메뉴 건너뛰기




Volumn 113, Issue 4, 2000, Pages 571-585

Polarization of cell growth in yeast. II. The role of the cortical actin cytoskeleton

Author keywords

Actin; Endocytosis; Myosin; Polarity; Secretion; Yeast

Indexed keywords

ACTIN; MESSENGER RNA; MYOSIN;

EID: 0034056057     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Note
Times cited : (412)

References (232)
  • 1
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud-growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae
    • Adams, A. and Pringle, J. (1984). Relationship of actin and tubulin distribution to bud-growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae. J. Cell Biol. 98, 934-945.
    • (1984) J. Cell Biol. , vol.98 , pp. 934-945
    • Adams, A.1    Pringle, J.2
  • 2
    • 0025294640 scopus 로고
    • CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae
    • Adams, A., Johnson, D., Longnecker, R., Sloat, B. and Pringle, J. (1990). CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. J. Cell Biol. 111, 131-142.
    • (1990) J. Cell Biol. , vol.111 , pp. 131-142
    • Adams, A.1    Johnson, D.2    Longnecker, R.3    Sloat, B.4    Pringle, J.5
  • 3
    • 0025983823 scopus 로고
    • Requirement of yeast fimbrin for actin organization and morphogenesis in vivo
    • Adams, A., Botstein, D. and Drubin, D. (1991). Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature 354, 404-408.
    • (1991) Nature , vol.354 , pp. 404-408
    • Adams, A.1    Botstein, D.2    Drubin, D.3
  • 4
    • 0028917764 scopus 로고
    • Isoform-specific complementation of the yeast sac6 null mutation by human fimbrin
    • Adams, A., Shen, W., Lin, C., Leavitt, J. and Matsudaira, P. (1995). Isoform-specific complementation of the yeast sac6 null mutation by human fimbrin. Mol. Cell. Biol. 15, 69-75.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 69-75
    • Adams, A.1    Shen, W.2    Lin, C.3    Leavitt, J.4    Matsudaira, P.5
  • 5
    • 0025344531 scopus 로고
    • Disruption of the actin cytoskeleton in yeast capping protein mutants
    • Amatruda, J., Cannon, J., Tatchell, K., Hug, C. and Cooper, J. (1990). Disruption of the actin cytoskeleton in yeast capping protein mutants. Nature 344, 352-354.
    • (1990) Nature , vol.344 , pp. 352-354
    • Amatruda, J.1    Cannon, J.2    Tatchell, K.3    Hug, C.4    Cooper, J.5
  • 6
    • 0026686092 scopus 로고
    • Purification, characterization, and immunofluorescence localization of Saccharomyces cerevisiae capping protein
    • Amatruda, J. and Cooper, J. (1992). Purification, characterization, and immunofluorescence localization of Saccharomyces cerevisiae capping protein. J. Cell Biol. 117, 1067-1076.
    • (1992) J. Cell Biol. , vol.117 , pp. 1067-1076
    • Amatruda, J.1    Cooper, J.2
  • 7
    • 0026482118 scopus 로고
    • Effects of null mutations and overexpression of capping protein on morphogenesis, actin distribution and polarized secretion in yeast
    • Amatruda, J., Gattermeir, D., Karpova, T. and Cooper, J. (1992). Effects of null mutations and overexpression of capping protein on morphogenesis, actin distribution and polarized secretion in yeast. J. Cell Biol. 119, 1151-1162.
    • (1992) J. Cell Biol. , vol.119 , pp. 1151-1162
    • Amatruda, J.1    Gattermeir, D.2    Karpova, T.3    Cooper, J.4
  • 8
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • Amberg, D., Basart, E. and Botstein, D. (1995). Defining protein interactions with yeast actin in vivo. Nature Struct. Biol. 2, 28-35.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.1    Basart, E.2    Botstein, D.3
  • 9
    • 0030989560 scopus 로고    scopus 로고
    • Aip3p/Bud6p, a yeast actin-interacting protein that is involved in morphogenesis and the selection of bipolar budding sites
    • Amberg, D., Zahner, J., Mulholland, J., Pringle, J. and Botstein, D. (1997). Aip3p/Bud6p, a yeast actin-interacting protein that is involved in morphogenesis and the selection of bipolar budding sites. Mol. Biol. Cell. 8, 729-753.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 729-753
    • Amberg, D.1    Zahner, J.2    Mulholland, J.3    Pringle, J.4    Botstein, D.5
  • 10
    • 0031772419 scopus 로고    scopus 로고
    • Three-dimensional imaging of the yeast actin cytoskeleton through the budding cell cycle
    • Amberg, D. (1998). Three-dimensional imaging of the yeast actin cytoskeleton through the budding cell cycle. Mol. Biol. Cell. 9, 3259-3262.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 3259-3262
    • Amberg, D.1
  • 11
    • 0032526679 scopus 로고    scopus 로고
    • The src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization
    • Anderson, B., Boldogh, I., Evangelista, M., Boone, C., Greene, L. and Pon, L. (1998). The src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. J. Cell Biol. 141, 1357-1370.
    • (1998) J. Cell Biol. , vol.141 , pp. 1357-1370
    • Anderson, B.1    Boldogh, I.2    Evangelista, M.3    Boone, C.4    Greene, L.5    Pon, L.6
  • 12
    • 0030852841 scopus 로고    scopus 로고
    • A small conserved domain in the yeast Spa2p is necessary and sufficient for its polarized localization
    • Arkowitz, R. and Lowe, N. (1997). A small conserved domain in the yeast Spa2p is necessary and sufficient for its polarized localization. J. Cell Biol. 138, 17-36.
    • (1997) J. Cell Biol. , vol.138 , pp. 17-36
    • Arkowitz, R.1    Lowe, N.2
  • 13
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough, K., Stryker, J., Pokala, N., Sanders, M., Crews, P. and Drubin, D. (1997). High rates of actin turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 137, 399-416.
    • (1997) J. Cell Biol. , vol.137 , pp. 399-416
    • Ayscough, K.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.6
  • 14
    • 0032934806 scopus 로고    scopus 로고
    • Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rholp-GTPase and Sla2p, a protein with talin homology
    • Ayscough, K., Eby, J., Lila, T., Dewar, H., Kozminski, K. and Drubin, D. (1999). Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rholp-GTPase and Sla2p, a protein with talin homology. Mol. Biol. Cell. 10, 1061-1075.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 1061-1075
    • Ayscough, K.1    Eby, J.2    Lila, T.3    Dewar, H.4    Kozminski, K.5    Drubin, D.6
  • 15
    • 0032771075 scopus 로고    scopus 로고
    • Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches
    • Balguerie, A., Sivadon, P., Bonneu, M. and Aigle, M. (1999). Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches. J. Cell Sci. 112, 2529-2537.
    • (1999) J. Cell Sci. , vol.112 , pp. 2529-2537
    • Balguerie, A.1    Sivadon, P.2    Bonneu, M.3    Aigle, M.4
  • 16
    • 0033555685 scopus 로고    scopus 로고
    • Niml-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast
    • Barral, Y., Parra, M., Bidlingmaier, S. and Snyder, M. (1999). Niml-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast. Genes Dev. 13, 176-187.
    • (1999) Genes Dev. , vol.13 , pp. 176-187
    • Barral, Y.1    Parra, M.2    Bidlingmaier, S.3    Snyder, M.4
  • 17
    • 0027219273 scopus 로고
    • Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns
    • Bauer, F., Urdaci, M., Aigle, M. and Crouzet, M. (1993). Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns. Mol. Cell. Biol. 13, 5070-5084.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5070-5084
    • Bauer, F.1    Urdaci, M.2    Aigle, M.3    Crouzet, M.4
  • 18
    • 0033519623 scopus 로고    scopus 로고
    • Localization and anchoring of mRNA in budding yeast
    • Beach, D., Salmon, E. and Bloom, K. (1999). Localization and anchoring of mRNA in budding yeast. Curr. Biol. 9, 569-578.
    • (1999) Curr. Biol. , vol.9 , pp. 569-578
    • Beach, D.1    Salmon, E.2    Bloom, K.3
  • 19
    • 0032494082 scopus 로고    scopus 로고
    • The yeast V159N actin mutant reveals roles for actin dynamics in vivo
    • Belmont, L., and Drubin, D. (1998). The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol. 142, 1289-1299.
    • (1998) J. Cell Biol. , vol.142 , pp. 1289-1299
    • Belmont, L.1    Drubin, D.2
  • 20
    • 0025959707 scopus 로고
    • Use of a screen for synthetic lethal and multicopy suppressee mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae
    • Bender, A. and Pringle, J. (1991). Use of a screen for synthetic lethal and multicopy suppressee mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 11, 1295-1305.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1295-1305
    • Bender, A.1    Pringle, J.2
  • 21
    • 0028024386 scopus 로고
    • The END3 gene encodes a protein that is required for the internalization step of endocytosis and tor actin cytoskeleton organization in yeast
    • Bénédetti, H., Raths, S., Crausaz, F. and Riezman, H. (1994). The END3 gene encodes a protein that is required for the internalization step of endocytosis and tor actin cytoskeleton organization in yeast. Mol. Biol. Cell. 5, 1023-1037.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 1023-1037
    • Bénédetti, H.1    Raths, S.2    Crausaz, F.3    Riezman, H.4
  • 22
    • 0027444749 scopus 로고
    • Genetic analysis of Cln/Cdc28 regulation of cell morphogenesis in budding yeast
    • Benton, B., Tinklenberg, A., Jean, D., Plump, S. and Cross, F. (1993). Genetic analysis of Cln/Cdc28 regulation of cell morphogenesis in budding yeast. EMBO J. 12, 5267-5275.
    • (1993) EMBO J. , vol.12 , pp. 5267-5275
    • Benton, B.1    Tinklenberg, A.2    Jean, D.3    Plump, S.4    Cross, F.5
  • 23
    • 0032494183 scopus 로고    scopus 로고
    • Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis
    • Bi, E., Maddov, P., Lew, D., Salmon, E., McMillan, J., Yen, E. and Pringle, J. (1998). Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis. J. Cell Biol. 142, 1301-1312.
    • (1998) J. Cell Biol. , vol.142 , pp. 1301-1312
    • Bi, E.1    Maddov, P.2    Lew, D.3    Salmon, E.4    McMillan, J.5    Yen, E.6    Pringle, J.7
  • 24
    • 0029914986 scopus 로고    scopus 로고
    • Asymmetric accumulation of Ashlp in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells
    • Bobola, N., Jansen, R. P., Shin, T. and Nasmyth, K. (1996). Asymmetric accumulation of Ashlp in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells. Cell 84, 699-709.
    • (1996) Cell , vol.84 , pp. 699-709
    • Bobola, N.1    Jansen, R.P.2    Shin, T.3    Nasmyth, K.4
  • 25
    • 0032526412 scopus 로고    scopus 로고
    • Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p
    • Boldogh, I., Vojtov, N., Karmon, S. and Pon, L. (1998). Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p. J. Cell Biol. 141, 1371-1381.
    • (1998) J. Cell Biol. , vol.141 , pp. 1371-1381
    • Boldogh, I.1    Vojtov, N.2    Karmon, S.3    Pon, L.4
  • 27
    • 0027470208 scopus 로고
    • Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4
    • Brennwald, P. and Novick, P. (1993). Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4. Nature 360, 560-563.
    • (1993) Nature , vol.360 , pp. 560-563
    • Brennwald, P.1    Novick, P.2
  • 28
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • Brennwald, P., Kearns, B., Champion, K., Keränen, V. and Novick, P. (1994). Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell 79, 245-258.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keränen, V.4    Novick, P.5
  • 29
    • 0028107971 scopus 로고
    • What are the basic functions of microfilaments? Insights from studies in budding yeast
    • Bretscher, A., Drees, B., Harsay, E., Schott, D. and Wang, T. (1994). What are the basic functions of microfilaments? Insights from studies in budding yeast. J. Cell Biol. 126, 821-825.
    • (1994) J. Cell Biol. , vol.126 , pp. 821-825
    • Bretscher, A.1    Drees, B.2    Harsay, E.3    Schott, D.4    Wang, T.5
  • 30
    • 0027531645 scopus 로고
    • An osmosensing signal transduction pathway in yeast
    • Brewster, J., de Valoir, T., Dwyer, N., Winter, E. and Gustin, M. (1993). An osmosensing signal transduction pathway in yeast. Science 259, 1760-1763.
    • (1993) Science , vol.259 , pp. 1760-1763
    • Brewster, J.1    De Valoir, T.2    Dwyer, N.3    Winter, E.4    Gustin, M.5
  • 31
    • 0028333962 scopus 로고
    • Positioning of cell growth and division after osmotic stress requires a MAP kinase pathway
    • Brewster, J. and Gustin, M. (1994). Positioning of cell growth and division after osmotic stress requires a MAP kinase pathway. Yeast 10, 425-439.
    • (1994) Yeast , vol.10 , pp. 425-439
    • Brewster, J.1    Gustin, M.2
  • 32
    • 0032482228 scopus 로고    scopus 로고
    • Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae
    • Brizzio, V., Gammie, A. and Rose, M. (1998). Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae. J. Cell Biol. 141, 567-584.
    • (1998) J. Cell Biol. , vol.141 , pp. 567-584
    • Brizzio, V.1    Gammie, A.2    Rose, M.3
  • 33
    • 0026637084 scopus 로고
    • Calmodulin concentrates at regions of cell growth in Saccharomyces cerevisiae
    • Brockerhoff, S. and Davis, T. (1992). Calmodulin concentrates at regions of cell growth in Saccharomyces cerevisiae. J. Cell Biol. 118, 619-629.
    • (1992) J. Cell Biol. , vol.118 , pp. 619-629
    • Brockerhoff, S.1    Davis, T.2
  • 35
    • 0030715361 scopus 로고    scopus 로고
    • Novel Cdc42-binding proteins Gic1 and Gic2 control cell polarity in yeast
    • Brown, J., Jaquenoud, M., Gulli, M. P., Chant, J. and Peter, M. (1997). Novel Cdc42-binding proteins Gic1 and Gic2 control cell polarity in yeast. Genes Dev. 11, 2972-2982.
    • (1997) Genes Dev. , vol.11 , pp. 2972-2982
    • Brown, J.1    Jaquenoud, M.2    Gulli, M.P.3    Chant, J.4    Peter, M.5
  • 36
    • 0033280225 scopus 로고    scopus 로고
    • Cooperation between microtubule- and actin-based motor proteins
    • Brown, S. (1999). Cooperation between microtubule- and actin-based motor proteins. Annu. Rev. Cell Dev. Biol. 15, 63-80.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 63-80
    • Brown, S.1
  • 37
    • 0026519160 scopus 로고
    • CSD2, CSD3, and CSD4, genes required for chitin synthesis in Saccharomyces cerevisiae: The CSD2 gene product is related to chitin synthases and to developmentally regulated proteins in Rhizobium species and Xenopus laevis
    • Bulawa, C. (1992). CSD2, CSD3, and CSD4, genes required for chitin synthesis in Saccharomyces cerevisiae: the CSD2 gene product is related to chitin synthases and to developmentally regulated proteins in Rhizobium species and Xenopus laevis. Mol. Cell. Biol. 12, 1764-1776.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1764-1776
    • Bulawa, C.1
  • 38
    • 0033606766 scopus 로고    scopus 로고
    • Sec1p binds to SNARE complexes and concentrates at sites of secretion
    • Carr, C., Grote, E., Munson, M., Hughson, F. and Novick, P. (1999). Sec1p binds to SNARE complexes and concentrates at sites of secretion. J. Cell Biol. 146, 333-344.
    • (1999) J. Cell Biol. , vol.146 , pp. 333-344
    • Carr, C.1    Grote, E.2    Munson, M.3    Hughson, F.4    Novick, P.5
  • 39
    • 0032426664 scopus 로고    scopus 로고
    • The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth
    • Catlett, N. and Weisman, L. (1998). The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth. Proc. Nat. Acad. Sci. USA 95, 14799-14804.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 14799-14804
    • Catlett, N.1    Weisman, L.2
  • 40
    • 0031945611 scopus 로고    scopus 로고
    • Ash1, a daughter cell-specific protein, is required for pseudohyphal growth of Saccharomyces cerevisiae
    • Chandarlapaty, S. and Errede, B. (1998). Ash1, a daughter cell-specific protein, is required for pseudohyphal growth of Saccharomyces cerevisiae. Mol. Cell. Biol. 18, 2884-2891.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2884-2891
    • Chandarlapaty, S.1    Errede, B.2
  • 41
    • 0025814609 scopus 로고
    • Genetic control of bud site selection in yeast by a set of gene products that constitute a morphogenetic pathway
    • Chant, J. and Herskowitz, I. (1991). Genetic control of bud site selection in yeast by a set of gene products that constitute a morphogenetic pathway. Cell 65, 1203-1212.
    • (1991) Cell , vol.65 , pp. 1203-1212
    • Chant, J.1    Herskowitz, I.2
  • 42
    • 0028931727 scopus 로고
    • Patterns of bud-site selection in the yeast Saccharomyces cerevisiae
    • Chant, J. and Pringle, J. (1995). Patterns of bud-site selection in the yeast Saccharomyces cerevisiae. J. Cell Biol. 129, 751-765.
    • (1995) J. Cell Biol. , vol.129 , pp. 751-765
    • Chant, J.1    Pringle, J.2
  • 44
    • 0033279824 scopus 로고    scopus 로고
    • Cell polarity in yeast
    • Chant, J. (1999). Cell Polarity in yeast. Annu. Rev. Cell Dev. Biol. 15, 365-391.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 365-391
    • Chant, J.1
  • 45
    • 0025200302 scopus 로고
    • Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line
    • Chavrier, P., Vingron, M., Sander, C., Simons, K. and Zerial, M. (1990). Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line. Mol. Biol. Cell 10, 6578-6585.
    • (1990) Mol. Biol. Cell , vol.10 , pp. 6578-6585
    • Chavrier, P.1    Vingron, M.2    Sander, C.3    Simons, K.4    Zerial, M.5
  • 46
    • 0030705142 scopus 로고    scopus 로고
    • The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for polarized cell growth in Saccharomyces cerevisiae
    • Chen, G. C., Kim, Y. J. and Clarence, C. (1997). The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for polarized cell growth in Saccharomyces cerevisiae. Genes Dev. 11, 2958-2971.
    • (1997) Genes Dev. , vol.11 , pp. 2958-2971
    • Chen, G.C.1    Kim, Y.J.2    Clarence, C.3
  • 47
    • 0026586631 scopus 로고
    • A yeast gene (BEMI) necessary for cell polarization whose product contains two SH3 domains
    • Chenevert, J., Corrado, K., Bender, A., Pringle, J. and Herskowitz, I. (1992). A yeast gene (BEMI) necessary for cell polarization whose product contains two SH3 domains. Nature 356, 77-79.
    • (1992) Nature , vol.356 , pp. 77-79
    • Chenevert, J.1    Corrado, K.2    Bender, A.3    Pringle, J.4    Herskowitz, I.5
  • 48
    • 0029844403 scopus 로고    scopus 로고
    • Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p
    • Chuang, J. and Schekman, R. (1996). Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p. J. Cell Biol. 135, 597-610.
    • (1996) J. Cell Biol. , vol.135 , pp. 597-610
    • Chuang, J.1    Schekman, R.2
  • 49
    • 0029094218 scopus 로고
    • Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiae
    • Cid, V., Duran, A., del Rey, F., Snyder, M., Nombela, C. and Sanchez, M. (1995). Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiae. Microbiol. Rev. 59, 345-386.
    • (1995) Microbiol. Rev. , vol.59 , pp. 345-386
    • Cid, V.1    Duran, A.2    Del Rey, F.3    Snyder, M.4    Nombela, C.5    Sanchez, M.6
  • 50
    • 0032798051 scopus 로고    scopus 로고
    • Vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions
    • Colwill, K., Field, D., Moore, L., Friesen, J. and Andrews, B. (1999). In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions. Genetics 152, 881-893.
    • (1999) Genetics , vol.152 , pp. 881-893
    • Colwill, K.1    Field, D.2    Moore, L.3    Friesen, J.4    Andrews, B.5
  • 51
    • 0033594087 scopus 로고    scopus 로고
    • Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast
    • Cope, M. J., Yang, S., Shang, C. and Drubin, D. (1999). Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast. J. Cell Biol. 144, 1203-1218.
    • (1999) J. Cell Biol. , vol.144 , pp. 1203-1218
    • Cope, M.J.1    Yang, S.2    Shang, C.3    Drubin, D.4
  • 52
    • 0025989149 scopus 로고
    • Yeast mutant affected for viability upon nutrient starvation: Characterization and cloning of the RVS161 gene
    • Crouzet, M., Urdaci, M., Dulau, L. and Aigle, M. (1991). Yeast mutant affected for viability upon nutrient starvation: characterization and cloning of the RVS161 gene. Yeast 7, 727-743.
    • (1991) Yeast , vol.7 , pp. 727-743
    • Crouzet, M.1    Urdaci, M.2    Dulau, L.3    Aigle, M.4
  • 53
    • 0029091498 scopus 로고
    • Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast
    • Cvreková, F., De Virgilio, C., Manser, E., Pringle, J. and Nasmyth, K. (1995). Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast. Genes Dev. 9, 1817-1830.
    • (1995) Genes Dev. , vol.9 , pp. 1817-1830
    • Cvreková, F.1    De Virgilio, C.2    Manser, E.3    Pringle, J.4    Nasmyth, K.5
  • 54
    • 0024313794 scopus 로고
    • Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable
    • Davis, T. and Thorner, J. (1989). Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable. Proc. Nat. Acad. Sci. USA 86, 7909-7913.
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 7909-7913
    • Davis, T.1    Thorner, J.2
  • 55
    • 0033523764 scopus 로고    scopus 로고
    • Cell wall stress depolarizes cell growth via hyperactivation of RHO1
    • Delley, P. A. and Hall, M. (1999). Cell wall stress depolarizes cell growth via hyperactivation of RHO1. J. Cell Biol. 147, 163-174.
    • (1999) J. Cell Biol. , vol.147 , pp. 163-174
    • Delley, P.A.1    Hall, M.2
  • 56
    • 0030763146 scopus 로고    scopus 로고
    • A septin-based hierarchy of proteins required for localized deposition of chitin in the Saccharomyces cerevisiae cell wall
    • DeMarini, D., Adams, A., Fares, H., De Virgilio, C., Valle, G., Chuang, J. and Pringle, J. (1997). A septin-based hierarchy of proteins required for localized deposition of chitin in the Saccharomyces cerevisiae cell wall. J. Cell Biol. 139, 75-93.
    • (1997) J. Cell Biol. , vol.139 , pp. 75-93
    • DeMarini, D.1    Adams, A.2    Fares, H.3    De Virgilio, C.4    Valle, G.5    Chuang, J.6    Pringle, J.7
  • 57
    • 0029966290 scopus 로고    scopus 로고
    • Movement of yeast cortical actin cytoskeleton visualized in vivo
    • Doyle, T. and Botstein, D. (1996). Movement of yeast cortical actin cytoskeleton visualized in vivo. Proc. Nat. Acad. Sci. USA 93, 3886-3891.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 3886-3891
    • Doyle, T.1    Botstein, D.2
  • 58
    • 0028954614 scopus 로고
    • Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions
    • Drees, B., Brown, C., Barrel, B. and Bretscher, A. (1995). Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions. J. Cell Biol. 128, 383-392.
    • (1995) J. Cell Biol. , vol.128 , pp. 383-392
    • Drees, B.1    Brown, C.2    Barrel, B.3    Bretscher, A.4
  • 59
    • 0033606798 scopus 로고    scopus 로고
    • The GTP-binding protein Rho1p is required for cell cycle progression and polarization of the yeast cell
    • Drgonová, J., Drgon, T., Roh, D. H. and Cabib, E. (1999). The GTP-binding protein Rho1p is required for cell cycle progression and polarization of the yeast cell. J. Cell Biol. 146, 373-387.
    • (1999) J. Cell Biol. , vol.146 , pp. 373-387
    • Drgonová, J.1    Drgon, T.2    Roh, D.H.3    Cabib, E.4
  • 60
    • 0024192883 scopus 로고
    • Yeast actin-binding proteins: Evidence fora role in morphogenesis
    • Drubin, D., Miller, K. and Botstein, D. (1988). Yeast actin-binding proteins: evidence fora role in morphogenesis. J. Cell Biol. 107, 2551-2561.
    • (1988) J. Cell Biol. , vol.107 , pp. 2551-2561
    • Drubin, D.1    Miller, K.2    Botstein, D.3
  • 61
    • 0025022491 scopus 로고
    • Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I
    • Drubin, D., Mulholland, J., Zhu, Z. and Botstein, D. (1990). Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I. Nature 343, 288-290.
    • (1990) Nature , vol.343 , pp. 288-290
    • Drubin, D.1    Mulholland, J.2    Zhu, Z.3    Botstein, D.4
  • 62
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D. and Nelson, W. J. (1996). Origins of cell polarity. Cell 84, 335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.1    Nelson, W.J.2
  • 63
    • 0032572702 scopus 로고    scopus 로고
    • Actin cytoskeleton organization regulated by the PAK family of protein kinases
    • Eby, J., Holly, S., van Drogan, F., Grishin, A., Peter, M., Drubin, D. and Blumer, K. (1998). Actin cytoskeleton organization regulated by the PAK family of protein kinases. Curr. Biol. 8, 967-970.
    • (1998) Curr. Biol. , vol.8 , pp. 967-970
    • Eby, J.1    Holly, S.2    Van Drogan, F.3    Grishin, A.4    Peter, M.5    Drubin, D.6    Blumer, K.7
  • 64
    • 0031444358 scopus 로고    scopus 로고
    • An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast
    • Epp, J. and Chant, J. (1997). An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast. Curr. Biol. 7, 921-929.
    • (1997) Curr. Biol. , vol.7 , pp. 921-929
    • Epp, J.1    Chant, J.2
  • 65
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista, M., Blundell, K., Longtine, M., Chow, C., Adames, N., Pringle, J., Peter, M. and Boone, C. (1997). Bni1p, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276, 118-121.
    • (1997) Science , vol.276 , pp. 118-121
    • Evangelista, M.1    Blundell, K.2    Longtine, M.3    Chow, C.4    Adames, N.5    Pringle, J.6    Peter, M.7    Boone, C.8
  • 66
    • 0032189837 scopus 로고    scopus 로고
    • Regulated nucleo/cytoplasmic exchange of HOG1 MAPK requires the importin β homologs NMD5 and XPO1
    • Ferrigno, P., Posas, F., Koepp, D., Saito, H. and Silver, P. (1998). Regulated nucleo/cytoplasmic exchange of HOG1 MAPK requires the importin β homologs NMD5 and XPO1. EMBO J. 17, 5606-5614.
    • (1998) EMBO J. , vol.17 , pp. 5606-5614
    • Ferrigno, P.1    Posas, F.2    Koepp, D.3    Saito, H.4    Silver, P.5
  • 67
    • 0033006993 scopus 로고    scopus 로고
    • Cytokinesis in eukaryotes: A mechanistic comparison
    • Field, C., Li, R. and Oegema, K. (1999). Cytokinesis in eukaryotes: a mechanistic comparison. Curr. Opin. Cell Biol. 11, 68-80.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 68-80
    • Field, C.1    Li, R.2    Oegema, K.3
  • 68
    • 0030898133 scopus 로고    scopus 로고
    • Sec3p is involved in secretion and morphogenesis in Saccharomyces cerevisiae
    • Finger, F. and Novick, P. (1997). Sec3p is involved in secretion and morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell. 8, 647-662.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 647-662
    • Finger, F.1    Novick, P.2
  • 69
    • 0031852067 scopus 로고    scopus 로고
    • Spatial regulation of exocytosis: Lessons from yeast
    • Finger, F. and Novick, P. (1998). Spatial regulation of exocytosis: lessons from yeast. J. Cell Biol. 142, 609-612.
    • (1998) J. Cell Biol. , vol.142 , pp. 609-612
    • Finger, F.1    Novick, P.2
  • 70
    • 0032548828 scopus 로고    scopus 로고
    • Sec3p is a spatial landmark for polarized secretion in budding yeast
    • Finger, F., Hughes, T. and Novick, P. (1998). Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 92, 559-571.
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.1    Hughes, T.2    Novick, P.3
  • 71
    • 0027219199 scopus 로고
    • Components required for cytokinesis are important for bud site selection in yeast
    • Flescher, E., Madden, K. and Snyder, M. (1993). Components required for cytokinesis are important for bud site selection in yeast. J. Cell Biol. 122, 373-386.
    • (1993) J. Cell Biol. , vol.122 , pp. 373-386
    • Flescher, E.1    Madden, K.2    Snyder, M.3
  • 72
    • 0026315451 scopus 로고
    • Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: Localization of the CDC11 gene product and the timing of events at the budding site
    • Ford, S. and Pringle, J. (1991). Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC11 gene product and the timing of events at the budding site. Dev. Genet. 12, 281-292.
    • (1991) Dev. Genet. , vol.12 , pp. 281-292
    • Ford, S.1    Pringle, J.2
  • 73
    • 0028920045 scopus 로고
    • An actin-monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein
    • Freeman, N., Chen, Z., Horenstein, J., Weber, A. and Field, J. (1995). An actin-monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein. J. Biol. Chem. 270, 5680-5685.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5680-5685
    • Freeman, N.1    Chen, Z.2    Horenstein, J.3    Weber, A.4    Field, J.5
  • 74
    • 0030048768 scopus 로고    scopus 로고
    • A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization
    • Freeman, N., Lila, T., Mintzer, K., Chen, Z., Pahk, A., Ren, R., Drubin, D. and Field, J. (1996). A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization. Mol. Cell. Biol. 16, 548-556.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 548-556
    • Freeman, N.1    Lila, T.2    Mintzer, K.3    Chen, Z.4    Pahk, A.5    Ren, R.6    Drubin, D.7    Field, J.8
  • 75
  • 76
    • 0025184193 scopus 로고
    • The SPA2 gene of Saccharomyces cerevisiae is important for pheromone-induced morphogenesis and efficient mating
    • Gehrung, S. and Snyder, M. (1990). The SPA2 gene of Saccharomyces cerevisiae is important for pheromone-induced morphogenesis and efficient mating. J. Cell Biol. 111, 1451-1464.
    • (1990) J. Cell Biol. , vol.111 , pp. 1451-1464
    • Gehrung, S.1    Snyder, M.2
  • 77
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli, M. I., and Riezman, H. (1996). Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272, 533-535.
    • (1996) Science , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 78
    • 0031980575 scopus 로고    scopus 로고
    • Endocytic internalization in yeast and animal cells: Similar and different
    • Geli, M. I. and Riezman, H. (1998). Endocytic internalization in yeast and animal cells: similar and different. J. Cell Sci. 111, 1031-1037.
    • (1998) J. Cell Sci. , vol.111 , pp. 1031-1037
    • Geli, M.I.1    Riezman, H.2
  • 79
    • 0032472908 scopus 로고    scopus 로고
    • Distinct functions of calmodulin are required for the uptake of receptor-mediated endocytosis in yeast: The type I myosin Myo5p is one of the calmodulin targets
    • Geli, M. I., Wesp, A. and Riezman, H. (1998). Distinct functions of calmodulin are required for the uptake of receptor-mediated endocytosis in yeast: the type I myosin Myo5p is one of the calmodulin targets. EMBO J. 17, 635-647.
    • (1998) EMBO J. , vol.17 , pp. 635-647
    • Geli, M.I.1    Wesp, A.2    Riezman, H.3
  • 80
    • 0026081344 scopus 로고
    • CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex
    • Gerst, J., Ferguson, K., Vojtek, A., Wigler, M. and Field, J. (1991). CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex. Mol. Biol. Cell. 11, 1248-1257.
    • (1991) Mol. Biol. Cell. , vol.11 , pp. 1248-1257
    • Gerst, J.1    Ferguson, K.2    Vojtek, A.3    Wigler, M.4    Field, J.5
  • 81
    • 0033602476 scopus 로고    scopus 로고
    • ASH1 mRNA localization in yeast involves multiple secondary structural elements and Ash1 protein translation
    • Gonzalez, I., Buonomo, S., Nasmyth, K. and von Ahsen, U. (1999). ASH1 mRNA localization in yeast involves multiple secondary structural elements and Ash1 protein translation. Curr. Biol. 9, 337-340.
    • (1999) Curr. Biol. , vol.9 , pp. 337-340
    • Gonzalez, I.1    Buonomo, S.2    Nasmyth, K.3    Von Ahsen, U.4
  • 82
    • 0031828002 scopus 로고    scopus 로고
    • Regulation of the cortical actin cytoskeleton in budding yeast by twinflin, a ubiquitous actin monomer-sequestering protein
    • Goode, B., Drubin, D. and Lappalainen, P. (1998). Regulation of the cortical actin cytoskeleton in budding yeast by twinflin, a ubiquitous actin monomer-sequestering protein. J. Cell Biol. 142, 723-733.
    • (1998) J. Cell Biol. , vol.142 , pp. 723-733
    • Goode, B.1    Drubin, D.2    Lappalainen, P.3
  • 83
    • 0033545203 scopus 로고    scopus 로고
    • Coronin promotes the rapid assembly and cross-linking of actin filaments and may link the actin and microtubule cytoskeleton in yeast
    • Goode, B., Wong, J., Butty, A. C., Peter, M., McCormack, A., Yates, J., Drubin, D. and Barnes, G. (1999). Coronin promotes the rapid assembly and cross-linking of actin filaments and may link the actin and microtubule cytoskeleton in yeast. J. Cell Biol. 144, 83-98.
    • (1999) J. Cell Biol. , vol.144 , pp. 83-98
    • Goode, B.1    Wong, J.2    Butty, A.C.3    Peter, M.4    McCormack, A.5    Yates, J.6    Drubin, D.7    Barnes, G.8
  • 84
    • 0029984773 scopus 로고    scopus 로고
    • Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton
    • Goodson, H., Anderson, B., Warrick, H., Pon, L. and Spudich., J. (1996). Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J. Cell Biol. 133, 1277-1291.
    • (1996) J. Cell Biol. , vol.133 , pp. 1277-1291
    • Goodson, H.1    Anderson, B.2    Warrick, H.3    Pon, L.4    Spudich, J.5
  • 85
    • 0028902506 scopus 로고
    • The role of Myo2p, a yeast class V myosin, in vesicular transport
    • Govindan, B., Bowser, R. and Novick, P. (1995). The role of Myo2p, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128, 1055-1068.
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 86
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo, W., Roth, D., Walch-Solimena, C. and Novick, P. (1999a). The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J. 18, 1071-1080.
    • (1999) EMBO J. , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 87
    • 0033551705 scopus 로고    scopus 로고
    • Exo84p is an exocyst protein essential for secretion
    • Guo, W., Grant, A. and Novick, P. (1999b). Exo84p is an exocyst protein essential for secretion. J. Biol. Chem. 274, 23558-23564.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23558-23564
    • Guo, W.1    Grant, A.2    Novick, P.3
  • 88
    • 0023429491 scopus 로고
    • Immunofluorescence localization of the Saccharomyces cerevisiae CDC12 gene product to the vicinity of the 10-nm filaments in the mother-bud neck
    • Haarer, B. and Pringle, J. (1987). Immunofluorescence localization of the Saccharomyces cerevisiae CDC12 gene product to the vicinity of the 10-nm filaments in the mother-bud neck. Mol. Cell. Biol. 7, 3678-3687.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3678-3687
    • Haarer, B.1    Pringle, J.2
  • 89
    • 0025008805 scopus 로고
    • Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells
    • Haarer, B., Lillie, S., Adams, A., Magdolen, V., Bandlow, W. and Brown, S. (1990). Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells. J. Cell Biol. 110, 105-114.
    • (1990) J. Cell Biol. , vol.110 , pp. 105-114
    • Haarer, B.1    Lillie, S.2    Adams, A.3    Magdolen, V.4    Bandlow, W.5    Brown, S.6
  • 90
    • 0028216280 scopus 로고
    • Identification of MYO4, a second class V myosin gene in yeast
    • Haarer, B., Petzold, A., Lillie, S. and Brown, S. (1994). Identification of MYO4, a second class V myosin gene in yeast. J. Cell Sci. 107, 1055-1064.
    • (1994) J. Cell Sci. , vol.107 , pp. 1055-1064
    • Haarer, B.1    Petzold, A.2    Lillie, S.3    Brown, S.4
  • 91
    • 0029816421 scopus 로고    scopus 로고
    • SEC3 mutations are synthetically lethal with profilin mutations and cause defects in diploid-specific bud-site selection
    • Haarer, B., Corbett, A., Kweon, Y., Petzold, A., Silver, P. and Brown, S. (1996). SEC3 mutations are synthetically lethal with profilin mutations and cause defects in diploid-specific bud-site selection. Genetics 144, 495-510.
    • (1996) Genetics , vol.144 , pp. 495-510
    • Haarer, B.1    Corbett, A.2    Kweon, Y.3    Petzold, A.4    Silver, P.5    Brown, S.6
  • 92
    • 0028787438 scopus 로고
    • Parallel secretory pathways to the cell surface in yeast
    • Harsay, E. and Bretscher, A. (1995). Parallel secretory pathways to the cell surface in yeast. J. Cell Biol. 131, 297-310.
    • (1995) J. Cell Biol. , vol.131 , pp. 297-310
    • Harsay, E.1    Bretscher, A.2
  • 93
    • 4243665946 scopus 로고    scopus 로고
    • A subset of secretory cargo in yeast transits an endosomal compartment prior to exocytosis
    • Harsay, E. and Schekman, R. (1998). A subset of secretory cargo in yeast transits an endosomal compartment prior to exocytosis. Mol. Biol. Cell. 9, 208a.
    • (1998) Mol. Biol. Cell. , vol.9
    • Harsay, E.1    Schekman, R.2
  • 94
    • 0015193588 scopus 로고
    • Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis
    • Hartwell, L. (1971). Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp. Cell Res 69, 265-276.
    • (1971) Exp. Cell Res , vol.69 , pp. 265-276
    • Hartwell, L.1
  • 95
    • 0015954720 scopus 로고
    • Genetic control of the cell division cycle in yeast
    • Hartwell, L., Culotti, J., Pringle, J. and Reid, B. (1974). Genetic control of the cell division cycle in yeast. Science 183, 46-51.
    • (1974) Science , vol.183 , pp. 46-51
    • Hartwell, L.1    Culotti, J.2    Pringle, J.3    Reid, B.4
  • 96
    • 0032547996 scopus 로고    scopus 로고
    • The role of Saccharomyces cerevisiae coronin in the actin and microtubule cytoskeletons
    • Heil-Chapdelaine, R., Trna, N. and Cooper, J. (1998). The role of Saccharomyces cerevisiae coronin in the actin and microtubule cytoskeletons. Curr. Biol. 8, 1281-1284.
    • (1998) Curr. Biol. , vol.8 , pp. 1281-1284
    • Heil-Chapdelaine, R.1    Trna, N.2    Cooper, J.3
  • 97
    • 0033565526 scopus 로고    scopus 로고
    • Endocytic delivery of intramolecularly quenched substrates and inhibitors to the intracellular yeast Kex2 protease
    • Henkel, M. K., Pott, G., Henkel, A., Juliano, L., Kam, C. M., Powers, J. and Franzusoff, A. (1999). Endocytic delivery of intramolecularly quenched substrates and inhibitors to the intracellular yeast Kex2 protease. Biochem. J. 341, 445-452.
    • (1999) Biochem. J. , vol.341 , pp. 445-452
    • Henkel, M.K.1    Pott, G.2    Henkel, A.3    Juliano, L.4    Kam, C.M.5    Powers, J.6    Franzusoff, A.7
  • 98
    • 0013658143 scopus 로고    scopus 로고
    • The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton during polarized morphogenesis
    • Hermann, G., King, E. and Shaw, J. (1997). The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton during polarized morphogenesis. Science 276, 118-122.
    • (1997) Science , vol.276 , pp. 118-122
    • Hermann, G.1    King, E.2    Shaw, J.3
  • 99
    • 0030803426 scopus 로고    scopus 로고
    • Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/N-ethylmaleimide-sensitive fusion protein
    • Hicke, L., Zanolari, B., Pypaert, M., Rohrer, J. and Riezman, H. (1997). Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/N-ethylmaleimide-sensitive fusion protein. Mol. Biol. Cell 8, 13-31.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 13-31
    • Hicke, L.1    Zanolari, B.2    Pypaert, M.3    Rohrer, J.4    Riezman, H.5
  • 100
    • 0032550179 scopus 로고    scopus 로고
    • Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization
    • Hicke, L., Zanolari, B. and Riezman, H. (1998). Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization. J. Cell Biol. 141, 349-358.
    • (1998) J. Cell Biol. , vol.141 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 101
    • 0030470182 scopus 로고    scopus 로고
    • Actin and myosin function in directed vacuole movements during cell division in Saccharomyces cerevisiae
    • Hill, K., Catlett, N. and Weisman, L. (1996). Actin and myosin function in directed vacuole movements during cell division in Saccharomyces cerevisiae. J. Cell Biol. 135, 1535-1549.
    • (1996) J. Cell Biol. , vol.135 , pp. 1535-1549
    • Hill, K.1    Catlett, N.2    Weisman, L.3
  • 102
    • 0033571294 scopus 로고    scopus 로고
    • PAK-family kinases regulate cell and actin polarization throughout the cell cycle of Saccharomyces cerevisiae
    • Holly, S. and Blunter, K. (1999). PAK-family kinases regulate cell and actin polarization throughout the cell cycle of Saccharomyces cerevisiae. J. Cell Biol. 147, 845-856.
    • (1999) J. Cell Biol. , vol.147 , pp. 845-856
    • Holly, S.1    Blunter, K.2
  • 103
    • 0032472324 scopus 로고    scopus 로고
    • Two syntaxin homologs in the TGN/endosomal system of yeast
    • Holthuis, J., Nichols, B., Dhruvakumar, S. and Pelham, H. (1998a). Two syntaxin homologs in the TGN/endosomal system of yeast. EMBO J. 17, 113-126.
    • (1998) EMBO J. , vol.17 , pp. 113-126
    • Holthuis, J.1    Nichols, B.2    Dhruvakumar, S.3    Pelham, H.4
  • 104
    • 0031795632 scopus 로고    scopus 로고
    • The syntaxin T1g1p mediates trafficking of chitin synthase III to polarized growth sites in yeast
    • Holthuis, J., Nichols, B. and Pelham, H. (1998b). The syntaxin T1g1p mediates trafficking of chitin synthase III to polarized growth sites in yeast. Mol. Biol. Cell 9, 3383-3397.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3383-3397
    • Holthuis, J.1    Nichols, B.2    Pelham, H.3
  • 105
    • 0027244817 scopus 로고
    • Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeletal assembly in Saccharomyces cerevisiae
    • Holtzman, D., Yang, S. and Drubin, D. (1993). Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeletal assembly in Saccharomyces cerevisiae. J. Cell Biol. 122, 635-644.
    • (1993) J. Cell Biol. , vol.122 , pp. 635-644
    • Holtzman, D.1    Yang, S.2    Drubin, D.3
  • 108
    • 0027475652 scopus 로고
    • Isolation of a yeast essential gene, COFI, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein
    • Iida, K., Moriyama, K., Matsumoto, S., Kawasaki, H., Nishida, E. and Yahara, I. (1993). Isolation of a yeast essential gene, COFI, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein. Gene. 124, 115-120.
    • (1993) Gene. , vol.124 , pp. 115-120
    • Iida, K.1    Moriyama, K.2    Matsumoto, S.3    Kawasaki, H.4    Nishida, E.5    Yahara, I.6
  • 109
    • 0032992123 scopus 로고    scopus 로고
    • Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae
    • Iida, K. and Yahara, I. (1999). Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Genes Cells 4, 21-32.
    • (1999) Genes Cells , vol.4 , pp. 21-32
    • Iida, K.1    Yahara, I.2
  • 110
    • 0030927327 scopus 로고    scopus 로고
    • Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • Imamura, H., Tanaka, K., Hihara, T., Umikawa, M., Kamei, T., Takahashi, K., Sasaki, T. and Takai, Y. (1997). Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J. 16, 2745-2755.
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5    Takahashi, K.6    Sasaki, T.7    Takai, Y.8
  • 111
    • 0029981258 scopus 로고    scopus 로고
    • Mother cell-specific HO expression in budding yeast depends on the unconventional myosin Myo4p and other cytoplasmic proteins
    • Jansen, R. P., Dowzer, C., Michaelis, C., Galova, M. and Nasmyth, K. (1996). Mother cell-specific HO expression in budding yeast depends on the unconventional myosin Myo4p and other cytoplasmic proteins. Cell 84, 687-697.
    • (1996) Cell , vol.84 , pp. 687-697
    • Jansen, R.P.1    Dowzer, C.2    Michaelis, C.3    Galova, M.4    Nasmyth, K.5
  • 112
    • 0025363198 scopus 로고
    • Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity
    • Johnson, D. and Pringle, J. (1990). Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111, 143-152.
    • (1990) J. Cell Biol. , vol.111 , pp. 143-152
    • Johnson, D.1    Pringle, J.2
  • 113
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston, G., Prendergast, J. and Singer, R. (1991). The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113, 539-551.
    • (1991) J. Cell Biol. , vol.113 , pp. 539-551
    • Johnston, G.1    Prendergast, J.2    Singer, R.3
  • 115
    • 0027484088 scopus 로고
    • Mutations that enhance the cap2 null mutant phenotype in Saccharomyces cerevisiae affect the actin cytoskeleton, morphogenesis and pattern of growth
    • Karpova, T., Leptit, M. and Cooper, J. (1993). Mutations that enhance the cap2 null mutant phenotype in Saccharomyces cerevisiae affect the actin cytoskeleton, morphogenesis and pattern of growth. Genetics 135, 693-709.
    • (1993) Genetics , vol.135 , pp. 693-709
    • Karpova, T.1    Leptit, M.2    Cooper, J.3
  • 116
    • 0032555918 scopus 로고    scopus 로고
    • Assembly and function of the actin cytoskeleton of yeast: Relationships between cables and patches
    • Karpova, T., McNally, J., Moltz, S. and Cooper, J. (1998). Assembly and function of the actin cytoskeleton of yeast: relationships between cables and patches. J. Cell Biol. 142, 1501-1517.
    • (1998) J. Cell Biol. , vol.142 , pp. 1501-1517
    • Karpova, T.1    McNally, J.2    Moltz, S.3    Cooper, J.4
  • 117
    • 0026019902 scopus 로고
    • Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: Localization of the CDC3 gene product and the timing of events at the budding site
    • Kim, H., Haarer, B. and Pringle, J. (1991). Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC3 gene product and the timing of events at the budding site. J. Cell Biol. 112, 535-544.
    • (1991) J. Cell Biol. , vol.112 , pp. 535-544
    • Kim, H.1    Haarer, B.2    Pringle, J.3
  • 118
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kübler, E. and Riezman, H. (1993). Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12, 2855-2862.
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kübler, E.1    Riezman, H.2
  • 119
    • 0028027789 scopus 로고
    • Calcium-independent calmodulin requirement for endocytosis in yeast
    • Kübler, E., Schimmöller, F. and Riezman, H. (1994). Calcium-independent calmodulin requirement for endocytosis in yeast. EMBO J. 13, 5539-5546.
    • (1994) EMBO J. , vol.13 , pp. 5539-5546
    • Kübler, E.1    Schimmöller, F.2    Riezman, H.3
  • 120
    • 0040826869 scopus 로고    scopus 로고
    • Distinct regulation of osmoprotective genes in yeast and mammals
    • Kültz, D., Garcia-Perez, A., Ferraris, J. and Burg, M. (1997). Distinct regulation of osmoprotective genes in yeast and mammals. J. Biol. Chem. 272, 13165-13170.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13165-13170
    • Kültz, D.1    Garcia-Perez, A.2    Ferraris, J.3    Burg, M.4
  • 121
    • 0028942256 scopus 로고
    • Actin- and microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • Langford, G. (1995). Actin- and microtubule-dependent organelle motors: interrelationships between the two motility systems. Curr. Opin. Cell Biol. 7, 82-88.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.1
  • 122
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen, P. and Drubin, D. (1997). Cofilin promotes rapid actin filament turnover in vivo. Nature 388, 78-82.
    • (1997) Nature , vol.388 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.2
  • 123
    • 0031015562 scopus 로고    scopus 로고
    • Functional characterization of the Cdc42p binding domain of yeast Ste20p protein kinase
    • Leberer, E., Wu, C., Leeuw, T., Fourest-Lieuvin, A., Segall, J. and Thomas, D. (1997). Functional characterization of the Cdc42p binding domain of yeast Ste20p protein kinase. EMBO J. 16, 83-97.
    • (1997) EMBO J. , vol.16 , pp. 83-97
    • Leberer, E.1    Wu, C.2    Leeuw, T.3    Fourest-Lieuvin, A.4    Segall, J.5    Thomas, D.6
  • 124
    • 0027266933 scopus 로고
    • A yeast mitogen-activated protein kinase homolog (Mpk1p) mediates signaling by protein kinase C
    • Lee, K., Irie, K., Gotoh, Y., Watanabe, Y., Araki, H., Nishida, E., Matsumoto, K. and Levin, D. (1993). A yeast mitogen-activated protein kinase homolog (Mpk1p) mediates signaling by protein kinase C. Mol. Cell Biol. 13, 3067-3075.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 3067-3075
    • Lee, K.1    Irie, K.2    Gotoh, Y.3    Watanabe, Y.4    Araki, H.5    Nishida, E.6    Matsumoto, K.7    Levin, D.8
  • 125
    • 0032481122 scopus 로고    scopus 로고
    • Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton
    • Lee, J., Colwill, K., Aneliunas, V., Tannyson, C., Moore, L., Ho, Y. and Andrews, B. (1998). Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton. Curr. Biol. 8, 1310-1321.
    • (1998) Curr. Biol. , vol.8 , pp. 1310-1321
    • Lee, J.1    Colwill, K.2    Aneliunas, V.3    Tannyson, C.4    Moore, L.5    Ho, Y.6    Andrews, B.7
  • 126
    • 0033535351 scopus 로고    scopus 로고
    • Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p
    • Lee, L., Klee, S., Evangelist, M., Boone, C. and Pellham, D. (1999). Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p. J. Cell Biol. 144, 947-961.
    • (1999) J. Cell Biol. , vol.144 , pp. 947-961
    • Lee, L.1    Klee, S.2    Evangelist, M.3    Boone, C.4    Pellham, D.5
  • 127
    • 0028925710 scopus 로고
    • Cell cycle control of morphogenesis in budding yeast
    • Lew, D. and Reed, S. (1995). Cell cycle control of morphogenesis in budding yeast. Curr. Opin. Genet. Dev. 5, 17-23.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 17-23
    • Lew, D.1    Reed, S.2
  • 128
    • 0031045512 scopus 로고    scopus 로고
    • Beel, a yeast protein with homology to Wiscott-Aldrich Syndrome Protein, is critical for the assembly of cortical actin cytoskeleton
    • Li, R. (1997). Beel, a yeast protein with homology to Wiscott-Aldrich Syndrome Protein, is critical for the assembly of cortical actin cytoskeleton. J. Cell Biol. 136, 649-658.
    • (1997) J. Cell Biol. , vol.136 , pp. 649-658
    • Li, R.1
  • 129
    • 0031027546 scopus 로고    scopus 로고
    • Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton
    • Lila, T. and Drubin, D. (1997). Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton. Mol. Biol. Cell. 8, 367-385.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 367-385
    • Lila, T.1    Drubin, D.2
  • 130
    • 0026539415 scopus 로고
    • Suppression of a myosin defect by a kinesin-related gene
    • Lillie, S. and Brown, S. (1992). Suppression of a myosin defect by a kinesin-related gene. Nature 356, 358-361.
    • (1992) Nature , vol.356 , pp. 358-361
    • Lillie, S.1    Brown, S.2
  • 131
    • 0028352176 scopus 로고
    • Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae
    • Lillie, S. and Brown, S. (1994). Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae. J. Cell Biol. 125, 825-842.
    • (1994) J. Cell Biol. , vol.125 , pp. 825-842
    • Lillie, S.1    Brown, S.2
  • 132
    • 0032559545 scopus 로고    scopus 로고
    • Smy1p. a kinesin-related protein that does not require microtubules
    • Lillie, S. and Brown, S. (1998). Smy1p. a kinesin-related protein that does not require microtubules. J. Cell Biol. 140, 873-883.
    • (1998) J. Cell Biol. , vol.140 , pp. 873-883
    • Lillie, S.1    Brown, S.2
  • 133
    • 0032576546 scopus 로고    scopus 로고
    • Dual function of Cyk2, a cdc15/PSTPIP family protein, in regulating aclomyosin ring dynamics and septin distribution
    • Lippincott, J. and Li, R. (1998a). Dual function of Cyk2, a cdc15/PSTPIP family protein, in regulating aclomyosin ring dynamics and septin distribution. J. Cell Biol. 143, 1947-1960.
    • (1998) J. Cell Biol. , vol.143 , pp. 1947-1960
    • Lippincott, J.1    Li, R.2
  • 134
    • 0032567760 scopus 로고    scopus 로고
    • Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis
    • Lippincott, J. and Li, R. (1998b). Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis. J. Cell Biol. 140, 355-366.
    • (1998) J. Cell Biol. , vol.140 , pp. 355-366
    • Lippincott, J.1    Li, R.2
  • 135
    • 0024516197 scopus 로고
    • Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton
    • Liu, H. and Bretscher, A. (1989). Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton. Cell 57, 233-242.
    • (1989) Cell , vol.57 , pp. 233-242
    • Liu, H.1    Bretscher, A.2
  • 136
    • 0030875775 scopus 로고    scopus 로고
    • Mating type switching in yeast controlled by asymmetric localization of ASHI mRNA
    • Long, R., Singer, R., Meng, X., Gonzalez, I., Nasmyth, K. and Jansen, R. P. (1997). Mating type switching in yeast controlled by asymmetric localization of ASHI mRNA. Science 277, 383-387.
    • (1997) Science , vol.277 , pp. 383-387
    • Long, R.1    Singer, R.2    Meng, X.3    Gonzalez, I.4    Nasmyth, K.5    Jansen, R.P.6
  • 137
    • 0032476712 scopus 로고    scopus 로고
    • Role of the yeast Gin4p protein kinase in septin assembly and the relationship between septin assembly and septin function
    • Longtine, M., Fares, J. and Pringle, J. (1998). Role of the yeast Gin4p protein kinase in septin assembly and the relationship between septin assembly and septin function. J. Cell Biol. 143, 719-736.
    • (1998) J. Cell Biol. , vol.143 , pp. 719-736
    • Longtine, M.1    Fares, J.2    Pringle, J.3
  • 138
    • 0032835492 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologue of human Wiskolt-Aldrich Syndrome Protein Las17p interacts with the Arp2/3 complex
    • Madania, A., Dumoulin, P., Grava, S., Kitamoto, H., Schärer-Brodbeck, C., Soulard, A., Moreau, V. and Winsor, B. (1999). The Saccharomyces cerevisiae homologue of human Wiskolt-Aldrich Syndrome Protein Las17p interacts with the Arp2/3 complex. Mol. Biol. Cell. 10, 3521-3538.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 3521-3538
    • Madania, A.1    Dumoulin, P.2    Grava, S.3    Kitamoto, H.4    Schärer-Brodbeck, C.5    Soulard, A.6    Moreau, V.7    Winsor, B.8
  • 139
    • 0030868676 scopus 로고    scopus 로고
    • The Rho-GEF Rom2p localizes to sites of polarized cell growth and participates in cytoskeletal functions in Saccharomyces cerevisiae
    • Manning, B., Padmanabha, R. and Snyder, M. (1997). The Rho-GEF Rom2p localizes to sites of polarized cell growth and participates in cytoskeletal functions in Saccharomyces cerevisiae. Mol. Biol. Cell 8, 1829-1844.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1829-1844
    • Manning, B.1    Padmanabha, R.2    Snyder, M.3
  • 140
    • 0031016037 scopus 로고    scopus 로고
    • Characterization of SKMI, a Saccharomyces cerevisiae gene encoding a novel Ste20/PAK-like protein kinase
    • Martin, H., Mendoza, A., Rodriguez-Pachon, J., Molina, M. and Nombela, C. (1997). Characterization of SKMI, a Saccharomyces cerevisiae gene encoding a novel Ste20/PAK-like protein kinase. Mol. Microbiol. 23, 431-444.
    • (1997) Mol. Microbiol. , vol.23 , pp. 431-444
    • Martin, H.1    Mendoza, A.2    Rodriguez-Pachon, J.3    Molina, M.4    Nombela, C.5
  • 141
    • 0026582424 scopus 로고
    • Isolation and characterization of two novel ras superfamily genes in Saccharomyces cerevisiae
    • Matsui, Y. and Toh-e, A. (1992a). Isolation and characterization of two novel ras superfamily genes in Saccharomyces cerevisiae. Gene 114, 43-49
    • (1992) Gene , vol.114 , pp. 43-49
    • Matsui, Y.1    Toh-e, A.2
  • 142
    • 0026484397 scopus 로고
    • Yeast RHO3 and RHO4 ras superfamily genes are necessary for bud growth, and their defect is suppressed by a high dose of bud formation genes CDC42 and REM1
    • Matsui, Y. and Toh-e, A. (1992b). Yeast RHO3 and RHO4 ras superfamily genes are necessary for bud growth, and their defect is suppressed by a high dose of bud formation genes CDC42 and REM1. Mol. Cell. Biol. 12, 5690-5699.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5690-5699
    • Matsui, Y.1    Toh-e, A.2
  • 143
    • 0029128074 scopus 로고
    • Differential expression and function of two homologous subunits of yeast 1, 3-beta-D-glucan synthase
    • Mazur, P., Morin, N., Baginsky, W., el-Sherbeini, M., Clemas, J., Nielson, J. and Foor, F. (1995). Differential expression and function of two homologous subunits of yeast 1, 3-beta-D-glucan synthase. Mol. Cell. Biol. 15, 5671-5681.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5671-5681
    • Mazur, P.1    Morin, N.2    Baginsky, W.3    El-Sherbeini, M.4    Clemas, J.5    Nielson, J.6    Foor, F.7
  • 144
    • 0027761005 scopus 로고
    • The SLT2(MPKI) MAP kinase homolog is involved in polarized cell growth in Saccharomyces cerevisiae
    • Mazzoni, C., Zarzov, P., Ranbourg, A. and Mann, C. (1993). The SLT2(MPKI) MAP kinase homolog is involved in polarized cell growth in Saccharomyces cerevisiae. J. Cell Biol. 123, 1821-1833.
    • (1993) J. Cell Biol. , vol.123 , pp. 1821-1833
    • Mazzoni, C.1    Zarzov, P.2    Ranbourg, A.3    Mann, C.4
  • 145
    • 0025987902 scopus 로고
    • The small GTP-binding protein Rho1p localized on the Golgi apparatus and post-Golgi vesicles in Saccharomyces cerevisiae
    • McCaffrey, M., Johnson, J., Goud, B., Myers, A., Rossier, J., Popoff, M., Madaule, P. and Boquet, P. (1991). The small GTP-binding protein Rho1p localized on the Golgi apparatus and post-Golgi vesicles in Saccharomyces cerevisiae. J. Cell Biol. 115, 309-319.
    • (1991) J. Cell Biol. , vol.115 , pp. 309-319
    • McCaffrey, M.1    Johnson, J.2    Goud, B.3    Myers, A.4    Rossier, J.5    Popoff, M.6    Madaule, P.7    Boquet, P.8
  • 146
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • McCann, R. and Craig, S. (1997). The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc. Nat. Acad. Sci. USA 94, 5679-5684.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 5679-5684
    • McCann, R.1    Craig, S.2
  • 148
    • 0032567757 scopus 로고    scopus 로고
    • Kar9p is a novel cortical protein required for cytoplasmic microtubule orientation in yeast
    • Miller, R. and Rose, M. (1998). Kar9p is a novel cortical protein required for cytoplasmic microtubule orientation in yeast. J. Cell Biol. 140, 377-390.
    • (1998) J. Cell Biol. , vol.140 , pp. 377-390
    • Miller, R.1    Rose, M.2
  • 149
    • 0033535321 scopus 로고    scopus 로고
    • The conical localization of the microtubule orientation protein, Kar9p, is dependent upon actin and proteins required for polarization
    • Miller, R., Matheos, D. and Rose, M. (1999). The conical localization of the microtubule orientation protein, Kar9p, is dependent upon actin and proteins required for polarization. J. Cell Biol. 144, 963-975.
    • (1999) J. Cell Biol. , vol.144 , pp. 963-975
    • Miller, R.1    Matheos, D.2    Rose, M.3
  • 150
    • 0032578776 scopus 로고    scopus 로고
    • Shs1p: A novel member of septin that interacts with Spa2p, involved in polarized growth in Saccharomyces cerevisiae
    • Mino, A., Tanaka, K., Kamei, T., Umikawa, M., Fujiwara, T. and Takai, Y. (1998). Shs1p: a novel member of septin that interacts with Spa2p, involved in polarized growth in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 251, 732-736.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 732-736
    • Mino, A.1    Tanaka, K.2    Kamei, T.3    Umikawa, M.4    Fujiwara, T.5    Takai, Y.6
  • 151
    • 0027446345 scopus 로고
    • Cotilin is an essential component of the yeast cortical cytoskeleton
    • Moon, A., Janmey, P., Louie, A. and Drubin, D. (1993). Cotilin is an essential component of the yeast cortical cytoskeleton. J. Cell Biol. 120, 421-435.
    • (1993) J. Cell Biol. , vol.120 , pp. 421-435
    • Moon, A.1    Janmey, P.2    Louie, A.3    Drubin, D.4
  • 152
    • 0029959468 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton
    • Moreau, V., Madania, A., Martin, R. and Winsor, B. (1996). The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J. Cell Biol. 134, 117-132.
    • (1996) J. Cell Biol. , vol.134 , pp. 117-132
    • Moreau, V.1    Madania, A.2    Martin, R.3    Winsor, B.4
  • 153
    • 0038765187 scopus 로고    scopus 로고
    • Dissection of filamentous growth by transposon mutagenesis in Saccharomyces cerevisiae
    • Mösch, H. U. and Fink, G. (1997) Dissection of filamentous growth by transposon mutagenesis in Saccharomyces cerevisiae. Genetics 145, 671-684.
    • (1997) Genetics , vol.145 , pp. 671-684
    • Mösch, H.U.1    Fink, G.2
  • 154
    • 0028204439 scopus 로고
    • Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane
    • Mulholland, J., Preuss, D., Moon, A., Wong, A., Drubin, D. and Botstein, D. (1994). Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J. Cell Biol. 125, 381-391.
    • (1994) J. Cell Biol. , vol.125 , pp. 381-391
    • Mulholland, J.1    Preuss, D.2    Moon, A.3    Wong, A.4    Drubin, D.5    Botstein, D.6
  • 155
    • 0030930123 scopus 로고    scopus 로고
    • Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretory vesicle
    • Mulholland, J., Wesp, A., Riezman, H. and Botstein, D. (1997). Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretory vesicle. Mol. Biol. Cell 8, 1481-1499.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1481-1499
    • Mulholland, J.1    Wesp, A.2    Riezman, H.3    Botstein, D.4
  • 157
    • 0344780902 scopus 로고    scopus 로고
    • Association of the class V myosin Myo4p with a localized messenger RNA in budding yeast depends on She proteins
    • Münchow, S., Sauter, C. and Jansen, R. P. (1999). Association of the class V myosin Myo4p with a localized messenger RNA in budding yeast depends on She proteins. J. Cell Sci. 112, 1511-1518.
    • (1999) J. Cell Sci. , vol.112 , pp. 1511-1518
    • Münchow, S.1    Sauter, C.2    Jansen, R.P.3
  • 158
    • 0025009803 scopus 로고
    • Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42
    • Munemitsu, S., Innis, M., Clark, R., McCormick, R., Ullrich, A. and Polakis, P. (1990). Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42. Mol. Cell. Biol. 10, 5977-5982.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5977-5982
    • Munemitsu, S.1    Innis, M.2    Clark, R.3    McCormick, R.4    Ullrich, A.5    Polakis, P.6
  • 159
    • 0028856410 scopus 로고
    • end5, end6, and end7: Mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae
    • Munn, A., Steveson, B., Geli, M. I., and Riezman, H. (1995). end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 6, 1721-1742.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1721-1742
    • Munn, A.1    Steveson, B.2    Geli, M.I.3    Riezman, H.4
  • 160
    • 0032572759 scopus 로고    scopus 로고
    • The WASp homologue Las17p functions with the W1P homologue End5p/verprolin and is essential for endocytosis in yeast
    • Naqvi, S., Zahn, R., Mitchell, D., Stevenson, B. and Munn, A. (1998). The WASp homologue Las17p functions with the W1P homologue End5p/verprolin and is essential for endocytosis in yeast. Curr. Biol. 8, 959-962.
    • (1998) Curr. Biol. , vol.8 , pp. 959-962
    • Naqvi, S.1    Zahn, R.2    Mitchell, D.3    Stevenson, B.4    Munn, A.5
  • 161
    • 0033593974 scopus 로고    scopus 로고
    • A Cdc24p-Far1p-Gβγ protein complex required for yeast orientation during mating
    • Nern, A. and Arkowitz, R. (1999). A Cdc24p-Far1p-Gβγ protein complex required for yeast orientation during mating. J. Cell Biol. 144, 1187-1202.
    • (1999) J. Cell Biol. , vol.144 , pp. 1187-1202
    • Nern, A.1    Arkowitz, R.2
  • 162
    • 0031555306 scopus 로고    scopus 로고
    • Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae
    • Novarro, P., Durrens, P. and Aigle, M. (1997). Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Biochim. Biophys. Acta 1343, 187-192.
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 187-192
    • Novarro, P.1    Durrens, P.2    Aigle, M.3
  • 163
    • 0021906692 scopus 로고
    • Phenotypic analysis of temperature-sensitive yeast actin mutants
    • Novick, P. and Botstein, D. (1985). Phenotypic analysis of temperature-sensitive yeast actin mutants. Cell 40, 405-416.
    • (1985) Cell , vol.40 , pp. 405-416
    • Novick, P.1    Botstein, D.2
  • 164
    • 0028266837 scopus 로고
    • Diverse essential functions revealed by complementing yeast calmodulin mutants
    • Ohya, Y. and Botstein, D. (1994). Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263, 963-966.
    • (1994) Science , vol.263 , pp. 963-966
    • Ohya, Y.1    Botstein, D.2
  • 165
    • 0033563261 scopus 로고    scopus 로고
    • Polyproline binding is an essential function of human profilin in yeast
    • Ostrander, D., Ernst, E., Lavoie, T. and Gorman, J. (1999). Polyproline binding is an essential function of human profilin in yeast. Eur. J. Biochem. 262, 26-35.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 26-35
    • Ostrander, D.1    Ernst, E.2    Lavoie, T.3    Gorman, J.4
  • 166
    • 0029920783 scopus 로고    scopus 로고
    • Rom1p and Rom2p are GDP/GTP exchange proteins (GEFs) for the Rholp small GTP binding protein in Saccharomyces cerevisiae
    • Ozaki, K., Tanaka, K., Imamura, H., Hihara, T., Kameyama, T., Nonaka, H., Hirano, H., Matsuura, Y. and Takai, Y. (1996). Rom1p and Rom2p are GDP/GTP exchange proteins (GEFs) for the Rholp small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15, 2196-2207.
    • (1996) EMBO J. , vol.15 , pp. 2196-2207
    • Ozaki, K.1    Tanaka, K.2    Imamura, H.3    Hihara, T.4    Kameyama, T.5    Nonaka, H.6    Hirano, H.7    Matsuura, Y.8    Takai, Y.9
  • 167
    • 0030743354 scopus 로고    scopus 로고
    • Suppressors of YCK-encoded yeast casein kinase I deficiency define the four subunits of a novel clathrin AP-like complex
    • Panek, H., Stepp, J., Engle, H., Marks, K., Tan, P., Lemmon, S. and Robinson, L. (1997). Suppressors of YCK-encoded yeast casein kinase I deficiency define the four subunits of a novel clathrin AP-like complex. EMBO J. 16, 4194-4204.
    • (1997) EMBO J. , vol.16 , pp. 4194-4204
    • Panek, H.1    Stepp, J.2    Engle, H.3    Marks, K.4    Tan, P.5    Lemmon, S.6    Robinson, L.7
  • 168
    • 0027264558 scopus 로고
    • BUD2 encodes a GTPase-activating protein for Bud1/Rsr1 necessary tor proper bud-site selection in yeast
    • Park, H. O., Chant, J. and Herskowitz, I. (1993). BUD2 encodes a GTPase-activating protein for Bud1/Rsr1 necessary tor proper bud-site selection in yeast. Nature 365, 269-274.
    • (1993) Nature , vol.365 , pp. 269-274
    • Park, H.O.1    Chant, J.2    Herskowitz, I.3
  • 169
    • 0033180065 scopus 로고    scopus 로고
    • Localization of Bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site
    • Park, H. O., Sanson, A. and Herskoitz, I. (1999). Localization of Bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site. Genes Dev. 13, 1912-1917.
    • (1999) Genes Dev. , vol.13 , pp. 1912-1917
    • Park, H.O.1    Sanson, A.2    Herskoitz, I.3
  • 170
    • 0030465534 scopus 로고    scopus 로고
    • Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast
    • Peter, M., Neiman, A., Park, H. O., van Lohuizen, M. and Herskowitz, I. (1996). Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast. EMBO J. 15, 7046-7059.
    • (1996) EMBO J. , vol.15 , pp. 7046-7059
    • Peter, M.1    Neiman, A.2    Park, H.O.3    Van Lohuizen, M.4    Herskowitz, I.5
  • 171
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the Myo2p-dependent delivery of secretory vesicles in budding yeast
    • Pruyne, D., Schott, D. and Bretscher, A. (1998). Tropomyosin-containing actin cables direct the Myo2p-dependent delivery of secretory vesicles in budding yeast. J. Cell Biol. 143, 1931-1945.
    • (1998) J. Cell Biol. , vol.143 , pp. 1931-1945
    • Pruyne, D.1    Schott, D.2    Bretscher, A.3
  • 172
    • 0034002965 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast. 1. Establishment and maintenance of polarity states
    • in press
    • Pruyne, D. and Bretscher, A. (2000). Polarization of cell growth in yeast. 1. Establishment and maintenance of polarity states. J. Cell Sci. (in press).
    • (2000) J. Cell Sci.
    • Pruyne, D.1    Bretscher, A.2
  • 174
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., Rohrer, J., Crausaz, F. and Riezman, H. (1993). end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120, 55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 175
    • 0032915418 scopus 로고    scopus 로고
    • The tail of a yeast class V myosin, Myo2p, functions as a localization domain
    • Reck-Peterson, S., Novick, P. and Mooseker, M. (1999). The tail of a yeast class V myosin, Myo2p, functions as a localization domain. Mol. Biol. Cell 10, 1001-1017.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1001-1017
    • Reck-Peterson, S.1    Novick, P.2    Mooseker, M.3
  • 176
    • 0033546275 scopus 로고    scopus 로고
    • 2/M morphogenetic checkpoint regulating the apical-isotropic switch and nuclear division in yeast
    • 2/M morphogenetic checkpoint regulating the apical-isotropic switch and nuclear division in yeast. J. Biol. Chem. 274, 16861-16870.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16861-16870
    • Richman, T.1    Sawyer, M.2    Johnson, D.3
  • 177
    • 0027168362 scopus 로고
    • Casein kinase I-like protein kinases encoded by KCK1 and YCK2 are required for yeast morphogenesis
    • Robinson, L., Menold, M., Garrett, S. and Culbertson, M. (1993). Casein kinase I-like protein kinases encoded by KCK1 and YCK2 are required for yeast morphogenesis. Mol. Cell. Biol. 13, 2870-2881.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2870-2881
    • Robinson, L.1    Menold, M.2    Garrett, S.3    Culbertson, M.4
  • 178
    • 0032938745 scopus 로고    scopus 로고
    • Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70
    • Robinson, N., Gou, L., Imai, J., Toh-E, A., Matsui, Y. and Tamanoi, F. (1999a). Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol. Cell. Biol. 19, 3580-3587.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3580-3587
    • Robinson, N.1    Gou, L.2    Imai, J.3    Toh-E, A.4    Matsui, Y.5    Tamanoi, F.6
  • 179
    • 0032911043 scopus 로고    scopus 로고
    • The Yck2 yeast casein kinase I isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization
    • Robinson, L., Bradley, C., Bryan, J., Jerome, A., Kweon, Y. and Panek, H. (1999b). The Yck2 yeast casein kinase I isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization. Mol. Biol. Cell. 10, 1077-1092.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 1077-1092
    • Robinson, L.1    Bradley, C.2    Bryan, J.3    Jerome, A.4    Kweon, Y.5    Panek, H.6
  • 180
  • 181
    • 0025605291 scopus 로고
    • Yeast myosin heavy chain mutant: Maintenance of the cell type specific budding pattern and the normal deposition of chitin and cell wall components requires an intact myosin heavy chain gene
    • Rodriguez, J. and Paterson, B. (1990). Yeast myosin heavy chain mutant: maintenance of the cell type specific budding pattern and the normal deposition of chitin and cell wall components requires an intact myosin heavy chain gene. Cell Motil. Cytoskel. 17, 301-308.
    • (1990) Cell Motil. Cytoskel. , vol.17 , pp. 301-308
    • Rodriguez, J.1    Paterson, B.2
  • 182
    • 0029995116 scopus 로고    scopus 로고
    • Selection of axial growth sites in yeast requires Ax12p, a novel plasma membrane glycoprotein
    • Roemer, T., Madden, K., Chang, J. and Snyder, M. (1996). Selection of axial growth sites in yeast requires Ax12p, a novel plasma membrane glycoprotein. Genes Dev. 10, 777-793.
    • (1996) Genes Dev. , vol.10 , pp. 777-793
    • Roemer, T.1    Madden, K.2    Chang, J.3    Snyder, M.4
  • 183
    • 0031908157 scopus 로고    scopus 로고
    • The Spa2-related protein. Sph1p, is important for polarized growth in yeast
    • Roemer, T., Vallier, L., Sheu, Y. J. and Snyder, M. (1998). The Spa2-related protein. Sph1p, is important for polarized growth in yeast. J. Cell Sci. 111, 479-494.
    • (1998) J. Cell Sci. , vol.111 , pp. 479-494
    • Roemer, T.1    Vallier, L.2    Sheu, Y.J.3    Snyder, M.4
  • 184
    • 0032426346 scopus 로고    scopus 로고
    • Early patterning of the c. elegans embryo
    • Rose, L. and Kemphues, K. (1998). Early patterning of the C. elegans embryo. Annu. Rev. Genet. 32, 521-545.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 521-545
    • Rose, L.1    Kemphues, K.2
  • 185
    • 0029999229 scopus 로고    scopus 로고
    • The Bud4 protein of yeast, required for axial budding, is localized to the mother/bud neck in a cell cycle-dependent manner
    • Sanders, S. and Herskowitz, I. (1996). The Bud4 protein of yeast, required for axial budding, is localized to the mother/bud neck in a cell cycle-dependent manner. J. Cell Biol. 134, 413-427.
    • (1996) J. Cell Biol. , vol.134 , pp. 413-427
    • Sanders, S.1    Herskowitz, I.2
  • 186
    • 0031013414 scopus 로고    scopus 로고
    • Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p
    • Santos, B. and Snyder, M. (1997). Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p. J. Cell Biol. 136, 95-110.
    • (1997) J. Cell Biol. , vol.136 , pp. 95-110
    • Santos, B.1    Snyder, M.2
  • 187
    • 0027943713 scopus 로고
    • Direct evidence for ligand-induced internalization of the yeast alpha-factor pheromone receptor
    • Schandel, K. and Jenness, D. (1994). Direct evidence for ligand-induced internalization of the yeast alpha-factor pheromone receptor. Mol. Cell. Biol. 14, 7245-7255.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7245-7255
    • Schandel, K.1    Jenness, D.2
  • 188
    • 0033571411 scopus 로고    scopus 로고
    • The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting
    • Schott, D., Ho, J., Pruyne, D. and Bretscher, A. (1999). The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J. Cell Biol. 147, 791-808.
    • (1999) J. Cell Biol. , vol.147 , pp. 791-808
    • Schott, D.1    Ho, J.2    Pruyne, D.3    Bretscher, A.4
  • 189
    • 0026058639 scopus 로고
    • The function of chitin synthases 2 and 3 in the Saccharomyces cerevisiae cell cycle
    • Shaw, J., Mol, P., Bowers, B., Silverman, S., Valdivieso, M., Duran, A. and Cabib, E. (1991). The function of chitin synthases 2 and 3 in the Saccharomyces cerevisiae cell cycle. J. Cell Biol. 114, 111-123.
    • (1991) J. Cell Biol. , vol.114 , pp. 111-123
    • Shaw, J.1    Mol, P.2    Bowers, B.3    Silverman, S.4    Valdivieso, M.5    Duran, A.6    Cabib, E.7
  • 190
    • 0025686144 scopus 로고
    • Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): Identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42
    • Shinjo, K., Koland, J., Hart, M., Narasimhan, V., Johnson, D., Evans, R. and Cerione, R. (1990). Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Proc. Nat. Acad Sci. USA 87, 9853-9857.
    • (1990) Proc. Nat. Acad Sci. USA , vol.87 , pp. 9853-9857
    • Shinjo, K.1    Koland, J.2    Hart, M.3    Narasimhan, V.4    Johnson, D.5    Evans, R.6    Cerione, R.7
  • 191
    • 0029864229 scopus 로고    scopus 로고
    • Identification of an asymmetrically localized determinant. Ash1p, required for lineage-specific transcription of the yeast HO gene
    • Sil, A. and Herskowitz, I. (1996). Identification of an asymmetrically localized determinant. Ash1p, required for lineage-specific transcription of the yeast HO gene. Cell 84, 711-722.
    • (1996) Cell , vol.84 , pp. 711-722
    • Sil, A.1    Herskowitz, I.2
  • 192
    • 0029078227 scopus 로고
    • Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: Identification of a motor activity on the mitochondrial surface
    • Simon, V., Swayne, T. and Pon, L. (1995). Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: identification of a motor activity on the mitochondrial surface. J. Cell Biol. 130, 345-354.
    • (1995) J. Cell Biol. , vol.130 , pp. 345-354
    • Simon, V.1    Swayne, T.2    Pon, L.3
  • 193
    • 0030854830 scopus 로고    scopus 로고
    • Mitochondrial inheritance: Cell cycle and actin cable dependence of polarized mitochondrial movements in Saccharomyces cerevisiae
    • Simon, V., Karmon, S. and Pon, L. (1997). Mitochondrial inheritance: cell cycle and actin cable dependence of polarized mitochondrial movements in Saccharomyces cerevisiae. Cell Motil. Cytoskel. 37, 199-210.
    • (1997) Cell Motil. Cytoskel. , vol.37 , pp. 199-210
    • Simon, V.1    Karmon, S.2    Pon, L.3
  • 194
    • 0028910268 scopus 로고
    • Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: The Rvs161 protein shares common domains with the brain protein amphiphysin
    • Sivadon, P., Bauer, F., Aigle, M. and Crouzet, M. (1995). Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin. Mol. Gen. Genet. 246, 485-495.
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 485-495
    • Sivadon, P.1    Bauer, F.2    Aigle, M.3    Crouzet, M.4
  • 195
    • 0019445379 scopus 로고
    • Roles of the CDC24 gene product in cellular morphogenesis during the Saccharomyces cerevisiae cell cycle
    • Sloat, B., Adams, A. and Pringle, J. (1981). Roles of the CDC24 gene product in cellular morphogenesis during the Saccharomyces cerevisiae cell cycle. J. Cell Biol. 89, 395-405.
    • (1981) J. Cell Biol. , vol.89 , pp. 395-405
    • Sloat, B.1    Adams, A.2    Pringle, J.3
  • 196
    • 0024539080 scopus 로고
    • The SPA2 protein of yeast localizes to sites of cell growth
    • Snyder, M. (1989). The SPA2 protein of yeast localizes to sites of cell growth. J. Cell Biol. 108, 1419-1429.
    • (1989) J. Cell Biol. , vol.108 , pp. 1419-1429
    • Snyder, M.1
  • 197
    • 0031822156 scopus 로고    scopus 로고
    • MIcIp is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae
    • Stevens, R. and Davis, T. (1998). MIcIp is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae. J. Cell Biol. 142, 711-722.
    • (1998) J. Cell Biol. , vol.142 , pp. 711-722
    • Stevens, R.1    Davis, T.2
  • 198
    • 0030930836 scopus 로고    scopus 로고
    • Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast
    • Takizawa, P., Sil, A., Swedlow, J., Herskowitz, I. and Vale, R. (1997). Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast. Nature 389, 90-93.
    • (1997) Nature , vol.389 , pp. 90-93
    • Takizawa, P.1    Sil, A.2    Swedlow, J.3    Herskowitz, I.4    Vale, R.5
  • 199
    • 0029772320 scopus 로고    scopus 로고
    • The EH-domain-containing protein Pan1p is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Tang, H. Y. and Cai, M. (1996). The EH-domain-containing protein Pan1p is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Cell. Biol. 16, 4897-4914.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4897-4914
    • Tang, H.Y.1    Cai, M.2
  • 200
    • 0344279906 scopus 로고    scopus 로고
    • EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae
    • Tang, H. Y., Munn, A. and Cai, M. (1997). EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae. Mol. Cell. Biol. 17, 4294-4304.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4294-4304
    • Tang, H.Y.1    Munn, A.2    Cai, M.3
  • 201
    • 0029045404 scopus 로고
    • Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae
    • TerBush, D. and Novick, P. (1995). Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae. J. Cell Biol. 130, 299-312.
    • (1995) J. Cell Biol. , vol.130 , pp. 299-312
    • TerBush, D.1    Novick, P.2
  • 202
    • 0029843493 scopus 로고    scopus 로고
    • The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush, D., Maurice, T., Roth, D. and Novick, P. (1996). The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 15, 6483-6494.
    • (1996) EMBO J. , vol.15 , pp. 6483-6494
    • TerBush, D.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 203
    • 0032858387 scopus 로고    scopus 로고
    • The role of actin in spindle orientation changes during the Saccharomyces cerevisiae cell cycle
    • Theesfeld, C., Irazoqui, J., Bloom, L. and Lew, D. (1999). The role of actin in spindle orientation changes during the Saccharomyces cerevisiae cell cycle. J. Cell Biol. 146, 1019-1032.
    • (1999) J. Cell Biol. , vol.146 , pp. 1019-1032
    • Theesfeld, C.1    Irazoqui, J.2    Bloom, L.3    Lew, D.4
  • 204
    • 0028807194 scopus 로고
    • rSec6 and rSec8, mammalian homologs of yeast proteins essential for secretion
    • Ting, A., Hazuka, C., Hsu, S., Kirk, M., Bean, A. and Scheller, R. (1995). rSec6 and rSec8, mammalian homologs of yeast proteins essential for secretion. Proc. Nat. Acad. Sci. USA 92, 9613-9617.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 9613-9617
    • Ting, A.1    Hazuka, C.2    Hsu, S.3    Kirk, M.4    Bean, A.5    Scheller, R.6
  • 205
    • 0033592690 scopus 로고    scopus 로고
    • The guanine-nucleotide-exchange factor Cdc24p is targeted to the nucleus and polarized growth sites
    • Toenjes, K., Sawyer, M. and Johnson, D. (1999). The guanine-nucleotide-exchange factor Cdc24p is targeted to the nucleus and polarized growth sites. Curr. Biol. 9, 1183-1186.
    • (1999) Curr. Biol. , vol.9 , pp. 1183-1186
    • Toenjes, K.1    Sawyer, M.2    Johnson, D.3
  • 206
    • 0031416482 scopus 로고    scopus 로고
    • Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton
    • Vaduva, G., Martin, N. and Hopper, A. (1997). Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. J. Cell Biol. 139, 1821-1833.
    • (1997) J. Cell Biol. , vol.139 , pp. 1821-1833
    • Vaduva, G.1    Martin, N.2    Hopper, A.3
  • 207
  • 208
    • 0029808463 scopus 로고    scopus 로고
    • Pea2 protein of yeast is localized to sites of polarized growth and is required for efficient mating and bipolar budding
    • Valtz, N. and Herskowitz, I. (1996). Pea2 protein of yeast is localized to sites of polarized growth and is required for efficient mating and bipolar budding. J. Cell Biol. 135, 725-739.
    • (1996) J. Cell Biol. , vol.135 , pp. 725-739
    • Valtz, N.1    Herskowitz, I.2
  • 209
    • 0031442669 scopus 로고    scopus 로고
    • A family of genes required for maintenance of cell wall integrity and for the stress response in Saccharomyces cerevisiae
    • Verna, J., Lodder, A., Lee, K., Vagts, A. and Ballester, R. (1997). A family of genes required for maintenance of cell wall integrity and for the stress response in Saccharomyces cerevisiae. Proc. Nat. Acad. Sci. USA 94, 13804-13809.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 13804-13809
    • Verna, J.1    Lodder, A.2    Lee, K.3    Vagts, A.4    Ballester, R.5
  • 210
    • 0025989194 scopus 로고
    • Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae
    • Vojtek, A., Haarer, B., Field, J., Gerst, J., Pollard, T., Brown, S. and Wigler, M. (1991). Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae. Cell 66, 497-505.
    • (1991) Cell , vol.66 , pp. 497-505
    • Vojtek, A.1    Haarer, B.2    Field, J.3    Gerst, J.4    Pollard, T.5    Brown, S.6    Wigler, M.7
  • 212
    • 0030930514 scopus 로고    scopus 로고
    • Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles
    • Walch-Solimena, C., Collins, R. and Novick, P. (1997). Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 137, 1495-1509.
    • (1997) J. Cell Biol. , vol.137 , pp. 1495-1509
    • Walch-Solimena, C.1    Collins, R.2    Novick, P.3
  • 213
    • 0030778198 scopus 로고    scopus 로고
    • Mutations synthetically lethal with rpm1Δ lie in genes involved in morphogenesis
    • Wang, T. and Bretscher, A. (1997). Mutations synthetically lethal with rpm1Δ lie in genes involved in morphogenesis. Genetics 147, 1595-1607.
    • (1997) Genetics , vol.147 , pp. 1595-1607
    • Wang, T.1    Bretscher, A.2
  • 214
    • 12644263389 scopus 로고    scopus 로고
    • A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15
    • Wendland, B., McCaffery, J. M., Xiao, Q. and Emr, S. (1996). A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15. J. Cell Biol. 135, 1485-1500.
    • (1996) J. Cell Biol. , vol.135 , pp. 1485-1500
    • Wendland, B.1    McCaffery, J.M.2    Xiao, Q.3    Emr, S.4
  • 215
    • 0032489873 scopus 로고    scopus 로고
    • Pan1, yeast esp15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis
    • Wendland, B. and Emr, S. (1998). Pan1, yeast esp15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis. J. Cell Biol. 141, 71-84.
    • (1998) J. Cell Biol. , vol.141 , pp. 71-84
    • Wendland, B.1    Emr, S.2
  • 216
    • 0032145902 scopus 로고    scopus 로고
    • Protein traffic in the yeast endocytic und vacuolar protein sorting pathways
    • Wendland, B., Emr, S. and Kiezman, H. (1998). Protein traffic in the yeast endocytic und vacuolar protein sorting pathways. Curr. Opin. Cell Biol. 10, 513-522.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 513-522
    • Wendland, B.1    Emr, S.2    Kiezman, H.3
  • 217
    • 0033575748 scopus 로고    scopus 로고
    • Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis
    • Wendland, B., Steece, K. and Emr, S. (1999). Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 18, 4383-4393.
    • (1999) EMBO J. , vol.18 , pp. 4383-4393
    • Wendland, B.1    Steece, K.2    Emr, S.3
  • 218
    • 0030785341 scopus 로고    scopus 로고
    • End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae
    • Wesp, A., Hicke, L., Palecek, J., Lombardi, R., Aust, T., Munn, A. and Riezman, H. (1997). End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 8, 2291-2306.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2291-2306
    • Wesp, A.1    Hicke, L.2    Palecek, J.3    Lombardi, R.4    Aust, T.5    Munn, A.6    Riezman, H.7
  • 219
    • 0031193920 scopus 로고    scopus 로고
    • The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches
    • Winter, D., Podtelejnikov, A., Mann, M. and Li, R. (1997). The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches. Curr. Biol. 7, 519-529.
    • (1997) Curr. Biol. , vol.7 , pp. 519-529
    • Winter, D.1    Podtelejnikov, A.2    Mann, M.3    Li, R.4
  • 220
    • 0033594955 scopus 로고    scopus 로고
    • Genetic dissection of the budding yeast Arp2/3 complex: A comparison of the in vivo and structural roles of individual subunits
    • Winter, D., Choe, E. and Li, R. (1999a). Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits. Proc. Nat. Acad. Sci. USA 96, 7288-7293.
    • (1999) Proc. Nat. Acad. Sci. USA , vol.96 , pp. 7288-7293
    • Winter, D.1    Choe, E.2    Li, R.3
  • 221
    • 0033528995 scopus 로고    scopus 로고
    • Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein
    • Winter, D., Lechler, T. and Li, R. (1999b). Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9, 501-504.
    • (1999) Curr. Biol. , vol.9 , pp. 501-504
    • Winter, D.1    Lechler, T.2    Li, R.3
  • 222
    • 0028930479 scopus 로고
    • In vitro motility of immunoadsorbed brain myosin-V using a Limulus acrosomal process and optical tweezer-based assay
    • Wolenski, J., Cheney, R., Mooseker, M. and Forscher, P. (1995). In vitro motility of immunoadsorbed brain myosin-V using a Limulus acrosomal process and optical tweezer-based assay. J. Cell Sci. 118, 1489-1496.
    • (1995) J. Cell Sci. , vol.118 , pp. 1489-1496
    • Wolenski, J.1    Cheney, R.2    Mooseker, M.3    Forscher, P.4
  • 223
    • 0030667791 scopus 로고    scopus 로고
    • The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast
    • Wu, C., Lytvyn, V., Thomas, D. and Leberer, E. (1997). The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast. J. Biol. Chem. 272, 30623-30626.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30623-30626
    • Wu, C.1    Lytvyn, V.2    Thomas, D.3    Leberer, E.4
  • 224
    • 0028228614 scopus 로고
    • Growth site localization of Rho1p small GTP-binding protein and its involvement in hud formation in Saccharomyces cerevisiae
    • Yamochi, W., Tanaka, K., Nonaka, H., Maeda, A., Musha, T. and Takai, V. (1994). Growth site localization of Rho1p small GTP-binding protein and its involvement in hud formation in Saccharomyces cerevisiae. J. Cell Biol. 125, 1077-1093.
    • (1994) J. Cell Biol. , vol.125 , pp. 1077-1093
    • Yamochi, W.1    Tanaka, K.2    Nonaka, H.3    Maeda, A.4    Musha, T.5    Takai, V.6
  • 225
    • 0031012576 scopus 로고    scopus 로고
    • A role for the actin cytoskeleton of Saccharomyces cerevisiae in bipolar bud-site selection
    • Yang, S., Ayscough, K. and Drubin, D. (1997). A role for the actin cytoskeleton of Saccharomyces cerevisiae in bipolar bud-site selection. J. Cell Biol. 136, 111-123.
    • (1997) J. Cell Biol. , vol.136 , pp. 111-123
    • Yang, S.1    Ayscough, K.2    Drubin, D.3
  • 226
    • 0033533697 scopus 로고    scopus 로고
    • A retention mechanism for distribution of mitochondria during cell division in budding yeast
    • Yang, H. C., Palazzo, A., Swayne, T. and Pon, L. (1999a). A retention mechanism for distribution of mitochondria during cell division in budding yeast. Curr. Biol. 9, 1111-1114.
    • (1999) Curr. Biol. , vol.9 , pp. 1111-1114
    • Yang, H.C.1    Palazzo, A.2    Swayne, T.3    Pon, L.4
  • 227
    • 0032589216 scopus 로고    scopus 로고
    • Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals
    • Yang, S., Cope, M. J. and Drubin, D. (1999b). Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol. Biol. Cell 10, 2265-2283.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2265-2283
    • Yang, S.1    Cope, M.J.2    Drubin, D.3
  • 228
    • 0029912384 scopus 로고    scopus 로고
    • Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae
    • Zahner, J., Harkins, H. and Pringle, J. (1996). Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 16, 1857-1870.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1857-1870
    • Zahner, J.1    Harkins, H.2    Pringle, J.3
  • 229
    • 0033545185 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p
    • Zeng, G. and Cai, M. (1999). Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p. J. Cell Biol. 144, 71-82.
    • (1999) J. Cell Biol. , vol.144 , pp. 71-82
    • Zeng, G.1    Cai, M.2
  • 230
    • 0027744475 scopus 로고
    • Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity
    • Ziman, M., Preuss, D., Mulholland, J., O'Brien, J., Botstein, D. and Johnson, D. (1993). Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity. Mol. Biol. Cell 4, 1307-1316.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1307-1316
    • Ziman, M.1    Preuss, D.2    Mulholland, J.3    O'Brien, J.4    Botstein, D.5    Johnson, D.6
  • 231
    • 0029808478 scopus 로고    scopus 로고
    • Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway
    • Ziman, M., Chuang, J. and Schekman, R. (1996). Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway. Mol. Biol. Cell 7, 1909-1919.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1909-1919
    • Ziman, M.1    Chuang, J.2    Schekman, R.3
  • 232
    • 0028791882 scopus 로고
    • Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery
    • Zoladek, T., Vaduva, G., Hunter, L., Boguta, M., Go, B., Martin, N. and Hopper, A. (1995). Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery. Mol. Cell. Biol. 12, 6884-6894.
    • (1995) Mol. Cell. Biol. , vol.12 , pp. 6884-6894
    • Zoladek, T.1    Vaduva, G.2    Hunter, L.3    Boguta, M.4    Go, B.5    Martin, N.6    Hopper, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.