xie, H. See Peng. Xie, Rossi, and Rotundo. Stevens, T.H., and Wickner, W. Three v-SNAREs and two t-SNAREs. present in a pentameric cis-SNARE complex on iso¬ lated vacuoles, are essential for homotypic fusion. 1435. Y Yaffe, M.P, See Fisk and Yaffe. V Yamaguchi, R„ Nakamura, M„ Mochizuki, N„ Kay, S.A„ and Nagatani, A. Light-dependent translocation of a phytochrome B-GFP fu¬ Van, G, See Burgess. Qian, Kaufman, Ring, Van, Capparelli, Kelley, sion protein to the nucleus in transgenic Arabidopsis. 437. Hsu, Boyle, Dunstan, Hu, and Lacey. Yamamoto, A., West, R.R., McIntosh, J.R., and Hiraoka, Y. A cyto¬ Van Criekinge, W. See Heyninck, De Vaick, Vanden Berghe, Van plasmic dynein heavy chain is required for oscillatory nuclear Criekinge, Contreras, Fiers. Haegeman, and Beyaert. movement of meiotic prophase and efficient meiotic recombina¬ Vanden Berghe, W. See Heyninck, De Vaick, Vanden Berghe, Van tion in fission yeast. 1233. Criekinge, Contreras, Fiers, Haegeman, and Beyaert. Yanagisawa, M. See Tripiciano, Peluso, Morena, Palombi, Stefanini, van Deursen, J.M.A. See Pritchard, Fornerod. Kasper, and van Ziparo, Yanagisawa, and Fiiippini. Deursen. Yao, Y. See Lin, Yao, Hofmeister, Tsien, and Farquhar. van’t Hof, W,, and Resh, M.D. Dual fatty acylation of p59’'>" is re¬ Yates, J.R. See Meeusen, Tieu, Wong, Weiss, Schieltz, Yates, and quired for association with the T cell receptor ^ chain through Nunnari. phosphotyrosine-Src homology domain-2 interactions. 377. Yeakley, J.M., Tronchere, H., Olesen, J., Dyck, J.A., Wang, H.-Y,, Venzke, D.P, See Crosbie, Lebakken, Holt, Venzke, Straub, Lee, and Fu, X.-D. Phosphorylation regulates in vivo interaction and Grady, Chamberlain, Sanes, and Campbell. molecular targeting of serine/arginine-rich pre-mRNA splicing Vlachou, A. See Kann, Sodeik, Vlachou, Gerlich, and Helenius. factors. 447. The Journal of Cell Biology, Volume 145, 1999 1532 Yednock. T. See Taooka. Chen. Yednock. and Sheppard. Zatloukal, K. See Eferl, Sibilia. Hilberg, Fuchsbichler, Kufferath, Yewdell, J.W. See Tortorella. Story, Huppa. Wiertz, Jones. Bacik, Guertl, Zenz, Wagner, and Zatloukal. Bennink. Yewdell. and Ploegh. Zeidman, R., Lofgren, B., Pahiman, S., and Larsson. C. PKCe. via its Yi, J.-H. See Tuma. Finnegan, Yi. and Hubbard. regulatory domain and independently of its catalytic domain, in¬ Yonekawa, Y. See Takeda. Yonekawa, Tanaka, Okada. Nonaka. and duces neurite-like processes in neuroblastoma cells. 713. Hirokawa. Zeng, L. See Fagotto, Jho, Zeng, Kurth, Joos, Kaufmann, and Yonemura, S., Tsukita, S., and Tsukita, S. Direct involvement of Constantini. ezrin/radixin/moesin (ERM)-binding membrane proteins in the Zenz, R. See Eferl, Sibilia. Hilberg, Fuchsbichler, Kufferath. Guertl, organization of microvilli in collaboration with activated ERM Zenz. Wagner, and Zatloukal. proteins. 1497. Zhang, J„ Reedy, M.C., Hannun, Y.A., and Obeid, L.M. Inhibition of Yu, H.-G., Muszynski, M.G., and Dawe, R.K. The maize homologue caspases inhibits the release of apoptotic bodies: Bcl-2 inhibits of the cell cycle checkpoint protein MAD2 reveals kinetochore the initiation of formation of apoptotic bodies in chemothera¬ substructure and contrasting mitotic and meiotic localization peutic agent-induced apoptosis. 99. patterns. 425. Zhou, X.-H. See Oohashi, Zhou. Feng, Richter, Morgelin. Perez, Su. Yu, VV. See Ahmad. Yu, McNally, and Baas. Chiquet-Ehrismann, Rauch, and Fassler. Yurchenco, P.D. See Colognato, Winkelmann. and Yurchenco. Ziparo, E. See Tripiciano, Peluso. Morena, Palombi, Stefanini, Ziparo. Yanagisawa. and Filippini. Zorzi, N. See Luetterforst. Stang. Zorzi. Carozzi. Way, and Parton. Zucker, R.S. See Lau, Zucker, and Bentley. Z Zuo, F.-R. See Bistrup. Bhakta. Lee. Belov, Gunn, Zuo. Huang, Kannagi, Rosen, and Hemmerich. ZafTran. S. See Fremion. Astier, Zaffran, Guillen. Homburger, and Zusman, S. See Martin. Zusman, Li, Williams, Khare, DaRocha. Semeriva. Chiquet-Ehrismann. and Baumgartner. Author Index 1533