메뉴 건너뛰기




Volumn 21, Issue 3, 2011, Pages 184-194

Modeling vesicle traffic reveals unexpected consequences for Cdc42p-mediated polarity establishment

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN CDC42; SEPTIN; SNARE PROTEIN;

EID: 79651475078     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2011.01.012     Document Type: Article
Times cited : (103)

References (45)
  • 2
    • 33947398366 scopus 로고    scopus 로고
    • Central roles of small GTPases in the development of cell polarity in yeast and beyond
    • DOI 10.1128/MMBR.00028-06
    • H.O. Park, and E. Bi Central roles of small GTPases in the development of cell polarity in yeast and beyond Microbiol. Mol. Biol. Rev. 71 2007 48 96 (Pubitemid 46456684)
    • (2007) Microbiology and Molecular Biology Reviews , vol.71 , Issue.1 , pp. 48-96
    • Park, H.-O.1    Bi, E.2
  • 3
    • 0344394312 scopus 로고    scopus 로고
    • Scaffold-mediated symmetry breaking by Cdc42p
    • DOI 10.1038/ncb1068
    • J.E. Irazoqui, A.S. Gladfelter, and D.J. Lew Scaffold-mediated symmetry breaking by Cdc42p Nat. Cell Biol. 5 2003 1062 1070 (Pubitemid 37509112)
    • (2003) Nature Cell Biology , vol.5 , Issue.12 , pp. 1062-1070
    • Irazoqui, J.E.1    Gladfelter, A.S.2    Lew, D.J.3
  • 5
    • 42049115235 scopus 로고    scopus 로고
    • Dynamics of Cdc42 network embodies a Turing-type mechanism of yeast cell polarity
    • A.B. Goryachev, and A.V. Pokhilko Dynamics of Cdc42 network embodies a Turing-type mechanism of yeast cell polarity FEBS Lett. 582 2008 1437 1443
    • (2008) FEBS Lett. , vol.582 , pp. 1437-1443
    • Goryachev, A.B.1    Pokhilko, A.V.2
  • 6
    • 0037458909 scopus 로고    scopus 로고
    • Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase
    • DOI 10.1126/science.1080944
    • R. Wedlich-Soldner, S. Altschuler, L. Wu, and R. Li Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase Science 299 2003 1231 1235 (Pubitemid 36237464)
    • (2003) Science , vol.299 , Issue.5610 , pp. 1231-1235
    • Wedlich-Soldner, R.1    Altschuter, S.2    Wu, L.3    Li, R.4
  • 7
    • 34147175165 scopus 로고    scopus 로고
    • Endocytosis Optimizes the Dynamic Localization of Membrane Proteins that Regulate Cortical Polarity
    • DOI 10.1016/j.cell.2007.02.043, PII S0092867407003522
    • E. Marco, R. Wedlich-Soldner, R. Li, S.J. Altschuler, and L.F. Wu Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity Cell 129 2007 411 422 (Pubitemid 46574971)
    • (2007) Cell , vol.129 , Issue.2 , pp. 411-422
    • Marco, E.1    Wedlich-Soldner, R.2    Li, R.3    Altschuler, S.J.4    Wu, L.F.5
  • 8
    • 4544295912 scopus 로고    scopus 로고
    • Robust cell polarity is a dynamic state established by coupling transport and GTPase signaling
    • DOI 10.1083/jcb.200405061
    • R. Wedlich-Soldner, S.C. Wai, T. Schmidt, and R. Li Robust cell polarity is a dynamic state established by coupling transport and GTPase signaling J. Cell Biol. 166 2004 889 900 (Pubitemid 39249839)
    • (2004) Journal of Cell Biology , vol.166 , Issue.6 , pp. 889-900
    • Wedlich-Soldner, R.1    Wai, S.C.2    Schmidt, T.3    Li, R.4
  • 9
    • 71649099053 scopus 로고    scopus 로고
    • Dual modes of cdc42 recycling fine-tune polarized morphogenesis
    • B.D. Slaughter, A. Das, J.W. Schwartz, B. Rubinstein, and R. Li Dual modes of cdc42 recycling fine-tune polarized morphogenesis Dev. Cell 17 2009 823 835
    • (2009) Dev. Cell , vol.17 , pp. 823-835
    • Slaughter, B.D.1    Das, A.2    Schwartz, J.W.3    Rubinstein, B.4    Li, R.5
  • 10
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae
    • DOI 10.1083/jcb.98.3.934
    • A.E.M. Adams, and J.R. Pringle Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae J. Cell Biol. 98 1984 934 945 (Pubitemid 14166523)
    • (1984) Journal of Cell Biology , vol.98 , Issue.3 , pp. 934-945
    • Adams, A.E.M.1    Pringle, J.R.2
  • 11
    • 0021369651 scopus 로고
    • Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces
    • DOI 10.1083/jcb.98.3.922
    • J.V. Kilmartin, and A.E.M. Adams Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces J. Cell Biol. 98 1984 922 933 (Pubitemid 14166522)
    • (1984) Journal of Cell Biology , vol.98 , Issue.3 , pp. 922-933
    • Kilmartin, J.V.1    Adams, A.E.M.2
  • 12
    • 0141727533 scopus 로고    scopus 로고
    • Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling
    • DOI 10.1016/j.cub.2003.09.001
    • J. Valdez-Taubas, and H.R. Pelham Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling Curr. Biol. 13 2003 1636 1640 (Pubitemid 37215889)
    • (2003) Current Biology , vol.13 , Issue.18 , pp. 1636-1640
    • Valdez-Taubas, J.1    Pelham, H.R.B.2
  • 13
    • 23444432144 scopus 로고
    • Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum
    • DOI 10.1016/0092-8674(94)90359-X
    • W.E. Balch, J.M. McCaffery, H. Plutner, and M.G. Farquhar Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum Cell 76 1994 841 852 (Pubitemid 24085322)
    • (1994) Cell , vol.76 , Issue.5 , pp. 841-852
    • Balch, W.E.1    Michael McCaffery, J.2    Plutner, H.3    Farquhar, M.G.4
  • 14
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • DOI 10.1146/annurev.biochem.72.121801.161800
    • J.S. Bonifacino, and L.M. Traub Signals for sorting of transmembrane proteins to endosomes and lysosomes Annu. Rev. Biochem. 72 2003 395 447 (Pubitemid 36930451)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 15
    • 3142583466 scopus 로고    scopus 로고
    • Cargo recognition during clathrin-mediated endocytosis: A team effort
    • DOI 10.1016/j.ceb.2004.06.001, PII S0955067404000705
    • A. Sorkin Cargo recognition during clathrin-mediated endocytosis: A team effort Curr. Opin. Cell Biol. 16 2004 392 399 (Pubitemid 38903145)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 392-399
    • Sorkin, A.1
  • 16
    • 33748969492 scopus 로고    scopus 로고
    • Endocytic adaptors: Recruiters, coordinators and regulators
    • DOI 10.1016/j.tcb.2006.08.001, PII S0962892406001978, Membrane Dynamics
    • L. Maldonado-Báez, and B. Wendland Endocytic adaptors: Recruiters, coordinators and regulators Trends Cell Biol. 16 2006 505 513 (Pubitemid 44442957)
    • (2006) Trends in Cell Biology , vol.16 , Issue.10 , pp. 505-513
    • Maldonado-Baez, L.1    Wendland, B.2
  • 17
    • 73949119447 scopus 로고    scopus 로고
    • Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast
    • H.E. Stimpson, C.P. Toret, A.T. Cheng, B.S. Pauly, and D.G. Drubin Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast Mol. Biol. Cell 20 2009 4640 4651
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4640-4651
    • Stimpson, H.E.1    Toret, C.P.2    Cheng, A.T.3    Pauly, B.S.4    Drubin, D.G.5
  • 18
    • 0022446007 scopus 로고
    • Down regulation of the α-factor pheromone receptor in S. cerevisiae
    • D.D. Jenness, and P. Spatrick Down regulation of the alpha-factor pheromone receptor in S. cerevisiae Cell 46 1986 345 353 (Pubitemid 16031673)
    • (1986) Cell , vol.46 , Issue.3 , pp. 345-353
    • Jenness, D.D.1    Spatrick, P.2
  • 19
    • 0027207946 scopus 로고
    • Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled α-pheromone receptor in yeast
    • J. Rohrer, H. Bénédetti, B. Zanolari, and H. Riezman Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled alpha-pheromone receptor in yeast Mol. Biol. Cell 4 1993 511 521 (Pubitemid 23150915)
    • (1993) Molecular Biology of the Cell , vol.4 , Issue.5 , pp. 511-521
    • Rohrer, J.1    Benedetti, H.2    Zanolari, B.3    Riezman, H.4
  • 20
    • 0027943713 scopus 로고
    • Direct evidence for ligand-induced internalization of the yeast α-factor pheromone receptor
    • K.A. Schandel, and D.D. Jenness Direct evidence for ligand-induced internalization of the yeast alpha-factor pheromone receptor Mol. Cell. Biol. 14 1994 7245 7255 (Pubitemid 24326389)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.11 , pp. 7245-7255
    • Schandel, K.A.1    Jenness, D.D.2
  • 21
    • 0032550179 scopus 로고    scopus 로고
    • Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization
    • DOI 10.1083/jcb.141.2.349
    • L. Hicke, B. Zanolari, and H. Riezman Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization J. Cell Biol. 141 1998 349 358 (Pubitemid 28237084)
    • (1998) Journal of Cell Biology , vol.141 , Issue.2 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 22
    • 73849117900 scopus 로고    scopus 로고
    • Requirements for recruitment of a G protein-coupled receptor to clathrin-coated pits in budding yeast
    • J.Y. Toshima, J. Nakanishi, K. Mizuno, J. Toshima, and D.G. Drubin Requirements for recruitment of a G protein-coupled receptor to clathrin-coated pits in budding yeast Mol. Biol. Cell 20 2009 5039 5050
    • (2009) Mol. Biol. Cell , vol.20 , pp. 5039-5050
    • Toshima, J.Y.1    Nakanishi, J.2    Mizuno, K.3    Toshima, J.4    Drubin, D.G.5
  • 25
    • 59449086932 scopus 로고    scopus 로고
    • A novel septin-associated protein, Syp1p, is required for normal cell cycle-dependent septin cytoskeleton dynamics in yeast
    • W. Qiu, S.P. Neo, X. Yu, and M. Cai A novel septin-associated protein, Syp1p, is required for normal cell cycle-dependent septin cytoskeleton dynamics in yeast Genetics 180 2008 1445 1457
    • (2008) Genetics , vol.180 , pp. 1445-1457
    • Qiu, W.1    Neo, S.P.2    Yu, X.3    Cai, M.4
  • 26
    • 0035204717 scopus 로고    scopus 로고
    • The septin cortex at the yeast mother-bud neck
    • DOI 10.1016/S1369-5274(01)00269-7
    • A.S. Gladfelter, J.R. Pringle, and D.J. Lew The septin cortex at the yeast mother-bud neck Curr. Opin. Microbiol. 4 2001 681 689 (Pubitemid 33116865)
    • (2001) Current Opinion in Microbiology , vol.4 , Issue.6 , pp. 681-689
    • Gladfelter, A.S.1    Pringle, J.R.2    Lew, D.J.3
  • 27
    • 64549158361 scopus 로고    scopus 로고
    • Septins and the lateral compartmentalization of eukaryotic membranes
    • F. Caudron, and Y. Barral Septins and the lateral compartmentalization of eukaryotic membranes Dev. Cell 16 2009 493 506
    • (2009) Dev. Cell , vol.16 , pp. 493-506
    • Caudron, F.1    Barral, Y.2
  • 29
    • 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
    • DOI 10.1083/jcb.137.2.399
    • K.R. Ayscough, J. Stryker, N. Pokala, M. Sanders, P. Crews, and D.G. Drubin 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 1997 399 416 (Pubitemid 27181293)
    • (1997) Journal of Cell Biology , vol.137 , Issue.2 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 30
    • 0344827286 scopus 로고    scopus 로고
    • A Pathway for Association of Receptors, Adaptors, and Actin during Endocytic Internalization
    • DOI 10.1016/S0092-8674(03)00883-3
    • M. Kaksonen, Y. Sun, and D.G. Drubin A pathway for association of receptors, adaptors, and actin during endocytic internalization Cell 115 2003 475 487 (Pubitemid 37456809)
    • (2003) Cell , vol.115 , Issue.4 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 31
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • DOI 10.1038/nrm1940, PII NRM1940
    • M. Kaksonen, C.P. Toret, and D.G. Drubin Harnessing actin dynamics for clathrin-mediated endocytosis Nat. Rev. Mol. Cell Biol. 7 2006 404 414 (Pubitemid 44050094)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.6 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 33
    • 0037599264 scopus 로고    scopus 로고
    • Negative regulation of yeast WASp by two SH3 domain-containing proteins
    • DOI 10.1016/S0960-9822(03)00383-X
    • A.A. Rodal, A.L. Manning, B.L. Goode, and D.G. Drubin Negative regulation of yeast WASp by two SH3 domain-containing proteins Curr. Biol. 13 2003 1000 1008 (Pubitemid 36726035)
    • (2003) Current Biology , vol.13 , Issue.12 , pp. 1000-1008
    • Rodal, A.A.1    Manning, A.L.2    Goode, B.L.3    Drubin, D.G.4
  • 34
    • 4444224966 scopus 로고    scopus 로고
    • Endocytosis by random initiation and stabilization of clathrin-coated pits
    • DOI 10.1016/j.cell.2004.08.017, PII S0092867404007901
    • M. Ehrlich, W. Boll, A. Van Oijen, R. Hariharan, K. Chandran, M.L. Nibert, and T. Kirchhausen Endocytosis by random initiation and stabilization of clathrin-coated pits Cell 118 2004 591 605 (Pubitemid 39179712)
    • (2004) Cell , vol.118 , Issue.5 , pp. 591-605
    • Ehrlich, M.1    Boll, W.2    Van Oijen, A.3    Hariharan, R.4    Chandran, K.5    Nibert, M.L.6    Kirchhausen, T.7
  • 36
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • P. Novick, C. Field, and R. Schekman Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway Cell 21 1980 205 215 (Pubitemid 10040069)
    • (1980) Cell , vol.21 , Issue.1 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 38
    • 0032555918 scopus 로고    scopus 로고
    • Assembly and function of the actin cytoskeleton of yeast: Relationships between cables and patches
    • DOI 10.1083/jcb.142.6.1501
    • T.S. Karpova, J.G. McNally, S.L. Moltz, and J.A. Cooper Assembly and function of the actin cytoskeleton of yeast: Relationships between cables and patches J. Cell Biol. 142 1998 1501 1517 (Pubitemid 28452599)
    • (1998) Journal of Cell Biology , vol.142 , Issue.6 , pp. 1501-1517
    • Karpova, T.S.1    McNally, J.G.2    Moltz, S.L.3    Cooper, J.A.4
  • 39
    • 0034002308 scopus 로고    scopus 로고
    • Identification of novel, evolutionarily conserved Cdc42p-interacting proteins and of redundant pathways linking Cdc24p and Cdc42p to actin polarization in yeast
    • E. Bi, J.B. Chiavetta, H. Chen, G.C. Chen, C.S. Chan, and J.R. Pringle Identification of novel, evolutionarily conserved Cdc42p-interacting proteins and of redundant pathways linking Cdc24p and Cdc42p to actin polarization in yeast Mol. Biol. Cell 11 2000 773 793 (Pubitemid 30112181)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.2 , pp. 773-793
    • Bi, E.1    Chiavetta, J.B.2    Chen, H.3    Chen, G.-C.4    Chan, C.S.M.5    Pringle, J.R.6
  • 40
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • DOI 10.1002/(SI CI)1097-00 61(199807)14:10<95 3::AID-YEA293>3. 0.CO;2-U
    • M.S. Longtine, A. McKenzie 3rd, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae Yeast 14 1998 953 961 (Pubitemid 28328001)
    • (1998) Yeast , vol.14 , Issue.10 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 41
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • DOI 10.1016/j.cell.2005.09.024, PII S0092867405009785
    • M. Kaksonen, C.P. Toret, and D.G. Drubin A modular design for the clathrin- and actin-mediated endocytosis machinery Cell 123 2005 305 320 (Pubitemid 41457219)
    • (2005) Cell , vol.123 , Issue.2 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 42
    • 21344469702 scopus 로고    scopus 로고
    • In vivo dynamics of clathrin and its adaptor-dependent recruitment to the actin-based endocytic machinery in yeast
    • DOI 10.1016/j.devcel.2005.04.014, PII S1534580705001693
    • T.M. Newpher, R.P. Smith, V. Lemmon, and S.K. Lemmon In vivo dynamics of clathrin and its adaptor-dependent recruitment to the actin-based endocytic machinery in yeast Dev. Cell 9 2005 87 98 (Pubitemid 40903662)
    • (2005) Developmental Cell , vol.9 , Issue.1 , pp. 87-98
    • Newpher, T.M.1    Smith, R.P.2    Lemmon, V.3    Lemmon, S.K.4
  • 43
    • 77955596267 scopus 로고    scopus 로고
    • Microtubule dynamics at the cell cortex probed by TIRF microscopy
    • I. Grigoriev, and A. Akhmanova Microtubule dynamics at the cell cortex probed by TIRF microscopy Methods Cell Biol. 97 2010 91 109
    • (2010) Methods Cell Biol. , vol.97 , pp. 91-109
    • Grigoriev, I.1    Akhmanova, A.2
  • 44
    • 77956283446 scopus 로고    scopus 로고
    • Imaging single molecules using total internal reflection fluorescence microscopy (TIRFM)
    • S.L. Reck-Peterson, N.D. Derr, and N. Stuurman Imaging single molecules using total internal reflection fluorescence microscopy (TIRFM) Cold Spring Harb Protoc 2010 2010 pdb.top73
    • (2010) Cold Spring Harb Protoc , vol.2010
    • Reck-Peterson, S.L.1    Derr, N.D.2    Stuurman, N.3
  • 45
    • 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
    • H.B. Kim, B.K. Haarer, and J.R. Pringle 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 1991 535 544 (Pubitemid 121000368)
    • (1991) Journal of Cell Biology , vol.112 , Issue.4 , pp. 535-544
    • Kim, H.B.1    Haarer, B.K.2    Pringle, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.