메뉴 건너뛰기




Volumn 20, Issue , 2004, Pages 559-591

Mechanisms of polarized growth and organelle segregation in yeast

Author keywords

Actin; Mitosis; Myosin; Polarity

Indexed keywords

ACTIN; MYOSIN II; MYOSIN IV; MYOSIN V; RHO FACTOR;

EID: 8444223155     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.20.010403.103108     Document Type: Review
Times cited : (308)

References (237)
  • 1
    • 0025983823 scopus 로고
    • Requirement of yeast fimbrin for actin organization and morphogenesis in vivo
    • Adams AE, Botstein D, Drubin DG. 1991. Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Nature 354:404-8
    • (1991) Nature , vol.354 , pp. 404-408
    • Adams, A.E.1    Botstein, D.2    Drubin, D.G.3
  • 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 AE, Johnson DI, Longnecker RM, Sloat BF, Pringle JR. 1990. CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. J. Cell Biol. 111:131-42
    • (1990) J. Cell Biol. , vol.111 , pp. 131-142
    • Adams, A.E.1    Johnson, D.I.2    Longnecker, R.M.3    Sloat, B.F.4    Pringle, J.R.5
  • 3
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae
    • Adams AE, Pringle JR. 1984. Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae. J. Cell Biol. 98:934-45
    • (1984) J. Cell Biol. , vol.98 , pp. 934-945
    • Adams, A.E.1    Pringle, J.R.2
  • 4
    • 0034657914 scopus 로고    scopus 로고
    • Microtubule interactions with the cell cortex causing nuclear movements in Saccharomyces cerevisiae
    • Adames NR, Cooper JA. 2000. Microtubule interactions with the cell cortex causing nuclear movements in Saccharomyces cerevisiae. J. Cell Biol. 149:863-74
    • (2000) J. Cell Biol. , vol.149 , pp. 863-874
    • Adames, N.R.1    Cooper, J.A.2
  • 5
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts AS. 2001. Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276:2824-30
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 6
    • 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 DC, Zahner JE, Mulholland JW, Pringle JR, 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 8:729-53
    • (1997) Mol. Biol. Cell , vol.8 , pp. 729-753
    • Amberg, D.C.1    Zahner, J.E.2    Mulholland, J.W.3    Pringle, J.R.4    Botstein, D.5
  • 7
    • 15644379785 scopus 로고    scopus 로고
    • Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae
    • Asakura T, Sasaki T, Nagano F, Satoh A, Obaishi H, et al. 1998. Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae. Oncogene 16:121-30
    • (1998) Oncogene , vol.16 , pp. 121-130
    • Asakura, T.1    Sasaki, T.2    Nagano, F.3    Satoh, A.4    Obaishi, H.5
  • 8
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough KR, Stryker J, Pokala N, Sanders M, Crews P, Drubin DG. 1997. High rates of actin filament 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.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 10
    • 0034735942 scopus 로고    scopus 로고
    • The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast
    • Beach DL, Thibodeaux J, Maddox P, Yeh E, Bloom K. 2000. The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast. Curr. Biol. 10:1497-506
    • (2000) Curr. Biol. , vol.10 , pp. 1497-1506
    • Beach, D.L.1    Thibodeaux, J.2    Maddox, P.3    Yeh, E.4    Bloom, K.5
  • 11
    • 0024829578 scopus 로고
    • Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the ras-related gene RSR1
    • Bender A, Pringle JR. 1989. Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the ras-related gene RSR1. Proc. Natl. Acad. Sci. USA 86:9976-80
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9976-9980
    • Bender, A.1    Pringle, J.R.2
  • 12
    • 0025959707 scopus 로고
    • Use of a screen for synthetic lethal and multicopy suppresse mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae
    • Bender A, Pringle JR. 1991. Use of a screen for synthetic lethal and multicopy suppresse mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae. Mol. Cell Biol. 11:1295-305
    • (1991) Mol. Cell Biol. , vol.11 , pp. 1295-1305
    • Bender, A.1    Pringle, J.R.2
  • 13
    • 0028024386 scopus 로고
    • The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast
    • Benedetti H, Raths S, Crausaz F, Riezman H. 1994. The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast. Mol. Biol. Cell 5:1023-37
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1023-1037
    • Benedetti, H.1    Raths, S.2    Crausaz, F.3    Riezman, H.4
  • 14
    • 0034004749 scopus 로고    scopus 로고
    • The yeast kinesin-related protein smy1p exerts its effects on the class V myosin myo2p via a physical interaction
    • Beningo KA, Lillie SH, Brown SS. 2000. The yeast kinesin-related protein smy1p exerts its effects on the class V myosin myo2p via a physical interaction. Mol. Biol. Cell 11:691-702
    • (2000) Mol. Biol. Cell , vol.11 , pp. 691-702
    • Beningo, K.A.1    Lillie, S.H.2    Brown, S.S.3
  • 15
    • 0029804680 scopus 로고    scopus 로고
    • Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast
    • Benli M, Doring F, Robinson DG, Yang X, Gallwitz D. 1996. Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast. EMBO J. 15:6460-75
    • (1996) EMBO J. , vol.15 , pp. 6460-6475
    • Benli, M.1    Doring, F.2    Robinson, D.G.3    Yang, X.4    Gallwitz, D.5
  • 16
    • 0030848931 scopus 로고    scopus 로고
    • Cla4p, a Saccharomyces cerevisiae Cdc42p-activated kinase involved in cytokinesis, is activated at mitosis
    • Benton BK, Tinkelenberg A, Gonzalez I, Cross FR. 1997. Cla4p, a Saccharomyces cerevisiae Cdc42p-activated kinase involved in cytokinesis, is activated at mitosis. Mol. Cell Biol. 17:5067-76
    • (1997) Mol. Cell Biol. , vol.17 , pp. 5067-5076
    • Benton, B.K.1    Tinkelenberg, A.2    Gonzalez, I.3    Cross, F.R.4
  • 19
    • 0035093062 scopus 로고    scopus 로고
    • Spindles cotton on to junctions, APC and EB1
    • Bienz M. 2001. Spindles cotton on to junctions, APC and EB1. Nat. Cell Biol. 3:E67-68
    • (2001) Nat. Cell Biol. , vol.3
    • Bienz, M.1
  • 20
    • 0029914986 scopus 로고    scopus 로고
    • Asymmetric accumulation of Ash1p in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells
    • Bobola N, Jansen RP, Shin TH, Nasmyth K. 1996. Asymmetric accumulation of Ash1p 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.H.3    Nasmyth, K.4
  • 21
    • 0034675993 scopus 로고    scopus 로고
    • She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p
    • Bohl F, Kruse C, Frank A, Ferring D, Jansen RP. 2000. She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p. EMBO J. 19:5514-24
    • (2000) EMBO J. , vol.19 , pp. 5514-5524
    • Bohl, F.1    Kruse, C.2    Frank, A.3    Ferring, D.4    Jansen, R.P.5
  • 22
    • 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, Pon LA. 1998. Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p. J. Cell Biol. 141:1371-81
    • (1998) J. Cell Biol. , vol.141 , pp. 1371-1381
    • Boldogh, I.1    Vojtov, N.2    Karmon, S.3    Pon, L.A.4
  • 23
    • 0344392841 scopus 로고    scopus 로고
    • A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery
    • Boldogh IR, Nowakowski DW, Yang HC, Chung H, Karmon S, et al. 2003. A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery. Mol. Biol. Cell 14:4618-27
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4618-4627
    • Boldogh, I.R.1    Nowakowski, D.W.2    Yang, H.C.3    Chung, H.4    Karmon, S.5
  • 25
    • 0035831555 scopus 로고    scopus 로고
    • Assembly of scaffold-mediated complexes containing Cdc 42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycle-regulated phosphorylation of Cdc24p
    • Bose I, Irazoqui JE, Moskow JJ, Bardes ES, Zyla TR, Lew DJ. 2001. Assembly of scaffold-mediated complexes containing Cdc 42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycle-regulated phosphorylation of Cdc24p. J. Biol. Chem. 276:7176-86
    • (2001) J. Biol. Chem. , vol.276 , pp. 7176-7186
    • Bose, I.1    Irazoqui, J.E.2    Moskow, J.J.3    Bardes, E.S.4    Zyla, T.R.5    Lew, D.J.6
  • 26
    • 0037451174 scopus 로고    scopus 로고
    • Polarized growth and organelle segregation in yeast: The tracks, motors, and receptors
    • Bretscher A. 2003. Polarized growth and organelle segregation in yeast: the tracks, motors, and receptors. J. Cell Biol. 160:811-16
    • (2003) J. Cell Biol. , vol.160 , pp. 811-816
    • Bretscher, A.1
  • 27
    • 0033280225 scopus 로고    scopus 로고
    • Cooperation between microtubule- and actin-based motor proteins
    • Brown SS. 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.S.1
  • 28
    • 0002739244 scopus 로고
    • Cytology of the yeast life cycle
    • ed. JN Strathern, EW Jones, JR Broach, Cold Spring Harbor, NY: Cold Spring Harbor Press
    • Byers B. 1981. Cytology of the yeast life cycle. In The Molecular Biology of the Yyeast Saccharomyces: Life Cycle and Inheritance, ed. JN Strathern, EW Jones, JR Broach, p. 59. Cold Spring Harbor, NY: Cold Spring Harbor Press
    • (1981) The Molecular Biology of the Yyeast Saccharomyces: Life Cycle and Inheritance , pp. 59
    • Byers, B.1
  • 29
    • 0016731336 scopus 로고
    • Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae
    • Byers B, Goetsch L. 1975. Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae. J. Bacteriol. 124:511-23
    • (1975) J. Bacteriol. , vol.124 , pp. 511-523
    • Byers, B.1    Goetsch, L.2
  • 30
    • 0030750203 scopus 로고    scopus 로고
    • Microtubules orient the mitotic spindle in yeast through dynein-dependent interactions with the cell cortex
    • Carminati JL, Stearns T. 1997. Microtubules orient the mitotic spindle in yeast through dynein-dependent interactions with the cell cortex. J. Cell Biol. 138:629-41
    • (1997) J. Cell Biol. , vol.138 , pp. 629-641
    • Carminati, J.L.1    Stearns, T.2
  • 31
    • 0036220079 scopus 로고    scopus 로고
    • Bud-site selection and cell polarity in budding yeast
    • Casamayor A, Snyder M. 2002. Bud-site selection and cell polarity in budding yeast. Curr. Opin. Microbiol. 5:179-86
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 179-186
    • Casamayor, A.1    Snyder, M.2
  • 32
    • 0034618049 scopus 로고    scopus 로고
    • Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes
    • Catlett NL, Duex JE, Tang F, Weisman LS. 2000. Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes. J. Cell Biol. 150:513-26
    • (2000) J. Cell Biol. , vol.150 , pp. 513-526
    • Catlett, N.L.1    Duex, J.E.2    Tang, F.3    Weisman, L.S.4
  • 33
    • 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 NL, Weisman LS. 1998. The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth. Proc. Natl. Acad. Sci. USA 95:14799-804
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14799-14804
    • Catlett, N.L.1    Weisman, L.S.2
  • 34
    • 0037126066 scopus 로고    scopus 로고
    • Singularity in budding: A role for the evolutionarily conserved small GTPase Cdc42p
    • Caviston JP, Tcheperegine SE, Bi E. 2002. Singularity in budding: a role for the evolutionarily conserved small GTPase Cdc42p. Proc. Natl. Acad. Sci. USA 99:12185-90
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12185-12190
    • Caviston, J.P.1    Tcheperegine, S.E.2    Bi, E.3
  • 35
    • 0028041168 scopus 로고
    • Cell polarity in yeast
    • Chant J. 1994. Cell polarity in yeast. Trends Genet. 10:328-33
    • (1994) Trends Genet. , vol.10 , pp. 328-333
    • Chant, J.1
  • 37
    • 0025899140 scopus 로고
    • Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for bud site selection and interacts with bud formation gene BEM1
    • Chant J, Corrado K, Pringle JR, Herskowitz I. 1991. Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for bud site selection and interacts with bud formation gene BEM1. Cell 65:1213-24
    • (1991) Cell , vol.65 , pp. 1213-1224
    • Chant, J.1    Corrado, K.2    Pringle, J.R.3    Herskowitz, I.4
  • 38
    • 0025814609 scopus 로고
    • Genetic control of bud site selection in yeast by a set of gene products that constitute a morphogenetic pathway
    • Chant J, Herskowitz I. 1991. Genetic control of bud site selection in yeast by a set of gene products that constitute a morphogenetic pathway. Cell 65:1203-12
    • (1991) Cell , vol.65 , pp. 1203-1212
    • Chant, J.1    Herskowitz, I.2
  • 39
    • 0026232880 scopus 로고
    • Budding and cell polarity in Saccharomyces cerevisiae
    • Chant J, Pringle JR. 1991. Budding and cell polarity in Saccharomyces cerevisiae. Curr. Opin. Genet. Dev. 1:342-50
    • (1991) Curr. Opin. Genet. Dev. , vol.1 , pp. 342-350
    • Chant, J.1    Pringle, J.R.2
  • 40
    • 0028915743 scopus 로고
    • GTPase cascades choreographing cellular behavior: Movement, morphogenesis, and more
    • Chant J, Stowers L. 1995. GTPase cascades choreographing cellular behavior: movement, morphogenesis, and more. Cell 81:1-4
    • (1995) Cell , vol.81 , pp. 1-4
    • Chant, J.1    Stowers, L.2
  • 41
    • 0034623789 scopus 로고    scopus 로고
    • Multigenerational cortical inheritance of the Rax2 protein in orienting polarity and division in yeast
    • Chen T, Hiroko T, Chaudhuri A, Inose F, Lord M, et al. 2000. Multigenerational cortical inheritance of the Rax2 protein in orienting polarity and division in yeast. Science 290:1975-78
    • (2000) Science , vol.290 , pp. 1975-1978
    • Chen, T.1    Hiroko, T.2    Chaudhuri, A.3    Inose, F.4    Lord, M.5
  • 42
    • 0026586631 scopus 로고
    • A yeast gene (BEM1) necessary for cell polarization whose product contains two SH3 domains
    • Chenevert J, Corrado K, Bender A, Pringle J, Herskowitz I. 1992. A yeast gene (BEM1) 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
  • 43
    • 0028074840 scopus 로고
    • ACT3: A putative centractin homologue in S. cerevisiae is required for proper orientation of the mitotic spindle
    • Clark SW, Meyer DI. 1994. ACT3: a putative centractin homologue in S. cerevisiae is required for proper orientation of the mitotic spindle. J. Cell Biol. 127:129-38
    • (1994) J. Cell Biol. , vol.127 , pp. 129-138
    • Clark, S.W.1    Meyer, D.I.2
  • 44
    • 10744220744 scopus 로고    scopus 로고
    • Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites
    • Desnos C, Schonn JS, Huet S, Tran VS, El-Amraoui A, et al. 2003. Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites. J. Cell Biol. 163:559-70
    • (2003) J. Cell Biol. , vol.163 , pp. 559-570
    • Desnos, C.1    Schonn, J.S.2    Huet, S.3    Tran, V.S.4    El-Amraoui, A.5
  • 45
    • 0029000061 scopus 로고
    • Lissencephaly and other malformations of cortical development: 1995 update
    • Dobyns WB, Truwit CL. 1995. Lissencephaly and other malformations of cortical development: 1995 update. Neuropediatrics 26:132-47
    • (1995) Neuropediatrics , vol.26 , pp. 132-147
    • Dobyns, W.B.1    Truwit, C.L.2
  • 46
    • 0037815488 scopus 로고    scopus 로고
    • Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast
    • Dong Y, Pruyne D, Bretscher A. 2003. Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast. J. Cell Biol. 161:1081-92
    • (2003) J. Cell Biol. , vol.161 , pp. 1081-1092
    • Dong, Y.1    Pruyne, D.2    Bretscher, A.3
  • 47
    • 0028954614 scopus 로고
    • Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions
    • Drees B, Brown C, Barrell BG, Bretscher A. 1995. Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions. J. Cell Biol. 128:383-92
    • (1995) J. Cell Biol. , vol.128 , pp. 383-392
    • Drees, B.1    Brown, C.2    Barrell, B.G.3    Bretscher, A.4
  • 48
    • 0027765526 scopus 로고
    • Actin structure and function: Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site
    • Drubin DG, Jones HD, Wertman KF. 1993. Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol. Biol. Cell 4:1277-94
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1277-1294
    • Drubin, D.G.1    Jones, H.D.2    Wertman, K.F.3
  • 49
    • 0035158456 scopus 로고    scopus 로고
    • Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae
    • Du Y, Pypaert M, Novick P, Ferro-Novick S. 2001. Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae. Mol. Biol. Cell 12:2614-28
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2614-2628
    • Du, Y.1    Pypaert, M.2    Novick, P.3    Ferro-Novick, S.4
  • 52
    • 0347185043 scopus 로고    scopus 로고
    • Myo4p and She3p are required for cortical ER inheritance in Saccharomyces cerevisiae
    • Estrada P, Kim J, Coleman J, Walker L, Dunn B, et al. 2003. Myo4p and She3p are required for cortical ER inheritance in Saccharomyces cerevisiae. J. Cell Biol. 163:1255-66
    • (2003) J. Cell Biol. , vol.163 , pp. 1255-1266
    • Estrada, P.1    Kim, J.2    Coleman, J.3    Walker, L.4    Dunn, B.5
  • 53
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista M, Blundell K, Longtine MS, Chow CJ, Adames N, et al. 1997. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276:118-22
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista, M.1    Blundell, K.2    Longtine, M.S.3    Chow, C.J.4    Adames, N.5
  • 54
    • 0036514271 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista M, Pruyne D, Amberg DC, Boone C, Bretscher A. 2002. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4:32-41
    • (2002) Nat. Cell Biol. , vol.4 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 55
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Signaling effectors for assembly and polarization of actin filaments
    • Evangelista M, Zigmond S, Boone C. 2003. Formins: signaling effectors for assembly and polarization of actin filaments. J. Cell Sci. 116:2603-11
    • (2003) J. Cell Sci. , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 56
    • 0035931754 scopus 로고    scopus 로고
    • Cortical Num1p interacts with the dynein intermediate chain Pac11p and cytoplasmic microtubules in budding yeast
    • Farkasovsky M, Kuntzel H. 2001. Cortical Num1p interacts with the dynein intermediate chain Pac11p and cytoplasmic microtubules in budding yeast. J. Cell Biol. 152:251-62
    • (2001) J. Cell Biol. , vol.152 , pp. 251-262
    • Farkasovsky, M.1    Kuntzel, H.2
  • 57
    • 0036198747 scopus 로고    scopus 로고
    • Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast
    • Fehrenbacher KL, Davis D, Wu M, Boldogh I, Pon LA. 2002. Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast. Mol. Biol. Cell 13:854-65
    • (2002) Mol. Biol. Cell , vol.13 , pp. 854-865
    • Fehrenbacher, K.L.1    Davis, D.2    Wu, M.3    Boldogh, I.4    Pon, L.A.5
  • 58
    • 0027219199 scopus 로고
    • Components required for cytokinesis are important for bud site selection in yeast
    • Flescher EG, Madden K, Snyder M. 1993. Components required for cytokinesis are important for bud site selection in yeast. J. Cell Biol. 122:373-86
    • (1993) J. Cell Biol. , vol.122 , pp. 373-386
    • Flescher, E.G.1    Madden, K.2    Snyder, M.3
  • 59
    • 0028151340 scopus 로고
    • A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes
    • Fujita A, Oka C, Arikawa Y, Katagai T, Tonouchi A, et al. 1994. A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes. Nature 372:567-70
    • (1994) Nature , vol.372 , pp. 567-570
    • Fujita, A.1    Oka, C.2    Arikawa, Y.3    Katagai, T.4    Tonouchi, A.5
  • 60
    • 0031665143 scopus 로고    scopus 로고
    • Rho1p-Bni1p-Spa2p interactions: Implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae
    • Fujiwara T, Tanaka K, Mino A, Kikyo M, Takahashi K, et al. 1998. Rho1p-Bni1p-Spa2p interactions: implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Biol. Cell 9:1221-33
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1221-1233
    • Fujiwara, T.1    Tanaka, K.2    Mino, A.3    Kikyo, M.4    Takahashi, K.5
  • 61
    • 0037044819 scopus 로고    scopus 로고
    • Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin
    • Fukuda M, Kuroda TS. 2002. Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin. J. Biol. Chem. 277:43096-103
    • (2002) J. Biol. Chem. , vol.277 , pp. 43096-43103
    • Fukuda, M.1    Kuroda, T.S.2
  • 62
    • 0030923317 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways
    • Geiser JR, Schott EJ, Kingsbury TJ, Cole NB, Totis LJ, et al. 1997. Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways. Mol. Biol. Cell 8:1035-50
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1035-1050
    • Geiser, J.R.1    Schott, E.J.2    Kingsbury, T.J.3    Cole, N.B.4    Totis, L.J.5
  • 63
    • 0037148528 scopus 로고    scopus 로고
    • Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p
    • Gladfelter AS, Bose I, Zyla TR, Bardes ES, Lew DJ. 2002. Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p. J. Cell Biol. 156:315-26
    • (2002) J. Cell Biol. , vol.156 , pp. 315-326
    • Gladfelter, A.S.1    Bose, I.2    Zyla, T.R.3    Bardes, E.S.4    Lew, D.J.5
  • 64
  • 66
    • 0029908193 scopus 로고    scopus 로고
    • Characterization of new vacuolar segregation mutants, isolated by screening for loss of proteinase B self-activation
    • Gomes de Mesquita DS, van den Hazel HB, Bouwman J, Woldringh CL. 1996. Characterization of new vacuolar segregation mutants, isolated by screening for loss of proteinase B self-activation. Eur. J. Cell Biol. 71:237-47
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 237-247
    • Gomes De Mesquita, D.S.1    Van Den Hazel, H.B.2    Bouwman, J.3    Woldringh, C.L.4
  • 67
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan B, Bowser R, Novick P. 1995. The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128:1055-68
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 68
    • 0033635230 scopus 로고    scopus 로고
    • Phosphorylation of the cdc42 exchange factor cdc24 by the PAK-like kinase cla4 may regulate polarized growth in yeast
    • Gulli M, Jaquenoud M, Shimada Y, Niederhauser G, Wiget P, Peter M. 2000. Phosphorylation of the cdc42 exchange factor cdc24 by the PAK-like kinase cla4 may regulate polarized growth in yeast. Mol. Cell 6:1155-67
    • (2000) Mol. Cell , vol.6 , pp. 1155-1167
    • Gulli, M.1    Jaquenoud, M.2    Shimada, Y.3    Niederhauser, G.4    Wiget, P.5    Peter, M.6
  • 69
    • 0033551705 scopus 로고    scopus 로고
    • Exo84p is an exocyst protein essential for secretion
    • Guo W, Grant A, Novick P. 1999. Exo84p is an exocyst protein essential for secretion. J. Biol. Chem. 274:23558-64
    • (1999) J. Biol. Chem. , vol.274 , pp. 23558-23564
    • Guo, W.1    Grant, A.2    Novick, P.3
  • 71
    • 0028216280 scopus 로고
    • Identification of MYO4, a second class V myosin gene in yeast
    • Haarer BK, Petzold A, Lillie SH, Brown SS. 1994. Identification of MYO4, a second class V myosin gene in yeast. J. Cell Sci. 107:1055-64
    • (1994) J. Cell Sci. , vol.107 , pp. 1055-1064
    • Haarer, B.K.1    Petzold, A.2    Lillie, S.H.3    Brown, S.S.4
  • 72
    • 0035914343 scopus 로고    scopus 로고
    • Identification and characterization of a family of Rab11-interacting proteins
    • Hales CM, Griner R, Hobdy-Henderson KC, Dorn MC, Hardy D, et al. 2001. Identification and characterization of a family of Rab11-interacting proteins. J. Biol. Chem. 276:39067-75
    • (2001) J. Biol. Chem. , vol.276 , pp. 39067-39075
    • Hales, C.M.1    Griner, R.2    Hobdy-Henderson, K.C.3    Dorn, M.C.4    Hardy, D.5
  • 73
    • 0037184989 scopus 로고    scopus 로고
    • Rab11 family interacting protein 2 associates with myosin Vb and regulates plasma membrane recycling
    • Hales CM, Vaerman JP, Goldenring JR. 2002. Rab11 family interacting protein 2 associates with myosin Vb and regulates plasma membrane recycling. J. Biol. Chem. 277:50415-21
    • (2002) J. Biol. Chem. , vol.277 , pp. 50415-50421
    • Hales, C.M.1    Vaerman, J.P.2    Goldenring, J.R.3
  • 74
    • 0030134132 scopus 로고    scopus 로고
    • Bud10p directs axial cell polarization in budding yeast and resembles a transmembrane receptor
    • Halme A, Michelitch M, Mitchell EL, Chant J. 1996. Bud10p directs axial cell polarization in budding yeast and resembles a transmembrane receptor. Curr. Biol. 6:570-79
    • (1996) Curr. Biol. , vol.6 , pp. 570-579
    • Halme, A.1    Michelitch, M.2    Mitchell, E.L.3    Chant, J.4
  • 75
    • 0036468368 scopus 로고    scopus 로고
    • Rabs grab motors: Defining the connections between Rab GTPases and motor proteins
    • Hammer JA 3rd, Wu XS. 2002. Rabs grab motors: defining the connections between Rab GTPases and motor proteins. Curr. Opin. Cell Biol. 14:69-75
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 69-75
    • Hammer III, J.A.1    Wu, X.S.2
  • 76
    • 0035158558 scopus 로고    scopus 로고
    • Bud8p and Bud9p, proteins that may mark the sites for bipolar budding in yeast
    • Harkins HA, Page N, Schenkman LR, De Virgilio C, Shaw S, et al. 2001. Bud8p and Bud9p, proteins that may mark the sites for bipolar budding in yeast. Mol. Biol. Cell 12:2497-518
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2497-2518
    • Harkins, H.A.1    Page, N.2    Schenkman, L.R.3    De Virgilio, C.4    Shaw, S.5
  • 77
    • 0034017607 scopus 로고    scopus 로고
    • Dynein-dependent movements of the mitotic spindle in Saccharomyces cerevisiae do not require filamentous actin
    • Heil-Chapdelaine RA, Tran NK, Cooper JA. 2000. Dynein-dependent movements of the mitotic spindle in Saccharomyces cerevisiae do not require filamentous actin. Mol. Biol. Cell 11:863-72
    • (2000) Mol. Biol. Cell , vol.11 , pp. 863-872
    • Heil-Chapdelaine, R.A.1    Tran, N.K.2    Cooper, J.A.3
  • 78
    • 0030951615 scopus 로고    scopus 로고
    • The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton
    • Hermann GJ, King EJ, Shaw JM. 1997. The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton. J. Cell Biol. 137:141-53
    • (1997) J. Cell Biol. , vol.137 , pp. 141-153
    • Hermann, G.J.1    King, E.J.2    Shaw, J.M.3
  • 80
    • 0030470182 scopus 로고    scopus 로고
    • Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae
    • Hill KL, Catlett NL, Weisman LS. 1996. Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae. J. Cell Biol. 135:1535-49
    • (1996) J. Cell Biol. , vol.135 , pp. 1535-1549
    • Hill, K.L.1    Catlett, N.L.2    Weisman, L.S.3
  • 81
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • Hoepfner D, van den Berg M, Philippsen P, Tabak HF, Hettema EH. 2001. A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J. Cell Biol. 155:979-90
    • (2001) J. Cell Biol. , vol.155 , pp. 979-990
    • Hoepfner, D.1    Van Den Berg, M.2    Philippsen, P.3    Tabak, H.F.4    Hettema, E.H.5
  • 82
    • 0031947483 scopus 로고    scopus 로고
    • The role of the dynactin complex in intracellular motility
    • Holleran EA, Karki S, Holzbaur EL. 1998. The role of the dynactin complex in intracellular motility. Int. Rev. Cytol. 182:69-109
    • (1998) Int. Rev. Cytol. , vol.182 , pp. 69-109
    • Holleran, E.A.1    Karki, S.2    Holzbaur, E.L.3
  • 83
    • 0033590558 scopus 로고    scopus 로고
    • Direct interaction of microtubule- and actin-based transport motors
    • Huang JD, Brady ST, Richards BW, Stenolen D, Resau JH, et al. 1999. Direct interaction of microtubule- and actin-based transport motors. Nature 397:267-70
    • (1999) Nature , vol.397 , pp. 267-270
    • Huang, J.D.1    Brady, S.T.2    Richards, B.W.3    Stenolen, D.4    Resau, J.H.5
  • 84
    • 0023794908 scopus 로고
    • Diverse effects of beta-tubulin mutations on microtubule formation and function
    • Huffaker TC, Thomas JH, Botstein D. 1988. Diverse effects of beta-tubulin mutations on microtubule formation and function. J. Cell Biol. 106:1997-2010
    • (1988) J. Cell Biol. , vol.106 , pp. 1997-2010
    • Huffaker, T.C.1    Thomas, J.H.2    Botstein, D.3
  • 85
    • 0036099629 scopus 로고    scopus 로고
    • The leaden gene product is required with Rab27a to recruit myosin Va to melanosomes in melanocytes
    • Hume AN, Collinson LM, Hopkins CR, Strom M, Barral DC, et al. 2002. The leaden gene product is required with Rab27a to recruit myosin Va to melanosomes in melanocytes. Traffic 3:193-202
    • (2002) Traffic , vol.3 , pp. 193-202
    • Hume, A.N.1    Collinson, L.M.2    Hopkins, C.R.3    Strom, M.4    Barral, D.C.5
  • 87
    • 0037508893 scopus 로고    scopus 로고
    • Spindle orientation in Saccharomyces cerevisiae depends on the transport of microtubule ends along polarized actin cables
    • Hwang E, Kusch J, Barral Y, Huffaker TC. 2003. Spindle orientation in Saccharomyces cerevisiae depends on the transport of microtubule ends along polarized actin cables. J. Cell Biol. 161:483-88
    • (2003) J. Cell Biol. , vol.161 , pp. 483-488
    • Hwang, E.1    Kusch, J.2    Barral, Y.3    Huffaker, T.C.4
  • 88
    • 0030044425 scopus 로고    scopus 로고
    • Genetic analysis of the Saccharomyces cerevisiae RHO3 gene, encoding a rho-type small GTPase, provides evidence for a role in bud formation
    • Imai J, Toh-e A, Matsui Y. 1996. Genetic analysis of the Saccharomyces cerevisiae RHO3 gene, encoding a rho-type small GTPase, provides evidence for a role in bud formation. Genetics 142:359-69
    • (1996) Genetics , vol.142 , pp. 359-369
    • Imai, J.1    Toh-e, A.2    Matsui, Y.3
  • 89
    • 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, et al. 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. 16:2745-55
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5
  • 92
    • 0036839610 scopus 로고    scopus 로고
    • Complex formation with Ypt11p, a rab-type small GTPase, is essential to facilitate the function of Myo2p, a class V myosin, in mitochondrial distribution in Saccharomyces cerevisiae
    • Itoh T, Watabe A, Toh EA, Matsui Y. 2002. Complex formation with Ypt11p, a rab-type small GTPase, is essential to facilitate the function of Myo2p, a class V myosin, in mitochondrial distribution in Saccharomyces cerevisiae. Mol. Cell Biol. 22:7744-57
    • (2002) Mol. Cell Biol. , vol.22 , pp. 7744-7757
    • Itoh, T.1    Watabe, A.2    Toh, E.A.3    Matsui, Y.4
  • 93
    • 0642336802 scopus 로고    scopus 로고
    • Cell biology. Smurfing at the leading edge
    • Jaffe AB, Hall A. 2003. Cell biology. Smurfing at the leading edge. Science 302:1690-91
    • (2003) Science , vol.302 , pp. 1690-1691
    • Jaffe, A.B.1    Hall, A.2
  • 94
    • 0029981258 scopus 로고    scopus 로고
    • Mother cell-specific HO expression in budding yeast depends on the unconventional myosin myo4p and other cytoplasmic proteins
    • Jansen RP, Dowzer C, Michaelis C, Galova M, Nasmyth K. 1996. Mother cell-specific HO expression in budding yeast depends on the unconventional myosin myo4p and other cytoplasmic proteins. Cell 84:687-97
    • (1996) Cell , vol.84 , pp. 687-697
    • Jansen, R.P.1    Dowzer, C.2    Michaelis, C.3    Galova, M.4    Nasmyth, K.5
  • 95
    • 0033846845 scopus 로고    scopus 로고
    • Gic2p may link activated Cdc42p to components involved in actin polarization, including Bni1p and Bud6p (Aip3p)
    • Jaquenoud M, Peter M. 2000. Gic2p may link activated Cdc42p to components involved in actin polarization, including Bni1p and Bud6p (Aip3p). Mol. Cell Biol. 20:6244-58
    • (2000) Mol. Cell Biol. , vol.20 , pp. 6244-6258
    • Jaquenoud, M.1    Peter, M.2
  • 96
    • 0030969912 scopus 로고    scopus 로고
    • Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment
    • Jedd G, Mulholland J, Segev N. 1997. Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment. J. Cell Biol. 137:563-80
    • (1997) J. Cell Biol. , vol.137 , pp. 563-580
    • Jedd, G.1    Mulholland, J.2    Segev, N.3
  • 97
    • 0033007293 scopus 로고    scopus 로고
    • Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity. Microbiol
    • Johnson DI. 1999. Cdc42: an essential Rho-type GTPase controlling eukaryotic cell polarity. Microbiol. Mol. Biol. Rev. 63:54-105
    • (1999) Mol. Biol. Rev. , vol.63 , pp. 54-105
    • Johnson, D.I.1
  • 98
    • 0025363198 scopus 로고
    • Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity
    • Johnson DI, Pringle JR. 1990. Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111:143-52
    • (1990) J. Cell Biol. , vol.111 , pp. 143-152
    • Johnson, D.I.1    Pringle, J.R.2
  • 99
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston GC, Prendergast JA, Singer RA. 1991. The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113:539-51
    • (1991) J. Cell Biol. , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, R.A.3
  • 100
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen M, Sun Y, Drubin DG. 2003. A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115:475-87
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 101
    • 0035906952 scopus 로고    scopus 로고
    • A GDP/GTP exchange factor involved in linking a spatial landmark to cell polarity
    • Kang PJ, Sanson A, Lee B, Park HO. 2001. A GDP/GTP exchange factor involved in linking a spatial landmark to cell polarity. Science 292:1376-78
    • (2001) Science , vol.292 , pp. 1376-1378
    • Kang, P.J.1    Sanson, A.2    Lee, B.3    Park, H.O.4
  • 102
    • 0032555918 scopus 로고    scopus 로고
    • Assembly and function of the actin cytoskeleton of yeast: Relationships between cables and patches
    • Karpova TS, McNally JG, Moltz SL, Cooper JA. 1998. Assembly and function of the actin cytoskeleton of yeast: relationships between cables and patches. J. Cell Biol. 142:1501-17
    • (1998) J. Cell Biol. , vol.142 , pp. 1501-1517
    • Karpova, T.S.1    McNally, J.G.2    Moltz, S.L.3    Cooper, J.A.4
  • 106
    • 0033604447 scopus 로고    scopus 로고
    • An FH domain-containing Bnr1p is a multifunctional protein interacting with a variety of cytoskeletal proteins in Saccharomyces cerevisiae
    • Kikyo M, Tanaka K, Kamei T, Ozaki K, Fujiwara T, et al. 1999. An FH domain-containing Bnr1p is a multifunctional protein interacting with a variety of cytoskeletal proteins in Saccharomyces cerevisiae. Oncogene 18:7046-54
    • (1999) Oncogene , vol.18 , pp. 7046-7054
    • Kikyo, M.1    Tanaka, K.2    Kamei, T.3    Ozaki, K.4    Fujiwara, T.5
  • 107
    • 0021369651 scopus 로고
    • Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces
    • Kilmartin JV, Adams AE. 1984. Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces. J. Cell Biol. 98:922-33
    • (1984) J. Cell Biol. , vol.98 , pp. 922-933
    • Kilmartin, J.V.1    Adams, A.E.2
  • 108
    • 1342310742 scopus 로고    scopus 로고
    • Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
    • Kobielak A, Pasolli HA, Fuchs E. 2004. Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables. Nat. Cell Biol. 6:21-30
    • (2004) Nat. Cell Biol. , vol.6 , pp. 21-30
    • Kobielak, A.1    Pasolli, H.A.2    Fuchs, E.3
  • 109
    • 10544228528 scopus 로고    scopus 로고
    • Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae
    • Kohno H, Tanaka K, Mino A, Umikawa M, Imamura H, et al. 1996. Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15:6060-68
    • (1996) EMBO J. , vol.15 , pp. 6060-6068
    • Kohno, H.1    Tanaka, K.2    Mino, A.3    Umikawa, M.4    Imamura, H.5
  • 110
    • 0034708459 scopus 로고    scopus 로고
    • Molecular linkage underlying microtubule orientation toward cortical sites in yeast
    • Korinek WS, Copeland MJ, Chaudhuri A, Chant J. 2000. Molecular linkage underlying microtubule orientation toward cortical sites in yeast. Science 287:2257-59
    • (2000) Science , vol.287 , pp. 2257-2259
    • Korinek, W.S.1    Copeland, M.J.2    Chaudhuri, A.3    Chant, J.4
  • 111
    • 0344012472 scopus 로고    scopus 로고
    • Interaction between a Ras and a Rho GTPase couples selection of a growth site to the development of cell polarity in yeast
    • Kozminski KG, Beven L, Angerman E, Tong AH, Boone C, Park HO. 2003. Interaction between a Ras and a Rho GTPase couples selection of a growth site to the development of cell polarity in yeast. Mol. Biol. Cell 14:4958-70
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4958-4970
    • Kozminski, K.G.1    Beven, L.2    Angerman, E.3    Tong, A.H.4    Boone, C.5    Park, H.O.6
  • 113
    • 0037148524 scopus 로고    scopus 로고
    • Modulation of substrate adhesion dynamics via microtubule targeting requires kinesin-1
    • Krylyshkina O, Kaverina I, Kranewitter W, Steffen W, Alonso MC, et al. 2002. Modulation of substrate adhesion dynamics via microtubule targeting requires kinesin-1. J. Cell Biol. 156:349-59
    • (2002) J. Cell Biol. , vol.156 , pp. 349-359
    • Krylyshkina, O.1    Kaverina, I.2    Kranewitter, W.3    Steffen, W.4    Alonso, M.C.5
  • 114
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kubler E, Riezman H. 1993. Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12:2855-62
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kubler, E.1    Riezman, H.2
  • 115
    • 0027964421 scopus 로고
    • Nuclear congression and membrane fusion: Two distinct events in the yeast karyogamy pathway
    • Kurihara LJ, Beh CT, Latterich M, Schekman R, Rose MD. 1994. Nuclear congression and membrane fusion: two distinct events in the yeast karyogamy pathway. J. Cell Biol. 126:911-23
    • (1994) J. Cell Biol. , vol.126 , pp. 911-923
    • Kurihara, L.J.1    Beh, C.T.2    Latterich, M.3    Schekman, R.4    Rose, M.D.5
  • 116
    • 0043093725 scopus 로고    scopus 로고
    • The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes
    • Kuroda TS, Ariga H, Fukuda M. 2003. The actin-binding domain of Slac2-a/melanophilin is required for melanosome distribution in melanocytes. Mol. Cell Biol. 23:5245-55
    • (2003) Mol. Cell Biol. , vol.23 , pp. 5245-5255
    • Kuroda, T.S.1    Ariga, H.2    Fukuda, M.3
  • 117
    • 0036645506 scopus 로고    scopus 로고
    • Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast
    • Kusch J, Meyer A, Snyder MP, Barral Y. 2002. Microtubule capture by the cleavage apparatus is required for proper spindle positioning in yeast. Genes Dev. 16:1627-39
    • (2002) Genes Dev. , vol.16 , pp. 1627-1639
    • Kusch, J.1    Meyer, A.2    Snyder, M.P.3    Barral, Y.4
  • 120
    • 0034708606 scopus 로고    scopus 로고
    • Positioning of the mitotic spindle by a cortical-microtubule capture mechanism
    • Lee L, Tirnauer JS, Li J, Schuyler SC, Liu JY, Pellman D. 2000. Positioning of the mitotic spindle by a cortical-microtubule capture mechanism. Science 287:2260-62
    • (2000) Science , vol.287 , pp. 2260-2262
    • Lee, L.1    Tirnauer, J.S.2    Li, J.3    Schuyler, S.C.4    Liu, J.Y.5    Pellman, D.6
  • 121
    • 0037415644 scopus 로고    scopus 로고
    • The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast
    • Lee WL, Oberle JR, Cooper JA. 2003. The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast. J. Cell Biol. 160:355-64
    • (2003) J. Cell Biol. , vol.160 , pp. 355-364
    • Lee, W.L.1    Oberle, J.R.2    Cooper, J.A.3
  • 122
    • 0346155805 scopus 로고    scopus 로고
    • The spindle assembly and spindle position checkpoints
    • Lew DJ, Burke DJ. 2003. The spindle assembly and spindle position checkpoints. Annu. Rev. Genet. 37:251-82
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 251-282
    • Lew, D.J.1    Burke, D.J.2
  • 123
    • 0028915943 scopus 로고
    • A cell cycle checkpoint monitors cell morphogenesis in budding yeast
    • Lew DJ, Reed SI. 1995. A cell cycle checkpoint monitors cell morphogenesis in budding yeast. J. Cell Biol. 129:739-49
    • (1995) J. Cell Biol. , vol.129 , pp. 739-749
    • Lew, D.J.1    Reed, S.I.2
  • 124
    • 0043202969 scopus 로고    scopus 로고
    • The mouse Formin mDial is a potent actin nucleation factor regulated by autoinhibition
    • Li F, Higgs HN. 2003. The mouse Formin mDial is a potent actin nucleation factor regulated by autoinhibition. Curr. Biol. 13:1335-40
    • (2003) Curr. Biol. , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 125
    • 0028871169 scopus 로고
    • Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast
    • Li R, Zheng Y, Drubin DG. 1995. Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast. J. Cell Biol. 128:599-615
    • (1995) J. Cell Biol. , vol.128 , pp. 599-615
    • Li, R.1    Zheng, Y.2    Drubin, D.G.3
  • 126
    • 0027453547 scopus 로고
    • Disruption of mitotic spindle orientation in a yeast dynein mutant
    • Li YY, Yeh E, Hays T, Bloom K. 1993. Disruption of mitotic spindle orientation in a yeast dynein mutant. Proc. Natl. Acad. Sci. USA 90:10096-100
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10096-10100
    • Li, Y.Y.1    Yeh, E.2    Hays, T.3    Bloom, K.4
  • 127
    • 0037459058 scopus 로고    scopus 로고
    • Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment
    • Liakopoulos D, Kusch J, Grava S, Vogel J, Barral Y. 2003. Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment. Cell 112:561-74
    • (2003) Cell , vol.112 , pp. 561-574
    • Liakopoulos, D.1    Kusch, J.2    Grava, S.3    Vogel, J.4    Barral, Y.5
  • 128
    • 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 SH, Brown SS. 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. 125:825-42
    • (1994) J. Cell Biol. , vol.125 , pp. 825-842
    • Lillie, S.H.1    Brown, S.S.2
  • 129
    • 0032559545 scopus 로고    scopus 로고
    • Smy1p, a kinesin-related protein that does not require microtubules
    • Lillie SH, Brown SS. 1998. Smy1p, a kinesin-related protein that does not require microtubules. J. Cell Biol. 140:873-83
    • (1998) J. Cell Biol. , vol.140 , pp. 873-883
    • Lillie, S.H.1    Brown, S.S.2
  • 130
    • 0035945345 scopus 로고    scopus 로고
    • Polyploids require Bik1 for kinetochore-microtubule attachment
    • Lin H, de Carvalho P, Kho D, Tai CY, Pierre P, et al. 2001. Polyploids require Bik1 for kinetochore-microtubule attachment. J. Cell Biol. 155:1173-84
    • (2001) J. Cell Biol. , vol.155 , pp. 1173-1184
    • Lin, H.1    De Carvalho, P.2    Kho, D.3    Tai, C.Y.4    Pierre, P.5
  • 131
    • 0037178832 scopus 로고    scopus 로고
    • Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain
    • Lindsay AJ, McCaffrey MW. 2002. Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain. J. Biol. Chem. 277:27193-99
    • (2002) J. Biol. Chem. , vol.277 , pp. 27193-27199
    • Lindsay, A.J.1    McCaffrey, M.W.2
  • 132
    • 0001647625 scopus 로고    scopus 로고
    • Exocytosis: The many masters of the exocyst
    • Lipschutz JH, Mostov KE. 2002. Exocytosis: the many masters of the exocyst. Curr. Biol. 12:R212-14
    • (2002) Curr. Biol. , vol.12
    • Lipschutz, J.H.1    Mostov, K.E.2
  • 133
    • 0024516197 scopus 로고
    • Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton
    • Liu HP, Bretscher A. 1989. Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton. Cell 57:233-42
    • (1989) Cell , vol.57 , pp. 233-242
    • Liu, H.P.1    Bretscher, A.2
  • 134
    • 0037031155 scopus 로고    scopus 로고
    • Subcellular localization of Axl1, the cell type-specific regulator of polarity
    • Lord M, Inose F, Hiroko T, Hata T, Fujita A, Chant J. 2002. Subcellular localization of Axl1, the cell type-specific regulator of polarity. Curr. Biol. 12:1347-52
    • (2002) Curr. Biol. , vol.12 , pp. 1347-1352
    • Lord, M.1    Inose, F.2    Hiroko, T.3    Hata, T.4    Fujita, A.5    Chant, J.6
  • 135
    • 0030707797 scopus 로고    scopus 로고
    • Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous
    • Lynch ED, Lee MK, Morrow JE, Welcsh PL, Leon PE, King MC. 1997. Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous. Science 278:1315-18
    • (1997) Science , vol.278 , pp. 1315-1318
    • Lynch, E.D.1    Lee, M.K.2    Morrow, J.E.3    Welcsh, P.L.4    Leon, P.E.5    King, M.C.6
  • 136
    • 0023293818 scopus 로고
    • Characterization of two members of the rho gene family from the yeast Saccharomyces cerevisiae
    • Madaule P, Axel R, Myers AM. 1987. Characterization of two members of the rho gene family from the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 84:779-83
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 779-783
    • Madaule, P.1    Axel, R.2    Myers, A.M.3
  • 137
    • 0037415689 scopus 로고    scopus 로고
    • Yeast Cdk1 translocates to the plus end of cytoplasmic microtubules to regulate bud cortex interactions
    • Maekawa H, Usui T, Knop M, Schiebel E. 2003. Yeast Cdk1 translocates to the plus end of cytoplasmic microtubules to regulate bud cortex interactions. EMBO J. 22:438-49
    • (2003) EMBO J. , vol.22 , pp. 438-449
    • Maekawa, H.1    Usui, T.2    Knop, M.3    Schiebel, E.4
  • 138
    • 0035873848 scopus 로고    scopus 로고
    • A localized GTPase exchange factor, Bud5, determines the orientation of division axes in yeast
    • Marston AL, Chen T, Yang MC, Belhumeur P, Chant J. 2001. A localized GTPase exchange factor, Bud5, determines the orientation of division axes in yeast. Curr. Biol. 11:803-7
    • (2001) Curr. Biol. , vol.11 , pp. 803-807
    • Marston, A.L.1    Chen, T.2    Yang, M.C.3    Belhumeur, P.4    Chant, J.5
  • 139
    • 0035964395 scopus 로고    scopus 로고
    • Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice
    • Matesic LE, Yip R, Reuss AE, Swing DA, O'Sullivan TN, et al. 2001. Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice. Proc. Natl. Acad. Sci. USA 98:10238-43
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10238-10243
    • Matesic, L.E.1    Yip, R.2    Reuss, A.E.3    Swing, D.A.4    O'Sullivan, T.N.5
  • 140
    • 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 BEM1
    • Matsui Y, Toh EA. 1992. 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 BEM1. Mol. Cell Biol. 12: 5690-99
    • (1992) Mol. Cell Biol. , vol.12 , pp. 5690-5699
    • Matsui, Y.1    Toh, E.A.2
  • 141
    • 0344002689 scopus 로고    scopus 로고
    • Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome
    • Menasche G, Pastural E, Feldmann J, Certain S, Ersoy F, et al. 2000. Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Nat. Genet. 25:173-76
    • (2000) Nat. Genet. , vol.25 , pp. 173-176
    • Menasche, G.1    Pastural, E.2    Feldmann, J.3    Certain, S.4    Ersoy, F.5
  • 143
    • 0030113924 scopus 로고    scopus 로고
    • A mechanism of Bud1p GTPase action suggested by mutational analysis and immunolocalization
    • Michelitch M, Chant J. 1996. A mechanism of Bud1p GTPase action suggested by mutational analysis and immunolocalization. Curr. Biol. 6:446-54
    • (1996) Curr. Biol. , vol.6 , pp. 446-454
    • Michelitch, M.1    Chant, J.2
  • 144
    • 0034490532 scopus 로고    scopus 로고
    • Bim1p/Yeb1p mediates the Kar9p-dependent cortical attachment of cytoplasmic microtubules
    • Miller RK, Cheng SC, Rose MD. 2000. Bim1p/Yeb1p mediates the Kar9p-dependent cortical attachment of cytoplasmic microtubules. Mol. Biol. Cell 11:2949-59
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2949-2959
    • Miller, R.K.1    Cheng, S.C.2    Rose, M.D.3
  • 145
    • 0032567757 scopus 로고    scopus 로고
    • Kar9p is a novel cortical protein required for cytoplasmic microtubule orientation in yeast
    • Miller RK, Rose MD. 1998. Kar9p is a novel cortical protein required for cytoplasmic microtubule orientation in yeast. J. Cell Biol. 140:377-90
    • (1998) J. Cell Biol. , vol.140 , pp. 377-390
    • Miller, R.K.1    Rose, M.D.2
  • 146
    • 0034644119 scopus 로고    scopus 로고
    • The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules
    • Mimori-Kiyosue Y, Shiina N, Tsukita S. 2000. The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules. Curr. Biol. 10:865-68
    • (2000) Curr. Biol. , vol.10 , pp. 865-868
    • Mimori-Kiyosue, Y.1    Shiina, N.2    Tsukita, S.3
  • 148
    • 0034689026 scopus 로고    scopus 로고
    • Nuclear migration. From fungi to the mammalian brain
    • Morris NR. 2000. Nuclear migration. From fungi to the mammalian brain. J. Cell Biol. 148:1097-101
    • (2000) J. Cell Biol. , vol.148 , pp. 1097-1101
    • Morris, N.R.1
  • 149
    • 0742305302 scopus 로고    scopus 로고
    • A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin
    • Moseley JB, Sagot I, Manning AL, Xu Y, Eck MJ, et al. 2004. A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin. Mol. Biol. Cell 15:896-907
    • (2004) Mol. Biol. Cell , vol.15 , pp. 896-907
    • Moseley, J.B.1    Sagot, I.2    Manning, A.L.3    Xu, Y.4    Eck, M.J.5
  • 150
    • 0028025571 scopus 로고
    • A yeast actin-related protein homologous to that in vertebrate dynactin complex is important for spindle orientation and nuclear migration
    • Muhua L, Karpova TS, Cooper JA. 1994. A yeast actin-related protein homologous to that in vertebrate dynactin complex is important for spindle orientation and nuclear migration. Cell 78:669-79
    • (1994) Cell , vol.78 , pp. 669-679
    • Muhua, L.1    Karpova, T.S.2    Cooper, J.A.3
  • 151
    • 0028856410 scopus 로고
    • end5, end6, and end7: Mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae
    • Munn AL, Stevenson BJ, Geli MI, 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 6:1721-42
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1721-1742
    • Munn, A.L.1    Stevenson, B.J.2    Geli, M.I.3    Riezman, H.4
  • 152
    • 0037165662 scopus 로고    scopus 로고
    • Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions
    • Nagashima K, Torii S, Yi Z, Igarashi M, Okamoto K, et al. 2002. Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett. 517:233-38
    • (2002) FEBS Lett. , vol.517 , pp. 233-238
    • Nagashima, K.1    Torii, S.2    Yi, Z.3    Igarashi, M.4    Okamoto, K.5
  • 153
    • 0033593974 scopus 로고    scopus 로고
    • A Cdc24p-Far1p-Gβγ protein complex required for yeast orientation during mating
    • Nern A, Arkowitz RA. 1999. A Cdc24p-Far1p-Gβγ protein complex required for yeast orientation during mating. J. Cell Biol. 144:1187-202
    • (1999) J. Cell Biol. , vol.144 , pp. 1187-1202
    • Nern, A.1    Arkowitz, R.A.2
  • 154
    • 0034688998 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the Cdc42p exchange factor Cdc24p
    • Nern A, Arkowitz RA. 2000. Nucleocytoplasmic shuttling of the Cdc42p exchange factor Cdc24p. J. Cell Biol. 148:1115-22
    • (2000) J. Cell Biol. , vol.148 , pp. 1115-1122
    • Nern, A.1    Arkowitz, R.A.2
  • 155
    • 0021906692 scopus 로고
    • Phenotypic analysis of temperature-sensitive yeast actin mutants
    • Novick P, Botstein D. 1985. Phenotypic analysis of temperature-sensitive yeast actin mutants. Cell 40:405-16
    • (1985) Cell , vol.40 , pp. 405-416
    • Novick, P.1    Botstein, D.2
  • 156
    • 0037054540 scopus 로고    scopus 로고
    • Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast
    • Ortiz D, Medkova M, Walch-Solimena C, Novick P. 2002. Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast. J. Cell Biol. 157:1005-15
    • (2002) J. Cell Biol. , vol.157 , pp. 1005-1015
    • Ortiz, D.1    Medkova, M.2    Walch-Solimena, C.3    Novick, P.4
  • 157
    • 0035137208 scopus 로고    scopus 로고
    • Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae
    • Ozaki-Kuroda K, Yamamoto Y, Nohara H, Kinoshita M, Fujiwara T, et al. 2001. Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae. Mol. Cell Biol. 21:827-39
    • (2001) Mol. Cell Biol. , vol.21 , pp. 827-839
    • Ozaki-Kuroda, K.1    Yamamoto, Y.2    Nohara, H.3    Kinoshita, M.4    Fujiwara, T.5
  • 158
    • 0026781163 scopus 로고
    • Role of astral microtubules and actin in spindle orientation and migration in the budding yeast, Saccharomyces cerevisiae
    • Palmer RE, Sullivan DS, Huffaker T, Koshland D. 1992. Role of astral microtubules and actin in spindle orientation and migration in the budding yeast, Saccharomyces cerevisiae. J. Cell Biol. 119:583-93
    • (1992) J. Cell Biol. , vol.119 , pp. 583-593
    • Palmer, R.E.1    Sullivan, D.S.2    Huffaker, T.3    Koshland, D.4
  • 159
    • 0030940119 scopus 로고    scopus 로고
    • Two active states of the Ras-related Bud1/Rsr1 protein bind to different effectors to determine yeast cell polarity
    • Park HO, Bi E, Pringle JR, Herskowitz I. 1997. Two active states of the Ras-related Bud1/Rsr1 protein bind to different effectors to determine yeast cell polarity. Proc. Natl. Acad. Sci. USA 94:4463-68
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4463-4468
    • Park, H.O.1    Bi, E.2    Pringle, J.R.3    Herskowitz, I.4
  • 160
    • 0027264558 scopus 로고
    • BUD2 encodes a GTPase-activating protein for Bud1/Rsr1 necessary for proper bud-site selection in yeast
    • Park HO, Chant J, Herskowitz I. 1993. BUD2 encodes a GTPase-activating protein for Bud1/Rsr1 necessary for proper bud-site selection in yeast. Nature 365:269-74
    • (1993) Nature , vol.365 , pp. 269-274
    • Park, H.O.1    Chant, J.2    Herskowitz, I.3
  • 161
    • 0037178792 scopus 로고    scopus 로고
    • Localization of the Rsr1/Bud1 GTPase involved in selection of a proper growth site in yeast
    • Park HO, Kang PJ, Rachfal AW. 2002. Localization of the Rsr1/Bud1 GTPase involved in selection of a proper growth site in yeast. J. Biol. Chem. 277:26721-24
    • (2002) J. Biol. Chem. , vol.277 , pp. 26721-26724
    • Park, H.O.1    Kang, P.J.2    Rachfal, A.W.3
  • 162
    • 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 HO, Sanson A, Herskowitz I. 1999. Localization of bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site. Genes Dev. 13:1912-17
    • (1999) Genes Dev. , vol.13 , pp. 1912-1917
    • Park, H.O.1    Sanson, A.2    Herskowitz, I.3
  • 163
    • 0030914460 scopus 로고    scopus 로고
    • Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene
    • Pastural E, Barrat FJ, Dufourcq-Lagelouse R, Certain S, Sanal O, et al. 1997. Griscelli disease maps to chromosome 15q21 and is associated with mutations in the myosin-Va gene. Nat. Genet. 16:289-92
    • (1997) Nat. Genet. , vol.16 , pp. 289-292
    • Pastural, E.1    Barrat, F.J.2    Dufourcq-Lagelouse, R.3    Certain, S.4    Sanal, O.5
  • 164
    • 0028148453 scopus 로고
    • Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast
    • Peterson J, Zheng Y, Bender L, Myers A, Cerione R, Bender A. 1994. Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast. J. Cell Biol. 127:1395-406
    • (1994) J. Cell Biol. , vol.127 , pp. 1395-1406
    • Peterson, J.1    Zheng, Y.2    Bender, L.3    Myers, A.4    Cerione, R.5    Bender, A.6
  • 165
    • 0026793891 scopus 로고
    • CLIP-170 links endocytic vesicles to microtubules
    • Pierre P, Scheel J, Rickard JE, Kreis TE. 1992. CLIP-170 links endocytic vesicles to microtubules. Cell 70:887-900
    • (1992) Cell , vol.70 , pp. 887-900
    • Pierre, P.1    Scheel, J.2    Rickard, J.E.3    Kreis, T.E.4
  • 166
    • 0030921711 scopus 로고    scopus 로고
    • 2+-dependent interaction with the sy naptobrevin- synaptophysin complex
    • 2+-dependent interaction with the sy naptobrevin-synaptophysin complex. J. Cell Biol. 137:1589-601
    • (1997) J. Cell Biol. , vol.137 , pp. 1589-1601
    • Prekeris, R.1    Terrian, D.M.2
  • 167
    • 0027056183 scopus 로고
    • Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy
    • Preuss D, Mulholland J, Franzusoff A, Segev N, Botstein D. 1992. Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy. Mol. Biol. Cell 3:789-803
    • (1992) Mol. Biol. Cell , vol.3 , pp. 789-803
    • Preuss, D.1    Mulholland, J.2    Franzusoff, A.3    Segev, N.4    Botstein, D.5
  • 168
    • 0026335172 scopus 로고
    • Structure of the yeast endoplasmic reticulum: Localization of ER proteins using immunofluorescence and immunoelectron microscopy
    • Preuss D, Mulholland J, Kaiser CA, Orlean P, Albright C, et al. 1991. Structure of the yeast endoplasmic reticulum: localization of ER proteins using immunofluorescence and immunoelectron microscopy. Yeast 7:891-911
    • (1991) Yeast , vol.7 , pp. 891-911
    • Preuss, D.1    Mulholland, J.2    Kaiser, C.A.3    Orlean, P.4    Albright, C.5
  • 170
    • 0036107354 scopus 로고    scopus 로고
    • Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes
    • Provance DW, James TL, Mercer JA. 2002. Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes. Traffic 3:124-32
    • (2002) Traffic , vol.3 , pp. 124-132
    • Provance, D.W.1    James, T.L.2    Mercer, J.A.3
  • 171
    • 0034002965 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast. II. The role of the cortical actin cytoskeleton
    • Pruyne D, Bretscher A. 2000. Polarization of cell growth in yeast. II. The role of the cortical actin cytoskeleton. J. Cell Sci. 113:365-75
    • (2000) J. Cell Sci. , vol.113 , pp. 365-375
    • Pruyne, D.1    Bretscher, A.2
  • 172
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed end association
    • Pruyne D, Evangelista M, Yang C, Bi E, Zigmond S, et al. 2002. Role of formins in actin assembly: nucleation and barbed end association. Science 297:612-15
    • (2002) Science , vol.297 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5
  • 173
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • Pruyne DW, Schott DH, Bretscher A. 1998. Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J. Cell Biol. 143:1931-45
    • (1998) J. Cell Biol. , vol.143 , pp. 1931-1945
    • Pruyne, D.W.1    Schott, D.H.2    Bretscher, A.3
  • 174
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosisin Saccharomyces cerevisiae
    • Raths S, Rohrer J, Crausaz F, Riezman H. 1993. end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosisin 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
  • 176
    • 0036500526 scopus 로고    scopus 로고
    • Human myosin-Vc is a novel class V myosin expressed in epithelial cells
    • Rodriguez OC, Cheney RE. 2002. Human myosin-Vc is a novel class V myosin expressed in epithelial cells. J. Cell Sci. 115:991-1004
    • (2002) J. Cell Sci. , vol.115 , pp. 991-1004
    • Rodriguez, O.C.1    Cheney, R.E.2
  • 177
    • 0029995116 scopus 로고    scopus 로고
    • Selection of axial growth sites in yeast requires Axl2p, a novel plasma membrane glycoprotein
    • Roemer T, Madden K, Chang J, Snyder M. 1996. Selection of axial growth sites in yeast requires Axl2p, a novel plasma membrane glycoprotein. Genes Dev. 10:777-93
    • (1996) Genes Dev. , vol.10 , pp. 777-793
    • Roemer, T.1    Madden, K.2    Chang, J.3    Snyder, M.4
  • 178
    • 0035795423 scopus 로고    scopus 로고
    • A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae
    • Rossanese OW, Reinke CA, Bevis BJ, Hammond AT, Sears IB, et al. 2001. A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae. J. Cell Biol. 153:47-62
    • (2001) J. Cell Biol. , vol.153 , pp. 47-62
    • Rossanese, O.W.1    Reinke, C.A.2    Bevis, B.J.3    Hammond, A.T.4    Sears, I.B.5
  • 179
    • 0037383440 scopus 로고    scopus 로고
    • Myosin Va facilitates the distribution of secretory granules in the F-actin rich cortex of PC12 cells
    • Rudolf R, Kogel T, Kuznetsov SA, Salm T, Schlicker O, et al. 2003. Myosin Va facilitates the distribution of secretory granules in the F-actin rich cortex of PC12 cells. J. Cell Sci. 116:1339-48
    • (2003) J. Cell Sci. , vol.116 , pp. 1339-1348
    • Rudolf, R.1    Kogel, T.2    Kuznetsov, S.A.3    Salm, T.4    Schlicker, O.5
  • 180
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot I, Klee SK, Pellman D. 2002a. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4:42-50
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 182
    • 0023662281 scopus 로고
    • A ras-like protein is required for a post-Golgi event in yeast secretion
    • Salminen A, Novick PJ. 1987. A ras-like protein is required for a post-Golgi event in yeast secretion. Cell 49:527-38
    • (1987) Cell , vol.49 , pp. 527-538
    • Salminen, A.1    Novick, P.J.2
  • 183
    • 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, 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
  • 185
    • 0037033787 scopus 로고    scopus 로고
    • Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length
    • Schott DH, Collins RN, Bretscher A. 2002b. Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length. J. Cell Biol. 156:35-39
    • (2002) J. Cell Biol. , vol.156 , pp. 35-39
    • Schott, D.H.1    Collins, R.N.2    Bretscher, A.3
  • 186
    • 0030668145 scopus 로고    scopus 로고
    • BIM1 encodes a microtubule-binding protein in yeast
    • Schwartz K, Richards K, Botstein D. 1997. BIM1 encodes a microtubule-binding protein in yeast. Mol. Biol. Cell 8:2677-91
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2677-2691
    • Schwartz, K.1    Richards, K.2    Botstein, D.3
  • 188
    • 0037418576 scopus 로고    scopus 로고
    • Determinants of S. cerevisiae dynein localization and activation. Implications for the mechanism of spindle positioning
    • Sheeman B, Carvalho P, Sagot I, Geiser J, Kho D, et al. 2003. Determinants of S. cerevisiae dynein localization and activation. Implications for the mechanism of spindle positioning. Curr. Biol. 13:2014
    • (2003) Curr. Biol. , vol.13 , pp. 2014
    • Sheeman, B.1    Carvalho, P.2    Sagot, I.3    Geiser, J.4    Kho, D.5
  • 189
    • 0031835436 scopus 로고    scopus 로고
    • Spa2p interacts with cell polarity proteins and signaling components involved in yeast cell morphogenesis
    • Sheu YJ, Santos B, Fortin N, Costigan C, Snyder M. 1998. Spa2p interacts with cell polarity proteins and signaling components involved in yeast cell morphogenesis. Mol. Cell Biol. 18:4053-69
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4053-4069
    • Sheu, Y.J.1    Santos, B.2    Fortin, N.3    Costigan, C.4    Snyder, M.5
  • 190
    • 0033788675 scopus 로고    scopus 로고
    • Nuclear sequestration of the exchange factor Cdc24 by Far1 regulates cell polarity during yeast mating
    • Shimada Y, Gulli MP, Peter M. 2000. Nuclear sequestration of the exchange factor Cdc24 by Far1 regulates cell polarity during yeast mating. Nat. Cell Biol. 2:117-24
    • (2000) Nat. Cell Biol. , vol.2 , pp. 117-124
    • Shimada, Y.1    Gulli, M.P.2    Peter, M.3
  • 191
    • 0029864229 scopus 로고    scopus 로고
    • Identification of asymmetrically localized determinant, Ash1p, required for lineage-specific transcription of the yeast HO gene
    • Sil A, Herskowitz I. 1996. Identification of asymmetrically localized determinant, Ash1p, required for lineage-specific transcription of the yeast HO gene. Cell 84:711-22
    • (1996) Cell , vol.84 , pp. 711-722
    • Sil, A.1    Herskowitz, I.2
  • 192
    • 0030854830 scopus 로고    scopus 로고
    • Mitochondrial inheritance: Cell cycle and actin cable dependence of polarized mitochondrial movements in Saccharomyces cerevisiae
    • Simon VR, Karmon SL, Pon LA. 1997. Mitochondrial inheritance: cell cycle and actin cable dependence of polarized mitochondrial movements in Saccharomyces cerevisiae. Cell Motil. Cytoskelet. 37:199-210
    • (1997) Cell Motil. Cytoskelet. , vol.37 , pp. 199-210
    • Simon, V.R.1    Karmon, S.L.2    Pon, L.A.3
  • 193
    • 0029078227 scopus 로고
    • Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: Identification of a motor activity on the mitochondrial surface
    • Simon VR, Swayne TC, Pon LA. 1995. Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: identification of a motor activity on the mitochondrial surface. J. Cell Biol. 130:345-54
    • (1995) J. Cell Biol. , vol.130 , pp. 345-354
    • Simon, V.R.1    Swayne, T.C.2    Pon, L.A.3
  • 194
    • 0033790210 scopus 로고    scopus 로고
    • Suppressors of mdm20 in yeast identify new alleles of ACT1 and TPM1 predicted to enhance actin-tropomyosin interactions
    • Singer JM, Hermann GJ, Shaw JM. 2000. Suppressors of mdm20 in yeast identify new alleles of ACT1 and TPM1 predicted to enhance actin-tropomyosin interactions. Genetics 156:523-34
    • (2000) Genetics , vol.156 , pp. 523-534
    • Singer, J.M.1    Hermann, G.J.2    Shaw, J.M.3
  • 195
    • 0018224763 scopus 로고
    • A mutant of yeast defective in cellular morphogenesis
    • Sloat BF, Pringle JR. 1978. A mutant of yeast defective in cellular morphogenesis. Science 200:1171-73
    • (1978) Science , vol.200 , pp. 1171-1173
    • Sloat, B.F.1    Pringle, J.R.2
  • 197
    • 0037221714 scopus 로고    scopus 로고
    • Microtubules meet substrate adhesions to arrange cell polarity
    • Small JV, Kaverina I. 2003. Microtubules meet substrate adhesions to arrange cell polarity. Curr. Opin. Cell Biol. 15:40-47
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 40-47
    • Small, J.V.1    Kaverina, I.2
  • 198
    • 0031822156 scopus 로고    scopus 로고
    • Mlc1p is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae
    • Stevens RC, Davis TN. 1998. Mlc1p is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae. J. Cell Biol. 142:711-22
    • (1998) J. Cell Biol. , vol.142 , pp. 711-722
    • Stevens, R.C.1    Davis, T.N.2
  • 199
    • 0026726516 scopus 로고
    • Astral microtubules are not required for anaphase B in Saccharomyces cerevisiae
    • Sullivan DS, Huffaker TC. 1992. Astral microtubules are not required for anaphase B in Saccharomyces cerevisiae. J. Cell Biol. 119:379-88
    • (1992) J. Cell Biol. , vol.119 , pp. 379-388
    • Sullivan, D.S.1    Huffaker, T.C.2
  • 200
    • 0034672010 scopus 로고    scopus 로고
    • Asymmetrically localized Bud8p and Bud9p proteins control yeast cell polarity and development
    • Taheri N, Kohler T, Braus GH, Mosch HU. 2000. Asymmetrically localized Bud8p and Bud9p proteins control yeast cell polarity and development. EMBO J. 19:6686-96
    • (2000) EMBO J. , vol.19 , pp. 6686-6696
    • Taheri, N.1    Kohler, T.2    Braus, G.H.3    Mosch, H.U.4
  • 202
    • 0034644626 scopus 로고    scopus 로고
    • Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier
    • Takizawa PA, DeRisi JL, Wilhelm JE, Vale RD. 2000. Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Science 290:341-44
    • (2000) Science , vol.290 , pp. 341-344
    • Takizawa, P.A.1    DeRisi, J.L.2    Wilhelm, J.E.3    Vale, R.D.4
  • 203
    • 0030930836 scopus 로고    scopus 로고
    • Actin-dependent localization of an RNA encoding a cell-fate determinant in yeast
    • Takizawa PA, Sil A, Swedlow JR, Herskowitz I, Vale RD. 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.A.1    Sil, A.2    Swedlow, J.R.3    Herskowitz, I.4    Vale, R.D.5
  • 204
    • 0034625003 scopus 로고    scopus 로고
    • The myosin motor, Myo4p, binds Ash1 mRNA via the adapter protein, She3p
    • Takizawa PA, Vale RD. 2000. The myosin motor, Myo4p, binds Ash1 mRNA via the adapter protein, She3p. Proc. Natl. Acad. Sci. USA 97:5273-78
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5273-5278
    • Takizawa, P.A.1    Vale, R.D.2
  • 205
    • 0037422115 scopus 로고    scopus 로고
    • Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole
    • Tang F, Kauffman EJ, Novak JL, Nau JJ, Catlett NL, Weisman LS. 2003. Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole. Nature 422:87-92
    • (2003) Nature , vol.422 , pp. 87-92
    • Tang, F.1    Kauffman, E.J.2    Novak, J.L.3    Nau, J.J.4    Catlett, N.L.5    Weisman, L.S.6
  • 206
    • 0029843493 scopus 로고    scopus 로고
    • The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush DR, Maurice T, Roth D, Novick P. 1996. The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 15:6483-94
    • (1996) EMBO J. , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 207
    • 0032858387 scopus 로고    scopus 로고
    • The role of actin in spindle orientation changes during the Saccharomyces cerevisiae cell cycle
    • Theesfeld CL, Irazoqui JE, Bloom K, Lew DJ. 1999. The role of actin in spindle orientation changes during the Saccharomyces cerevisiae cell cycle. J. Cell Biol. 146:1019-32
    • (1999) J. Cell Biol. , vol.146 , pp. 1019-1032
    • Theesfeld, C.L.1    Irazoqui, J.E.2    Bloom, K.3    Lew, D.J.4
  • 209
    • 0033592690 scopus 로고    scopus 로고
    • The guanine-nucleotide-exchange factor Cdc24p is targeted to the nucleus and polarized growth sites
    • Toenjes KA, Sawyer MM, Johnson DI. 1999. The guanine-nucleotide-exchange factor Cdc24p is targeted to the nucleus and polarized growth sites. Curr. Biol. 9:1183-86
    • (1999) Curr. Biol. , vol.9 , pp. 1183-1186
    • Toenjes, K.A.1    Sawyer, M.M.2    Johnson, D.I.3
  • 211
    • 0034000126 scopus 로고    scopus 로고
    • Roles of Hof1p, Bni1p, Bnr1p, and Myo1p in cytokinesis in Saccharomyces cerevisiae
    • Vallen EA, Caviston J, Bi E. 2000. Roles of Hof1p, Bni1p, Bnr1p, and Myo1p in cytokinesis in Saccharomyces cerevisiae. Mol. Biol. Cell 11:593-611
    • (2000) Mol. Biol. Cell , vol.11 , pp. 593-611
    • Vallen, E.A.1    Caviston, J.2    Bi, E.3
  • 212
    • 0037112197 scopus 로고    scopus 로고
    • Rab11a and myosin Vb regulate recycling of the M4 muscarinic acetylcholine receptor
    • Volpicelli LA, Lah JJ, Fang G, Goldenring JR, Levey AI. 2002. Rab11a and myosin Vb regulate recycling of the M4 muscarinic acetylcholine receptor. J. Neurosci. 22:9776-84
    • (2002) J. Neurosci. , vol.22 , pp. 9776-9784
    • Volpicelli, L.A.1    Lah, J.J.2    Fang, G.3    Goldenring, J.R.4    Levey, A.I.5
  • 213
    • 0037011063 scopus 로고    scopus 로고
    • Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p
    • Wagner W, Bielli P, Wacha S, Ragnini-Wilson A. 2002. Mlc1p promotes septum closure during cytokinesis via the IQ motifs of the vesicle motor Myo2p. EMBO J. 21:6397-408
    • (2002) EMBO J. , vol.21 , pp. 6397-6408
    • Wagner, W.1    Bielli, P.2    Wacha, S.3    Ragnini-Wilson, A.4
  • 214
    • 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 RN, Novick PJ. 1997. Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 137:1495-509
    • (1997) J. Cell Biol. , vol.137 , pp. 1495-1509
    • Walch-Solimena, C.1    Collins, R.N.2    Novick, P.J.3
  • 215
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • Wallar BJ, Alberts AS. 2003. The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13:435-46
    • (2003) Trends Cell Biol. , vol.13 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 216
    • 0029812691 scopus 로고    scopus 로고
    • Multiple classes of yeast mutants are defective in vacuole partitioning yet target vacuole proteins correctly
    • Wang YX, Zhao H, Harding TM, Gomes de Mesquita DS, Woldringh CL, et al. 1996. Multiple classes of yeast mutants are defective in vacuole partitioning yet target vacuole proteins correctly. Mol. Biol. Cell 7:1375-89
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1375-1389
    • Wang, Y.X.1    Zhao, H.2    Harding, T.M.3    Gomes De Mesquita, D.S.4    Woldringh, C.L.5
  • 217
    • 0032031388 scopus 로고    scopus 로고
    • FH proteins as cytoskeletal organizers
    • Wasserman S. 1998. FH proteins as cytoskeletal organizers. Trends Cell Biol. 8:111-15
    • (1998) Trends Cell Biol. , vol.8 , pp. 111-115
    • Wasserman, S.1
  • 219
    • 0037458909 scopus 로고    scopus 로고
    • Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase
    • Wedlich-Soldner R, Altschuler S, Wu L, Li R. 2003. Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase. Science 299:1231-35
    • (2003) Science , vol.299 , pp. 1231-1235
    • Wedlich-Soldner, R.1    Altschuler, S.2    Wu, L.3    Li, R.4
  • 220
    • 0347416707 scopus 로고    scopus 로고
    • Yeast vacuole inheritance and dynamics
    • Weisman LS. 2003. Yeast vacuole inheritance and dynamics. Annu. Rev. Genet. 37:435-60
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 435-460
    • Weisman, L.S.1
  • 221
    • 0344875517 scopus 로고    scopus 로고
    • Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum
    • Wiederkehr A, Du Y, Pypaert M, Ferro-Novick S, Novick P. 2003. Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum. Mol. Biol. Cell 14:4770-82
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4770-4782
    • Wiederkehr, A.1    Du, Y.2    Pypaert, M.3    Ferro-Novick, S.4    Novick, P.5
  • 223
    • 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
    • Erratum 1997. Curr. Biol. 7(9):R593
    • Winter D, Podtelejnikov AV, Mann M, 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. 7:519-29. Erratum 1997. Curr. Biol. 7(9):R593
    • (1997) Curr. Biol. , vol.7 , pp. 519-529
    • Winter, D.1    Podtelejnikov, A.V.2    Mann, M.3    Li, R.4
  • 224
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo
    • Wu X, Bowers B, Rao K, Wei Q, Hammer JA. 1998. Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo. J. Cell Biol. 143:1899-918
    • (1998) J. Cell Biol. , vol.143 , pp. 1899-1918
    • Wu, X.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer, J.A.5
  • 225
    • 0035073174 scopus 로고    scopus 로고
    • Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle
    • Wu X, Rao K, Bowers MB, Copeland NG, Jenkins NA, Hammer JA. 2001. Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle. J. Cell Sci. 114:1091-100
    • (2001) J. Cell Sci. , vol.114 , pp. 1091-1100
    • Wu, X.1    Rao, K.2    Bowers, M.B.3    Copeland, N.G.4    Jenkins, N.A.5    Hammer, J.A.6
  • 226
    • 0036000020 scopus 로고    scopus 로고
    • Rab27a is an essential component of melanosome receptor for myosin Va
    • Wu X, Wang F, Rao K, Sellers JR, Hammer JA 3rd. 2002a. Rab27a is an essential component of melanosome receptor for myosin Va. Mol. Biol. Cell 13:1735-49
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1735-1749
    • Wu, X.1    Wang, F.2    Rao, K.3    Sellers, J.R.4    Hammer III, J.A.5
  • 228
    • 0033533697 scopus 로고    scopus 로고
    • A retention mechanism for distribution of mitochondria during cell division in budding yeast
    • Yang HC, Palazzo A, Swayne TC, Pon LA. 1999. A retention mechanism for distribution of mitochondria during cell division in budding yeast. Curr. Biol. 9:1111-14
    • (1999) Curr. Biol. , vol.9 , pp. 1111-1114
    • Yang, H.C.1    Palazzo, A.2    Swayne, T.C.3    Pon, L.A.4
  • 230
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orientates the mitotic spindle in yeast
    • Yin H, Pruyne D, Huffaker TC, Bretscher A. 2000. Myosin V orientates the mitotic spindle in yeast. Nature 406:1013-15
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1    Pruyne, D.2    Huffaker, T.C.3    Bretscher, A.4
  • 231
    • 0029912384 scopus 로고    scopus 로고
    • Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae
    • Zahner JE, Harkins HA, Pringle JR. 1996. Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae. Mol. Cell Biol. 16:1857-70
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1857-1870
    • Zahner, J.E.1    Harkins, H.A.2    Pringle, J.R.3
  • 233
    • 0028955710 scopus 로고
    • Interactions among proteins involved in bud-site selection and bud-site assembly in Saccharomyces cerevisiae
    • Zheng Y, Bender A, Cerione RA. 1995. Interactions among proteins involved in bud-site selection and bud-site assembly in Saccharomyces cerevisiae. J. Biol. Chem. 270:626-30
    • (1995) J. Biol. Chem. , vol.270 , pp. 626-630
    • Zheng, Y.1    Bender, A.2    Cerione, R.A.3
  • 234
    • 0028023358 scopus 로고
    • Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3
    • Zheng Y, Cerione R, Bender A. 1994. Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3. J. Biol. Chem. 269:2369-72
    • (1994) J. Biol. Chem. , vol.269 , pp. 2369-2372
    • Zheng, Y.1    Cerione, R.2    Bender, A.3
  • 235
    • 0142136092 scopus 로고    scopus 로고
    • Formin leaky cap allows elongation in the presence of tight capping proteins
    • Zigmond SH, Evangelista M, Boone C, Yang C, Dar AC, et al. 2003. Formin leaky cap allows elongation in the presence of tight capping proteins. Curr. Biol. 13:1820-23
    • (2003) Curr. Biol. , vol.13 , pp. 1820-1823
    • Zigmond, S.H.1    Evangelista, M.2    Boone, C.3    Yang, C.4    Dar, A.C.5
  • 236
    • 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 JM, Botstein D, Johnson DI. 1993. Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity. Mol. Biol. Cell 4:1307-16
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1307-1316
    • Ziman, M.1    Preuss, D.2    Mulholland, J.3    O'Brien, J.M.4    Botstein, D.5    Johnson, D.I.6
  • 237
    • 0020340108 scopus 로고
    • Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae
    • Zubenko GS, Park FJ, Jones EW. 1982. Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae. Genetics 102:679-90
    • (1982) Genetics , vol.102 , pp. 679-690
    • Zubenko, G.S.1    Park, F.J.2    Jones, E.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.