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Volumn 23, Issue 19, 2012, Pages 3814-3826

Cdc42p regulation of the yeast formin Bni1p mediated by the effector Gic2p

Author keywords

[No Author keywords available]

Indexed keywords

CDC42P; FUNGAL PROTEIN; PROTEIN BNI1P; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84867178299     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-05-0400     Document Type: Article
Times cited : (33)

References (69)
  • 1
    • 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, 131-142.
    • (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
  • 2
    • 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, 2824-2830.
    • (2001) J Biol Chem , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 3
    • 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, 729-753. (Pubitemid 27176179)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.4 , pp. 729-753
    • Amberg, D.C.1    Zahner, J.E.2    Mulholland, J.W.3    Pringle, J.R.4    Botstein, D.5
  • 4
    • 0030852841 scopus 로고    scopus 로고
    • A small conserved domain in the yeast Spa2p is necessary and sufficient for its polarized localization
    • DOI 10.1083/jcb.138.1.17
    • Arkowitz RA, Lowe N (1997). A small conserved domain in the yeast Spa2p is necessary and sufficient for its polarized localization. J Cell Biol 138, 17-36. (Pubitemid 27337449)
    • (1997) Journal of Cell Biology , vol.138 , Issue.1 , pp. 17-36
    • Arkowitz, R.A.1    Lowe, N.2
  • 5
    • 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
    • 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. (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
  • 7
    • 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
    • Bi E, Chiavetta JB, Chen H, Chen GC, Chan CS, Pringle JR (2000). 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, 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
  • 9
    • 0030715361 scopus 로고    scopus 로고
    • Novel Cdc42-binding proteins Gic1 and Gic2 control cell polarity in yeast
    • Brown JL, Jaquenoud M, Gulli MP, Chant J, Peter M (1997). Novel Cdc42-binding proteins Gic1 and Gic2 control cell polarity in yeast. Genes Dev 11, 2972-2982. (Pubitemid 27508508)
    • (1997) Genes and Development , vol.11 , Issue.22 , pp. 2972-2982
    • Brown, J.L.1    Jaquenoud, M.2    Gulli, M.-P.3    Chant, J.4    Peter, M.5
  • 10
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo PD, Drechsel D, Hall A (1995). A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J Biol Chem 270, 29071-29074.
    • (1995) J Biol Chem , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 11
    • 34248170173 scopus 로고    scopus 로고
    • Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables
    • DOI 10.1091/mbc.E06-09-0820
    • Buttery SM, Yoshida S, Pellman D (2007). Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables. Mol Biol Cell 18, 1826-1838. (Pubitemid 46717563)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.5 , pp. 1826-1838
    • Buttery, S.M.1    Yoshida, S.2    Pellman, D.3
  • 12
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: Cellular control of actin assembly
    • Campellone KG, Welch MD (2010). A nucleator arms race: cellular control of actin assembly. Nat Rev Mol Cell Biol 11, 237-251.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 13
    • 0030705142 scopus 로고    scopus 로고
    • The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for polarized cell growth in Saccharomyces cerevisiae
    • Chen GC, Kim YJ, Chan CS (1997). The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for polarized cell growth in Saccharomyces cerevisiae. Genes Dev 11, 2958-2971.
    • (1997) Genes Dev , vol.11 , pp. 2958-2971
    • Chen, G.C.1    Kim, Y.J.2    Chan, C.S.3
  • 14
    • 80052693186 scopus 로고    scopus 로고
    • Dynamics of septin ring and collar formation in Saccharomyces cerevisiae
    • Chen H, Howell AS, Robeson A, Lew DJ (2011). Dynamics of septin ring and collar formation in Saccharomyces cerevisiae. Biol Chem 392, 689-697.
    • (2011) Biol Chem , vol.392 , pp. 689-697
    • Chen, H.1    Howell, A.S.2    Robeson, A.3    Lew, D.J.4
  • 15
    • 59649092799 scopus 로고    scopus 로고
    • Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function
    • Chesarone M, Gould CJ, Moseley JB, Goode BL (2009). Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function. Dev Cell 16, 292-302.
    • (2009) Dev Cell , vol.16 , pp. 292-302
    • Chesarone, M.1    Gould, C.J.2    Moseley, J.B.3    Goode, B.L.4
  • 16
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone MA, DuPage AG, Goode BL (2010). Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat Rev Mol Cell Biol 11, 62-74.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 62-74
    • Chesarone, M.A.1    DuPage, A.G.2    Goode, B.L.3
  • 17
    • 79961235785 scopus 로고    scopus 로고
    • The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper
    • Chesarone-Cataldo M, Guerin C, Yu JH, Wedlich-Soldner R, Blanchoin L, Goode BL (2011). The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper. Dev Cell 21, 217-230.
    • (2011) Dev Cell , vol.21 , pp. 217-230
    • Chesarone-Cataldo, M.1    Guerin, C.2    Yu, J.H.3    Wedlich-Soldner, R.4    Blanchoin, L.5    Goode, B.L.6
  • 18
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morphogenesis
    • DOI 10.1126/science.276.5309.118
    • Evangelista M, Blundell K, Longtine MS, Chow CJ, Adames N, Pringle JR, Peter M, Boone C (1997). Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276, 118-122. (Pubitemid 27161258)
    • (1997) Science , vol.276 , Issue.5309 , pp. 118-122
    • Evangelista, M.1    Blundell, K.2    Longtine, M.S.3    Chow, C.J.4    Adames, N.5    Pringle, J.R.6    Peter, M.7    Boone, C.8
  • 19
    • 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, 260-269.
    • (2002) Nat Cell Biol , vol.4 , pp. 260-269
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 20
    • 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, Shimizu K, Takai Y (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, 1221-1233. (Pubitemid 28457311)
    • (1998) Molecular Biology of the Cell , vol.9 , Issue.5 , pp. 1221-1233
    • Fujiwara, T.1    Tanaka, K.2    Mino, A.3    Kikyo, M.4    Takahashi, K.5    Shimizu, K.6    Takai, Y.7
  • 21
    • 66249091620 scopus 로고    scopus 로고
    • Polarized growth in budding yeast in the absence of a localized formin
    • Gao L, Bretscher A (2009). Polarized growth in budding yeast in the absence of a localized formin. Mol Biol Cell 20, 2540-2548.
    • (2009) Mol Biol Cell , vol.20 , pp. 2540-2548
    • Gao, L.1    Bretscher, A.2
  • 22
    • 77950685176 scopus 로고    scopus 로고
    • The yeast formin Bnr1p has two localization regions that show spatially and temporally distinct association with septin structures
    • Gao L, Liu W, Bretscher A (2010). The yeast formin Bnr1p has two localization regions that show spatially and temporally distinct association with septin structures. Mol Biol Cell 21, 1253-1262.
    • (2010) Mol Biol Cell , vol.21 , pp. 1253-1262
    • Gao, L.1    Liu, W.2    Bretscher, A.3
  • 23
    • 18844452708 scopus 로고    scopus 로고
    • Interplay between septin organization, cell cycle and cell shape in yeast
    • DOI 10.1242/jcs.02286
    • Gladfelter AS, Kozubowski L, Zyla TR, Lew DJ (2005). Interplay between septin organization, cell cycle and cell shape in yeast. J Cell Sci 118, 1617-1628. (Pubitemid 40691890)
    • (2005) Journal of Cell Science , vol.118 , Issue.8 , pp. 1617-1628
    • Gladfelter, A.S.1    Kozubowski, L.2    Zyla, T.R.3    Lew, D.J.4
  • 25
    • 85078505418 scopus 로고    scopus 로고
    • Improved flow cytometric analysis of the budding yeast cell cycle
    • Haase SB, Reed SI (2002). Improved flow cytometric analysis of the budding yeast cell cycle. Cell Cycle 1, 132-136.
    • (2002) Cell Cycle , vol.1 , pp. 132-136
    • Haase, S.B.1    Reed, S.I.2
  • 26
    • 84859760140 scopus 로고    scopus 로고
    • Negative feedback enhances robustness in the yeast polarity establishment circuit
    • Howell AS, Jin M, Wu CF, Zyla TR, Elston TC, Lew DJ (2012). Negative feedback enhances robustness in the yeast polarity establishment circuit. Cell 149, 322-333.
    • (2012) Cell , vol.149 , pp. 322-333
    • Howell, A.S.1    Jin, M.2    Wu, C.F.3    Zyla, T.R.4    Elston, T.C.5    Lew, D.J.6
  • 27
    • 84855428523 scopus 로고    scopus 로고
    • Morphogenesis and the cell cycle
    • Howell AS, Lew DJ (2012). Morphogenesis and the cell cycle. Genetics 190, 51-77.
    • (2012) Genetics , vol.190 , pp. 51-77
    • Howell, A.S.1    Lew, D.J.2
  • 29
    • 0344394312 scopus 로고    scopus 로고
    • Scaffold-mediated symmetry breaking by Cdc42p
    • DOI 10.1038/ncb1068
    • Irazoqui JE, Gladfelter AS, Lew DJ (2003). Scaffold-mediated symmetry breaking by Cdc42p. Nat Cell Biol 5, 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
  • 31
    • 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, 6244-6258.
    • (2000) Mol Cell Biol , vol.20 , pp. 6244-6258
    • Jaquenoud, M.1    Peter, M.2
  • 32
    • 0032851813 scopus 로고    scopus 로고
    • The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins
    • Joberty G, Perlungher RR, Macara IG (1999). The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins. Mol Cell Biol 19, 6585-6597. (Pubitemid 29441843)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.10 , pp. 6585-6597
    • Joberty, G.1    Perlungher, R.R.2    Macara, I.G.3
  • 33
    • 81955160696 scopus 로고    scopus 로고
    • Symmetry breaking and the establishment of cell polarity in budding yeast
    • Johnson JM, Jin M, Lew DJ (2011). Symmetry breaking and the establishment of cell polarity in budding yeast. Curr Opin Genet Dev 21, 740-746.
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 740-746
    • Johnson, J.M.1    Jin, M.2    Lew, D.J.3
  • 34
    • 9444257597 scopus 로고    scopus 로고
    • Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E04-03-0254
    • Kadota J, Yamamoto T, Yoshiuchi S, Bi E, Tanaka K (2004). Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae. Mol Biol Cell 15, 5329-5345. (Pubitemid 39564728)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.12 , pp. 5329-5345
    • Kadota, J.1    Yamamoto, T.2    Yoshiuchi, S.3    Bi, E.4    Tanaka, K.5
  • 37
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • DOI 10.1016/j.cell.2005.11.038, PII S009286740501398X
    • Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD (2006). Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124, 423-435. (Pubitemid 43121988)
    • (2006) Cell , vol.124 , Issue.2 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 39
    • 23044500737 scopus 로고    scopus 로고
    • Role of the septin ring in the asymmetric localization of proteins at the mother-bud neck in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E04-09-0764
    • Kozubowski L, Larson JR, Tatchell K (2005). Role of the septin ring in the asymmetric localization of proteins at the mother-bud neck in Saccharomyces cerevisiae. Mol Biol Cell 16, 3455-3466. (Pubitemid 41077060)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.8 , pp. 3455-3466
    • Kozubowski, L.1    Larson, J.R.2    Tatchell, K.3
  • 41
    • 28644442126 scopus 로고    scopus 로고
    • The regulation of mDia1 by autoinhibition and its release by Rho*GTP
    • DOI 10.1038/sj.emboj.7600879
    • Lammers M, Rose R, Scrima A, Wittinghofer A (2005). The regulation of mDia1 by autoinhibition and its release by Rho*GTP. EMBO J 24, 4176-4187. (Pubitemid 41752886)
    • (2005) EMBO Journal , vol.24 , Issue.23 , pp. 4176-4187
    • Lammers, M.1    Rose, R.2    Scrima, A.3    Wittinghofer, A.4
  • 42
    • 0027414941 scopus 로고
    • Morphogenesis in the yeast cell cycle: Regulation by Cdc28 and cyclins
    • Lew DJ, Reed SI (1993). Morphogenesis in the yeast cell cycle: regulation by Cdc28 and cyclins. J Cell Biol 120, 1305-1320. (Pubitemid 23081679)
    • (1993) Journal of Cell Biology , vol.120 , Issue.6 , pp. 1305-1320
    • Lew, D.J.1    Reed, S.I.2
  • 43
    • 0043202969 scopus 로고    scopus 로고
    • The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • DOI 10.1016/S0960-9822(03)00540-2
    • Li F, Higgs HN (2003). The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr Biol 13, 1335-1340. (Pubitemid 36953308)
    • (2003) Current Biology , vol.13 , Issue.15 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 44
    • 84863059653 scopus 로고    scopus 로고
    • Yeast formin Bni1p has multiple localization regions that function in polarized growth and spindle orientation
    • Liu W, Santiago-Tirado FH, Bretscher A (2012). Yeast formin Bni1p has multiple localization regions that function in polarized growth and spindle orientation. Mol Biol Cell 23, 412-422.
    • (2012) Mol Biol Cell , vol.23 , pp. 412-422
    • Liu, W.1    Santiago-Tirado, F.H.2    Bretscher, A.3
  • 45
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • DOI 10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U
    • Longtine MS, McKenzie A 3rd, Demarini DJ, Shah NG, Wach A, Brachat A, Philippsen P, Pringle JR (1998). Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 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
  • 47
    • 32044470440 scopus 로고    scopus 로고
    • Structure of the autoinhibitory switch in formin mDia1
    • DOI 10.1016/j.str.2005.12.003, PII S0969212606000451
    • Nezami AG, Poy F, Eck MJ (2006). Structure of the autoinhibitory switch in formin mDia1. Structure 14, 257-263. (Pubitemid 43202015)
    • (2006) Structure , vol.14 , Issue.2 , pp. 257-263
    • Nezami, A.G.1    Poy, F.2    Eck, M.J.3
  • 48
    • 20844439387 scopus 로고    scopus 로고
    • Structural basis of Rho GTPase-mediated activation of the formin mDia1
    • DOI 10.1016/j.molcel.2005.04.002, PII S1097276505012268
    • Otomo T, Otomo C, Tomchick DR, Machius M, Rosen MK (2005a). Structural basis of Rho GTPase-mediated activation of the formin mDia1. Mol Cell 18, 273-281. (Pubitemid 41350533)
    • (2005) Molecular Cell , vol.18 , Issue.3 , pp. 273-281
    • Otomo, T.1    Otomo, C.2    Tomchick, D.R.3    Machius, M.4    Rosen, M.K.5
  • 49
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • DOI 10.1038/nature03251
    • Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK (2005b). Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433, 488-494. (Pubitemid 40204299)
    • (2005) Nature , vol.433 , Issue.7025 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 51
    • 33947398366 scopus 로고    scopus 로고
    • Central roles of small GTPases in the development of cell polarity in yeast and beyond
    • Park HO, Bi E (2007). Central roles of small GTPases in the development of cell polarity in yeast and beyond. Microbiol Mol Biol Rev 71, 48-96.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 48-96
    • Park, H.O.1    Bi, E.2
  • 52
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • DOI 10.1126/science.1072309
    • Pruyne D, Evangelista M, Yang C, Bi E, Zigmond S, Bretscher A, Boone C (2002). Role of formins in actin assembly: nucleation and barbed-end association. Science 297, 612-615. (Pubitemid 34815347)
    • (2002) Science , vol.297 , Issue.5581 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5    Bretscher, A.6    Boone, C.7
  • 53
    • 6344275302 scopus 로고    scopus 로고
    • Stable and dynamic axes of polarity use distinct formin isoforms in budding yeast
    • DOI 10.1091/mbc.E04-04-0296
    • Pruyne D, Gao L, Bi E, Bretscher A (2004). Stable and dynamic axes of polarity use distinct formin isoforms in budding yeast. Mol Biol Cell 15, 4971-4989. (Pubitemid 39392212)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.11 , pp. 4971-4989
    • Pruyne, D.1    Gao, L.2    Bi, E.3    Bretscher, A.4
  • 55
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • DOI 10.1016/j.cell.2004.09.039, PII S0092867404009365
    • Romero S, Le Clainche C, Didry D, Egile C, Pantaloni D, Carlier MF (2004). Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119, 419-429. (Pubitemid 39423843)
    • (2004) Cell , vol.119 , Issue.3 , pp. 419-429
    • Romero, S.1    Le, C.C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.-F.6
  • 56
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • DOI 10.1038/nature03604
    • Rose R, Weyand M, Lammers M, Ishizaki T, Ahmadian MR, Wittinghofer A (2005). Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 435, 513-518. (Pubitemid 40734249)
    • (2005) Nature , vol.435 , Issue.7041 , pp. 513-518
    • Rose, R.1    Weyand, M.2    Lammers, M.3    Ishizaki, T.4    Ahmadian, M.R.5    Wittinghofer, A.6
  • 57
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • DOI 10.1038/ncb719
    • 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. (Pubitemid 34071979)
    • (2002) Nature Cell Biology , vol.4 , Issue.1 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 59
    • 33748123994 scopus 로고    scopus 로고
    • Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1
    • DOI 10.1083/jcb.200605006
    • Seth A, Otomo C, Rosen MK (2006). Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1. J Cell Biol 174, 701-713. (Pubitemid 44306726)
    • (2006) Journal of Cell Biology , vol.174 , Issue.5 , pp. 701-713
    • Seth, A.1    Otomo, C.2    Rosen, M.K.3
  • 60
    • 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, 4053-4069. (Pubitemid 28287929)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.7 , pp. 4053-4069
    • Sheu, Y.-J.1    Santos, B.2    Fortin, N.3    Costigan, C.4    Snyder, M.5
  • 61
    • 0024539080 scopus 로고
    • The SPA2 protein of yeast localizes to sites of cell growth
    • Snyder M (1989). The SPA2 protein of yeast localizes to sites of cell growth. J Cell Biol 108, 1419-1429.
    • (1989) J Cell Biol , vol.108 , pp. 1419-1429
    • Snyder, M.1
  • 62
    • 37049012678 scopus 로고    scopus 로고
    • Identification of novel membrane-binding domains in multiple yeast Cdc42 effectors
    • DOI 10.1091/mbc.E07-07-0676
    • Takahashi S, Pryciak PM (2007). Identification of novel membrane-binding domains in multiple yeast Cdc42 effectors. Mol Biol Cell 18, 4945-4956. (Pubitemid 350246695)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.12 , pp. 4945-4956
    • Takahashi, S.1    Pryciak, P.M.2
  • 63
    • 49649109812 scopus 로고    scopus 로고
    • Membrane localization of scaffold proteins promotes graded signaling in the yeast MAP kinase cascade
    • Takahashi S, Pryciak PM (2008). Membrane localization of scaffold proteins promotes graded signaling in the yeast MAP kinase cascade. Curr Biol 18, 1184-1191.
    • (2008) Curr Biol , vol.18 , pp. 1184-1191
    • Takahashi, S.1    Pryciak, P.M.2
  • 64
    • 38049063098 scopus 로고    scopus 로고
    • Adjacent positioning of cellular structures enabled by a Cdc42 GTPase-activating protein-mediated zone of inhibition
    • Tong Z, Gao XD, Howell AS, Bose I, Lew DJ, Bi E (2007). Adjacent positioning of cellular structures enabled by a Cdc42 GTPase-activating protein-mediated zone of inhibition. J Cell Biol 179, 1375-1384.
    • (2007) J Cell Biol , vol.179 , pp. 1375-1384
    • Tong, Z.1    Gao, X.D.2    Howell, A.S.3    Bose, I.4    Lew, D.J.5    Bi, E.6
  • 65
    • 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. (Pubitemid 30112168)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.2 , pp. 593-611
    • Vallen, E.A.1    Caviston, J.2    Bi, E.3
  • 66
    • 64849094913 scopus 로고    scopus 로고
    • Regulation of the yeast formin Bni1p by the actin-regulating kinase Prk1p
    • Wang J, Neo SP, Cai M (2009). Regulation of the yeast formin Bni1p by the actin-regulating kinase Prk1p. Traffic 10, 528-535.
    • (2009) Traffic , vol.10 , pp. 528-535
    • Wang, J.1    Neo, S.P.2    Cai, M.3
  • 68
    • 0031193920 scopus 로고    scopus 로고
    • The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches
    • Winter D, Podtelejnikov 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, 519-529. (Pubitemid 27308975)
    • (1997) Current Biology , vol.7 , Issue.7 , pp. 519-529
    • Winter, D.1    Podtelejnikov, A.V.2    Mann, M.3    Li, R.4
  • 69
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • DOI 10.1016/S0092-8674(04)00210-7, PII S0092867404002107
    • Xu Y, Moseley JB, Sagot I, Poy F, Pellman D, Goode BL, Eck MJ (2004). Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116, 711-723. (Pubitemid 38326729)
    • (2004) Cell , vol.116 , Issue.5 , pp. 711-723
    • Xu, Y.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7


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