메뉴 건너뛰기




Volumn 301, Issue 1, 2004, Pages 8-15

Closing the loops: New insights into the role and regulation of actin during cell polarization

Author keywords

Actin; Cell polarization; Cytokinesis

Indexed keywords

ACTIN; METHENAMINE; PROTEIN;

EID: 6344289295     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.08.011     Document Type: Review
Times cited : (18)

References (70)
  • 1
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • D.G. Drubin, and W.J. Nelson Origins of cell polarity Cell 84 1996 335 344
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 2
    • 0034729916 scopus 로고    scopus 로고
    • Rho GTPases: Molecular switches that control the organization and dynamics of the actin cytoskeleton
    • A. Hall, and C.D. Nobes Rho GTPases: molecular switches that control the organization and dynamics of the actin cytoskeleton Philos. Trans. R. Soc. Lond., B Biol. Sci. 355 2000 965 970
    • (2000) Philos. Trans. R. Soc. Lond., B Biol. Sci. , vol.355 , pp. 965-970
    • Hall, A.1    Nobes, C.D.2
  • 3
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through Arp2/3 complex: Activation by a diverse array of proteins
    • H.N. Higgs, and T.D. Pollard Regulation of actin filament network formation through Arp2/3 complex: activation by a diverse array of proteins Annu. Rev. Biochem. 70 2001 649 676
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 4
    • 1242265771 scopus 로고    scopus 로고
    • Actin polymerization: Riding the wave
    • L.G. Smith, and R. Li Actin polymerization: riding the wave Curr. Biol. 14 2004 R109 R111
    • (2004) Curr. Biol. , vol.14
    • Smith, L.G.1    Li, R.2
  • 5
    • 0025344531 scopus 로고
    • Disruption of the actin cytoskeleton in yeast capping protein mutants
    • J.F. Amatruda, J.F. Cannon, K. Tatchell, C. Hug, and J.A. Cooper Disruption of the actin cytoskeleton in yeast capping protein mutants Nature 344 1990 352 354
    • (1990) Nature , vol.344 , pp. 352-354
    • Amatruda, J.F.1    Cannon, J.F.2    Tatchell, K.3    Hug, C.4    Cooper, J.A.5
  • 6
    • 1642391823 scopus 로고    scopus 로고
    • Formin-induced nucleation of actin filaments
    • S.H. Zigmond Formin-induced nucleation of actin filaments Curr. Opin. Cell Biol. 16 2004 99 105
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 99-105
    • Zigmond, S.H.1
  • 7
    • 0035914408 scopus 로고    scopus 로고
    • MDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation
    • S. Satoh, and T. Tominaga mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation J. Biol. Chem. 276 2001 39290 39294
    • (2001) J. Biol. Chem. , vol.276 , pp. 39290-39294
    • Satoh, S.1    Tominaga, T.2
  • 8
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • M. Evangelista, D. Pruyne, D.C. Amberg, C. Boone, and A. Bretscher Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast Nat. Cell Biol. 4 2002 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
  • 9
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • I. Sagot, S.K. Klee, and D. Pellman Yeast formins regulate cell polarity by controlling the assembly of actin cables Nat. Cell Biol. 4 2002 42 50
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 10
    • 0033594955 scopus 로고    scopus 로고
    • Genetic dissection of the budding yeast Arp2/3 complex: A comparison of the in vivo and structural roles of individual subunits
    • D.C. Winter, E.Y. Choe, and R. Li Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits Proc. Natl. Acad. Sci. U. S. A. 96 1999 7288 7293
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7288-7293
    • Winter, D.C.1    Choe, E.Y.2    Li, R.3
  • 11
    • 0037780973 scopus 로고    scopus 로고
    • The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin
    • D.R. Kovar, J.R. Kuhn, A.L. Tichy, and T.D. Pollard The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin J. Cell Biol. 161 2003 875 887
    • (2003) J. Cell Biol. , vol.161 , pp. 875-887
    • Kovar, D.R.1    Kuhn, J.R.2    Tichy, A.L.3    Pollard, T.D.4
  • 12
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture
    • Y. Xu, J.B. Moseley, I. Sagot, F. Poy, D. Pellman, B.L. Goode, and M.J. Eck Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture Cell 116 2004 711 723
    • (2004) Cell , vol.116 , 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
  • 13
    • 1542285173 scopus 로고    scopus 로고
    • The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization
    • A. Shimada, M. Nyitrai, I.R. Vetter, D. Kuhlmann, B. Bugyi, S. Narumiya, M.A. Geeves, and A. Wittinghofer The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization Mol. Cell 13 2004 511 522
    • (2004) Mol. Cell , vol.13 , pp. 511-522
    • Shimada, A.1    Nyitrai, M.2    Vetter, I.R.3    Kuhlmann, D.4    Bugyi, B.5    Narumiya, S.6    Geeves, M.A.7    Wittinghofer, A.8
  • 14
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Signaling effectors for assembly and polarization of actin filaments
    • M. Evangelista, S. Zigmond, and C. Boone Formins: signaling effectors for assembly and polarization of actin filaments J. Cell Sci. 116 2003 2603 2611
    • (2003) J. Cell Sci. , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 15
    • 0037451174 scopus 로고    scopus 로고
    • Polarized growth and organelle segregation in yeast: The tracks, motors, and receptors
    • A. Bretscher Polarized growth and organelle segregation in yeast: the tracks, motors, and receptors J. Cell Biol. 160 2003 811 816
    • (2003) J. Cell Biol. , vol.160 , pp. 811-816
    • Bretscher, A.1
  • 17
    • 0037195254 scopus 로고    scopus 로고
    • Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis
    • N. Tolliday, L. VerPlank, and R. Li Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis Curr. Biol. 12 2002 1864 1870
    • (2002) Curr. Biol. , vol.12 , pp. 1864-1870
    • Tolliday, N.1    Verplank, L.2    Li, R.3
  • 18
    • 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
    • H. Imamura, K. Tanaka, T. Hihara, M. Umikawa, T. Kamei, K. Takahashi, T. Sasaki, and Y. Takai 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 1997 2745 2755
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5    Takahashi, K.6    Sasaki, T.7    Takai, Y.8
  • 19
    • 0037815488 scopus 로고    scopus 로고
    • Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast
    • Y. Dong, D. Pruyne, and A. Bretscher Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast J. Cell Biol. 161 2003 1081 1092
    • (2003) J. Cell Biol. , vol.161 , pp. 1081-1092
    • Dong, Y.1    Pruyne, D.2    Bretscher, A.3
  • 20
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • B.J. Wallar, and A.S. Alberts The formins: active scaffolds that remodel the cytoskeleton Trends Cell Biol. 13 2003 435 446
    • (2003) Trends Cell Biol. , vol.13 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 21
    • 2442436379 scopus 로고    scopus 로고
    • Pheromone-induced polarization is dependent on the Fus3p MAPK acting through the formin Bni1p
    • D. Matheos, M. Metodiev, E. Muller, D. Stone, and M.D. Rose Pheromone-induced polarization is dependent on the Fus3p MAPK acting through the formin Bni1p J. Cell Biol. 165 2004 99 109
    • (2004) J. Cell Biol. , vol.165 , pp. 99-109
    • Matheos, D.1    Metodiev, M.2    Muller, E.3    Stone, D.4    Rose, M.D.5
  • 22
    • 2642514777 scopus 로고    scopus 로고
    • Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells
    • Y. Wang, M.R. El-Zaru, H.K. Surks, and M.E. Mendelsohn Formin homology domain protein (FHOD1) is a cyclic GMP-dependent protein kinase I-binding protein and substrate in vascular smooth muscle cells J. Biol. Chem. 279 2004 24420 24426
    • (2004) J. Biol. Chem. , vol.279 , pp. 24420-24426
    • Wang, Y.1    El-Zaru, M.R.2    Surks, H.K.3    Mendelsohn, M.E.4
  • 23
    • 0036468733 scopus 로고    scopus 로고
    • Regulation of Wiskottâ€"Aldrich syndrome protein and related molecules
    • E. Caron Regulation of Wiskottâ€"Aldrich syndrome protein and related molecules Curr. Opin. Cell Biol. 14 2002 82 87
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 82-87
    • Caron, E.1
  • 24
    • 0142211212 scopus 로고    scopus 로고
    • Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90
    • S. Suetsugu, and T. Takenawa Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90 J. Biol. Chem. 278 2003 42515 42523
    • (2003) J. Biol. Chem. , vol.278 , pp. 42515-42523
    • Suetsugu, S.1    Takenawa, T.2
  • 25
    • 0036514271 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • M. Evangelista, D. Pruyne, D.C. Amberg, C. Boone, and A. Bretscher Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast Nat. Cell Biol. 4 2002 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
  • 26
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • I. Sagot, S.K. Klee, and D. Pellman Yeast formins regulate cell polarity by controlling the assembly of actin cables Nat. Cell Biol. 4 2002 42 50
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 28
    • 0346991750 scopus 로고    scopus 로고
    • A role for GEA1 and GEA2 in the organization of the actin cytoskeleton in Saccharomyces cerevisiae
    • E. Zakrzewska, M. Perron, A. Laroche, and D. Pallotta A role for GEA1 and GEA2 in the organization of the actin cytoskeleton in Saccharomyces cerevisiae Genetics 165 2003 985 995
    • (2003) Genetics , vol.165 , pp. 985-995
    • Zakrzewska, E.1    Perron, M.2    Laroche, A.3    Pallotta, D.4
  • 29
    • 0141521593 scopus 로고    scopus 로고
    • Role for Arf3p in development of polarity, but not endocytosis, in Saccharomyces cerevisiae
    • C.F. Huang, Y.W. Liu, L. Tung, C.H. Lin, and F.J. Lee Role for Arf3p in development of polarity, but not endocytosis, in Saccharomyces cerevisiae Mol. Biol. Cell 14 2003 3834 3847
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3834-3847
    • Huang, C.F.1    Liu, Y.W.2    Tung, L.3    Lin, C.H.4    Lee, F.J.5
  • 30
    • 0032900498 scopus 로고    scopus 로고
    • ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements
    • H. Radhakrishna, O. Al-Awar, Z. Khachikian, and J.G. Donaldson ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements J. Cell Sci. 112 Pt 6 1999 855 866
    • (1999) J. Cell Sci. , vol.112 , Issue.6 , pp. 855-866
    • Radhakrishna, H.1    Al-Awar, O.2    Khachikian, Z.3    Donaldson, J.G.4
  • 31
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin polymerization and defines the direction of cell motility
    • M. Ghosh, X. Song, G. Mouneimne, M. Sidani, D.S. Lawrence, and J.S. Condeelis Cofilin promotes actin polymerization and defines the direction of cell motility Science 304 2004 743 746
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 32
    • 12244303674 scopus 로고    scopus 로고
    • ADF/cofilin controls cell polarity during fibroblast migration
    • H.R. Dawe, L.S. Minamide, J.R. Bamburg, and L.P. Cramer ADF/cofilin controls cell polarity during fibroblast migration Curr. Biol. 13 2003 252 257
    • (2003) Curr. Biol. , vol.13 , pp. 252-257
    • Dawe, H.R.1    Minamide, L.S.2    Bamburg, J.R.3    Cramer, L.P.4
  • 33
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • J.R. Bamburg Proteins of the ADF/cofilin family: essential regulators of actin dynamics Annu. Rev. Cell Dev. Biol. 15 1999 185 230
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 34
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • I. Ichetovkin, W. Grant, and J. Condeelis Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex Curr. Biol. 12 2002 79 84
    • (2002) Curr. Biol. , vol.12 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 35
    • 0037452660 scopus 로고    scopus 로고
    • Polarised migration: Cofilin holds the front
    • M. Bailly, and G.E. Jones Polarised migration: cofilin holds the front Curr. Biol. 13 2003 R128 R130
    • (2003) Curr. Biol. , vol.13
    • Bailly, M.1    Jones, G.E.2
  • 36
    • 0036220079 scopus 로고    scopus 로고
    • Bud-site selection and cell polarity in budding yeast
    • A. Casamayor, and M. Snyder Bud-site selection and cell polarity in budding yeast Curr. Opin. Microbiol. 5 2002 179 186
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 179-186
    • Casamayor, A.1    Snyder, M.2
  • 37
    • 0032495489 scopus 로고    scopus 로고
    • A GTP-exchange factor required for cell orientation
    • A. Nern, and R.A. Arkowitz A GTP-exchange factor required for cell orientation Nature 391 1998 195 198
    • (1998) Nature , vol.391 , pp. 195-198
    • Nern, A.1    Arkowitz, R.A.2
  • 38
    • 0036773899 scopus 로고    scopus 로고
    • Temporal and spatial regulation of chemotaxis
    • M. Iijima, Y.E. Huang, and P. Devreotes Temporal and spatial regulation of chemotaxis Dev. Cell. 3 2002 469 478
    • (2002) Dev. Cell. , vol.3 , pp. 469-478
    • Iijima, M.1    Huang, Y.E.2    Devreotes, P.3
  • 39
    • 0042922893 scopus 로고    scopus 로고
    • Epithelial cell polarity from the outside looking in
    • W.J. Nelson Epithelial cell polarity from the outside looking in News Physiol. Sci. 18 2003 143 146
    • (2003) News Physiol. Sci. , vol.18 , pp. 143-146
    • Nelson, W.J.1
  • 41
    • 0034090975 scopus 로고    scopus 로고
    • The C. elegans par-4 gene encodes a putative serineâ€" threonine kinase required for establishing embryonic asymmetry
    • J.L. Watts, D.G. Morton, J. Bestman, and K.J. Kemphues The C. elegans par-4 gene encodes a putative serineâ€"threonine kinase required for establishing embryonic asymmetry Development 127 2000 1467 1475
    • (2000) Development , vol.127 , pp. 1467-1475
    • Watts, J.L.1    Morton, D.G.2    Bestman, J.3    Kemphues, K.J.4
  • 42
    • 0037458909 scopus 로고    scopus 로고
    • Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase
    • 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
    • (2003) Science , vol.299 , pp. 1231-1235
    • Wedlich-Soldner, R.1    Altschuler, S.2    Wu, L.3    Li, R.4
  • 43
    • 13144302852 scopus 로고    scopus 로고
    • A role for the yeast actin cytoskeleton in pheromone receptor clustering and signalling
    • K.R. Ayscough, and D.G. Drubin A role for the yeast actin cytoskeleton in pheromone receptor clustering and signalling Curr. Biol. 8 1998 927 930
    • (1998) Curr. Biol. , vol.8 , pp. 927-930
    • Ayscough, K.R.1    Drubin, D.G.2
  • 44
    • 0033846845 scopus 로고    scopus 로고
    • Gic2p may link activated Cdc42p to components involved in actin polarization, including Bni1p and Bud6p (Aip3p)
    • M. Jaquenoud, and M. Peter Gic2p may link activated Cdc42p to components involved in actin polarization, including Bni1p and Bud6p (Aip3p) Mol Cell. Biol. 20 2000 6244 6258
    • (2000) Mol Cell. Biol. , vol.20 , pp. 6244-6258
    • Jaquenoud, M.1    Peter, M.2
  • 45
    • 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
    • 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
    • (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
  • 47
    • 0033635230 scopus 로고    scopus 로고
    • Phosphorylation of the Cdc42 exchange factor Cdc24 by the PAK-like kinase Cla4 may regulate polarized growth in yeast
    • M.P. Gulli, M. Jaquenoud, Y. Shimada, G. Niederhauser, P. Wiget, and M. Peter Phosphorylation of the Cdc42 exchange factor Cdc24 by the PAK-like kinase Cla4 may regulate polarized growth in yeast Mol. Cell 6 2000 1155 1167
    • (2000) Mol. Cell , vol.6 , pp. 1155-1167
    • Gulli, M.P.1    Jaquenoud, M.2    Shimada, Y.3    Niederhauser, G.4    Wiget, P.5    Peter, M.6
  • 48
    • 0035831555 scopus 로고    scopus 로고
    • Assembly of scaffold-mediated complexes containing Cdc42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycle-regulated phosphorylation of Cdc24p
    • I. Bose, J.E. Irazoqui, J.J. Moskow, E.S. Bardes, T.R. Zyla, and D.J. Lew Assembly of scaffold-mediated complexes containing Cdc42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycle-regulated phosphorylation of Cdc24p J. Biol. Chem. 276 2001 7176 7186
    • (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
  • 49
    • 4544295912 scopus 로고    scopus 로고
    • Robust cell polarity is a dynamic state established by coupling transport and GTPase signalling
    • R. Wedlich-Soldner, C.S. Wai, T. Schmidt, and R. Li Robust cell polarity is a dynamic state established by coupling transport and GTPase signalling J. Cell Biol. 2004 (in press)
    • (2004) J. Cell Biol.
    • Wedlich-Soldner, R.1    Wai, C.S.2    Schmidt, T.3    Li, R.4
  • 51
    • 0141727533 scopus 로고    scopus 로고
    • Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling
    • 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
    • (2003) Curr. Biol. , vol.13 , pp. 1636-1640
    • Valdez-Taubas, J.1    Pelham, H.R.2
  • 52
    • 0038783734 scopus 로고    scopus 로고
    • Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation
    • H. Friesen, K. Murphy, A. Breitkreutz, M. Tyers, and B. Andrews Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation Mol. Biol. Cell 14 2003 3027 3040
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3027-3040
    • Friesen, H.1    Murphy, K.2    Breitkreutz, A.3    Tyers, M.4    Andrews, B.5
  • 53
    • 0033801741 scopus 로고    scopus 로고
    • Role of Cdc42p in pheromone-stimulated signal transduction in Saccharomyces cerevisiae
    • J.J. Moskow, A.S. Gladfelter, R.E. Lamson, P.M. Pryciak, and D.J. Lew Role of Cdc42p in pheromone-stimulated signal transduction in Saccharomyces cerevisiae Mol. Cell Biol. 20 2000 7559 7571
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7559-7571
    • Moskow, J.J.1    Gladfelter, A.S.2    Lamson, R.E.3    Pryciak, P.M.4    Lew, D.J.5
  • 54
    • 0036240658 scopus 로고    scopus 로고
    • Cdc42 regulation of kinase activity and signaling by the yeast p21-activated kinase Ste20
    • R.E. Lamson, M.J. Winters, and P.M. Pryciak Cdc42 regulation of kinase activity and signaling by the yeast p21-activated kinase Ste20 Mol. Cell Biol. 22 2002 2939 2951
    • (2002) Mol. Cell Biol. , vol.22 , pp. 2939-2951
    • Lamson, R.E.1    Winters, M.J.2    Pryciak, P.M.3
  • 55
    • 0037484259 scopus 로고    scopus 로고
    • Gbetagamma recruits Rho1 to the site of polarized growth during mating in budding yeast
    • E.E. Bar, A.T. Ellicott, and D.E. Stone Gbetagamma recruits Rho1 to the site of polarized growth during mating in budding yeast J. Biol. Chem. 278 2003 21798 21804
    • (2003) J. Biol. Chem. , vol.278 , pp. 21798-21804
    • Bar, E.E.1    Ellicott, A.T.2    Stone, D.E.3
  • 56
    • 1642539977 scopus 로고    scopus 로고
    • Regulation of polarized growth initiation and termination cycles by the polarisome and Cdc42 regulators
    • S. Bidlingmaier, and M. Snyder Regulation of polarized growth initiation and termination cycles by the polarisome and Cdc42 regulators J. Cell Biol. 164 2004 207 218
    • (2004) J. Cell Biol. , vol.164 , pp. 207-218
    • Bidlingmaier, S.1    Snyder, M.2
  • 57
    • 0034635567 scopus 로고    scopus 로고
    • Localization of the G protein betagamma complex in living cells during chemotaxis
    • T. Jin, N. Zhang, Y. Long, C.A. Parent, and P.N. Devreotes Localization of the G protein betagamma complex in living cells during chemotaxis [see comments] Science 287 2000 1034 1036
    • (2000) Science , vol.287 , pp. 1034-1036
    • Jin, T.1    Zhang, N.2    Long, Y.3    Parent, C.A.4    Devreotes, P.N.5
  • 58
    • 0036308458 scopus 로고    scopus 로고
    • Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils
    • F. Wang, P. Herzmark, O.D. Weiner, S. Srinivasan, G. Servant, and H.R. Bourne Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils Nat. Cell Biol. 4 2002 513 518
    • (2002) Nat. Cell Biol. , vol.4 , pp. 513-518
    • Wang, F.1    Herzmark, P.2    Weiner, O.D.3    Srinivasan, S.4    Servant, G.5    Bourne, H.R.6
  • 59
    • 0034640350 scopus 로고    scopus 로고
    • A membrane-permeant ester of phosphatidylinositol 3,4, 5-trisphosphate (PIP(3)) is an activator of human neutrophil migration
    • V. Niggli A membrane-permeant ester of phosphatidylinositol 3,4, 5-trisphosphate (PIP(3)) is an activator of human neutrophil migration FEBS Lett. 473 2000 217 221
    • (2000) FEBS Lett. , vol.473 , pp. 217-221
    • Niggli, V.1
  • 62
    • 0035928737 scopus 로고    scopus 로고
    • Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin
    • L. Blanchoin, T.D. Pollard, and S.E. Hitchcock-DeGregori Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin Curr. Biol. 11 2001 1300 1304
    • (2001) Curr. Biol. , vol.11 , pp. 1300-1304
    • Blanchoin, L.1    Pollard, T.D.2    Hitchcock-Degregori, S.E.3
  • 63
    • 0036912348 scopus 로고    scopus 로고
    • Spatial regulation of actin dynamics: A tropomyosin-free, actin-rich compartment at the leading edge
    • V. DesMarais, I. Ichetovkin, J. Condeelis, and S.E. Hitchcock-DeGregori Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge J. Cell Sci. 115 2002 4649 4660
    • (2002) J. Cell Sci. , vol.115 , pp. 4649-4660
    • Desmarais, V.1    Ichetovkin, I.2    Condeelis, J.3    Hitchcock-Degregori, S.E.4
  • 64
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • L.C. Cantley The phosphoinositide 3-kinase pathway Science 296 2002 1655 1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 65
    • 1942501586 scopus 로고    scopus 로고
    • Novel mechanism of PTEN regulation by its phosphatidylinositol 4,5-bisphosphate binding motif is critical for chemotaxis
    • M. Iijima, Y.E. Huang, H.R. Luo, F. Vazquez, and P.N. Devreotes Novel mechanism of PTEN regulation by its phosphatidylinositol 4,5-bisphosphate binding motif is critical for chemotaxis J. Biol. Chem. 279 2004 16606 16613
    • (2004) J. Biol. Chem. , vol.279 , pp. 16606-16613
    • Iijima, M.1    Huang, Y.E.2    Luo, H.R.3    Vazquez, F.4    Devreotes, P.N.5
  • 66
    • 0033868140 scopus 로고    scopus 로고
    • Pattern formation by local self-activation and lateral inhibition
    • H. Meinhardt, and A. Gierer Pattern formation by local self-activation and lateral inhibition BioEssays 22 2000 753 760
    • (2000) BioEssays , vol.22 , pp. 753-760
    • Meinhardt, H.1    Gierer, A.2
  • 67
    • 0015454185 scopus 로고
    • A theory of biological pattern formation
    • A. Gierer, and H. Meinhardt A theory of biological pattern formation Kybernetik 12 1972 30 39
    • (1972) Kybernetik , vol.12 , pp. 30-39
    • Gierer, A.1    Meinhardt, H.2
  • 68
    • 2942588534 scopus 로고    scopus 로고
    • From the cover: An actin-like gene can determine cell polarity in bacteria
    • Z. Gitai, N. Dye, and L. Shapiro From the cover: an actin-like gene can determine cell polarity in bacteria Proc. Natl. Acad. Sci. U. S. A. 101 2004 8643 8648
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8643-8648
    • Gitai, Z.1    Dye, N.2    Shapiro, L.3
  • 69
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • L.J. Jones, R. Carballido-Lopez, and J. Errington Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis Cell 104 2001 913 922
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 70
    • 0242381270 scopus 로고    scopus 로고
    • Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins
    • H.J. Soufo, and P.L. Graumann Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins Curr. Biol. 13 2003 1916 1920
    • (2003) Curr. Biol. , vol.13 , pp. 1916-1920
    • Soufo, H.J.1    Graumann, P.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.