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Volumn 202, Issue 7, 2013, Pages 1091-1106

Independence of symmetry breaking on Bem1-mediated autocatalytic activation of Cdc42

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; BEM1 PROTEIN; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PROTEIN CDC42; UNCLASSIFIED DRUG;

EID: 84886903385     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201304180     Document Type: Article
Times cited : (53)

References (58)
  • 1
    • 49649089500 scopus 로고    scopus 로고
    • On the spontaneous emergence of cell polarity
    • Altschuler, S.J., S.B. Angenent, Y. Wang, and L.F. Wu. 2008. On the spontaneous emergence of cell polarity. Nature. 454:886-889. http://dx.doi.org/10.1038/nature07119
    • (2008) Nature. , vol.454 , pp. 886-889
    • Altschuler, S.J.1    Angenent, S.B.2    Wang, Y.3    Wu, L.F.4
  • 2
    • 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, K.R., J. Stryker, N. Pokala, M. Sanders, P. Crews, and D.G. Drubin. 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. http://dx.doi.org/10.1083/jcb.137.2.399
    • (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
  • 3
    • 15844384186 scopus 로고    scopus 로고
    • Associations among PH and SH3 domain-containing proteins and Rho-type GTPases in Yeast
    • Bender, L., H.S. Lo, H. Lee, V. Kokojan, V. Peterson, and A. Bender. 1996. Associations among PH and SH3 domain-containing proteins and Rho-type GTPases in Yeast. J. Cell Biol. 133:879-894. http://dx.doi.org/10.1083/jcb.133.4.879
    • (1996) J. Cell Biol. , vol.133 , pp. 879-894
    • Bender, L.1    Lo, H.S.2    Lee, H.3    Kokojan, V.4    Peterson, V.5    Bender, A.6
  • 4
    • 0035831555 scopus 로고    scopus 로고
    • Assembly of scaffold-mediated complexes containing Cdc42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycleregulated phosphorylation of Cdc24p
    • Bose, I., J.E. Irazoqui, J.J. Moskow, E.S.G. Bardes, T.R. Zyla, and D.J. Lew. 2001. Assembly of scaffold-mediated complexes containing Cdc42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycleregulated phosphorylation of Cdc24p. J. Biol. Chem. 276:7176-7186. http://dx.doi.org/10.1074/jbc. M010546200
    • (2001) J. Biol. Chem. , vol.276 , pp. 7176-7186
    • Bose, I.1    Irazoqui, J.E.2    Moskow, J.J.3    Bardes, E.S.G.4    Zyla, T.R.5    Lew, D.J.6
  • 5
    • 0003559611 scopus 로고    scopus 로고
    • Methods in Yeast Genetics: a Cold Spring Harbor Laboratory Course Manual
    • Cold Spring Harbor Laboratory Press, Plainview, NY
    • Burke, D., D. Dawson, and T. Stearns. 2000. Methods in Yeast Genetics: a Cold Spring Harbor Laboratory Course Manual. Cold Spring Harbor Laboratory Press, Plainview, NY. 205 pp.
    • (2000) , pp. 205
    • Burke, D.1    Dawson, D.2    Stearns, T.3
  • 6
    • 0037007225 scopus 로고    scopus 로고
    • A positive feedback loop stabilizes the guanine-nucleotide exchange factor Cdc24 at sites of polarization
    • Butty, A.-C., N. Perrinjaquet, A. Petit, M. Jaquenoud, J.E. Segall, K. Hofmann, C. Zwahlen, and M. Peter. 2002. A positive feedback loop stabilizes the guanine-nucleotide exchange factor Cdc24 at sites of polarization. EMBO J. 21:1565-1576. http://dx.doi.org/10.1093/emboj/21.7.1565
    • (2002) EMBO J. , vol.21 , pp. 1565-1576
    • Butty, A.-C.1    Perrinjaquet, N.2    Petit, A.3    Jaquenoud, M.4    Segall, J.E.5    Hofmann, K.6    Zwahlen, C.7    Peter, M.8
  • 7
    • 0036220079 scopus 로고    scopus 로고
    • Bud-site selection and cell polarity in budding yeast
    • Casamayor, A., and M. Snyder. 2002. Bud-site selection and cell polarity in budding yeast. Curr. Opin. Microbiol. 5:179-186. http://dx.doi.org/10.1016/S1369-5274(02)00300-4
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 179-186
    • Casamayor, A.1    Snyder, M.2
  • 8
    • 84863419997 scopus 로고    scopus 로고
    • Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity
    • Das, A., B.D. Slaughter, J.R. Unruh, W.D. Bradford, R. Alexander, B. Rubinstein, and R. Li. 2012. Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity. Nat. Cell Biol. 14:304-310. http://dx.doi.org/10.1038/ncb2444
    • (2012) Nat. Cell Biol. , vol.14 , pp. 304-310
    • Das, A.1    Slaughter, B.D.2    Unruh, J.R.3    Bradford, W.D.4    Alexander, R.5    Rubinstein, B.6    Li, R.7
  • 9
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: central regulatory molecules in Rho GTPase activation
    • DerMardirossian, C., and G.M. Bokoch. 2005. GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol. 15:356-363. http://dx.doi.org/10.1016/j.tcb.2005.05.001
    • (2005) Trends Cell Biol. , vol.15 , pp. 356-363
    • DerMardirossian, C.1    Bokoch, G.M.2
  • 10
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42-the centre of polarity
    • Etienne-Manneville, S. 2004. Cdc42-the centre of polarity. J. Cell Sci. 117: 1291-1300. http://dx.doi.org/10.1242/jcs.01115
    • (2004) J. Cell Sci. , vol.117 , pp. 1291-1300
    • Etienne-Manneville, S.1
  • 12
    • 1242316183 scopus 로고    scopus 로고
    • Rax1, a protein required for the establishment of the bipolar budding pattern in yeast
    • Fujita, A., M. Lord, T. Hiroko, F. Hiroko, T. Chen, C. Oka, Y. Misumi, and J. Chant. 2004. Rax1, a protein required for the establishment of the bipolar budding pattern in yeast. Gene. 327:161-169. http://dx.doi.org/10.1016/j.gene.2003.11.021
    • (2004) Gene. , vol.327 , pp. 161-169
    • Fujita, A.1    Lord, M.2    Hiroko, T.3    Hiroko, F.4    Chen, T.5    Oka, C.6    Misumi, Y.7    Chant, J.8
  • 13
    • 34548176518 scopus 로고    scopus 로고
    • Sequential and distinct roles of the cadherin domain-containing protein Axl2p in cell polarization in yeast cell cycle
    • Gao, X.-D., L.M. Sperber, S.A. Kane, Z. Tong, A.H.Y. Tong, C. Boone, and E. Bi. 2007. Sequential and distinct roles of the cadherin domain-containing protein Axl2p in cell polarization in yeast cell cycle. Mol. Biol. Cell. 18:2542-2560. http://dx.doi.org/10.1091/mbc. E06-09-0822
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 2542-2560
    • Gao, X.-D.1    Sperber, L.M.2    Kane, S.A.3    Tong, Z.4    Tong, A.H.Y.5    Boone, C.6    Bi, E.7
  • 14
    • 82255175673 scopus 로고    scopus 로고
    • Polarization of PAR proteins by advective triggering of a pattern-forming system
    • Goehring, N.W., P.K. Trong, J.S. Bois, D. Chowdhury, E.M. Nicola, A.A. Hyman, and S.W. Grill. 2011. Polarization of PAR proteins by advective triggering of a pattern-forming system. Science. 334:1137-1141. http://dx.doi.org/10.1126/science.1208619
    • (2011) Science. , vol.334 , pp. 1137-1141
    • Goehring, N.W.1    Trong, P.K.2    Bois, J.S.3    Chowdhury, D.4    Nicola, E.M.5    Hyman, A.A.6    Grill, S.W.7
  • 15
    • 33846002372 scopus 로고    scopus 로고
    • Computational model explains high activity and rapid cycling of Rho GTPases within protein complexes
    • Goryachev, A.B., and A.V. Pokhilko. 2006. Computational model explains high activity and rapid cycling of Rho GTPases within protein complexes. PLOS Comput. Biol. 2:e172. http://dx.doi.org/10.1371/journal.pcbi.0020172
    • (2006) PLOS Comput. Biol. , vol.2
    • Goryachev, A.B.1    Pokhilko, A.V.2
  • 16
    • 42049115235 scopus 로고    scopus 로고
    • Dynamics of Cdc42 network embodies a Turing-type mechanism of yeast cell polarity
    • Goryachev, A.B., and A.V. Pokhilko. 2008. Dynamics of Cdc42 network embodies a Turing-type mechanism of yeast cell polarity. FEBS Lett. 582:1437-1443. http://dx.doi.org/10.1016/j.febslet.2008.03.029
    • (2008) FEBS Lett. , vol.582 , pp. 1437-1443
    • Goryachev, A.B.1    Pokhilko, A.V.2
  • 17
    • 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.-P., M. Jaquenoud, Y. Shimada, G. Niederhäuser, P. Wiget, and M. Peter. 2000. Phosphorylation of the Cdc42 exchange factor Cdc24 by the PAK-like kinase Cla4 may regulate polarized growth in yeast. Mol. Cell. 6:1155-1167. http://dx.doi.org/10.1016/S1097-2765(00)00113-1
    • (2000) Mol. Cell. , vol.6 , pp. 1155-1167
    • Gulli, M.-P.1    Jaquenoud, M.2    Shimada, Y.3    Niederhäuser, G.4    Wiget, P.5    Peter, M.6
  • 18
    • 37249008219 scopus 로고    scopus 로고
    • Design and optimization of genetically encoded fluorescent biosensors: GTPase biosensors
    • Hodgson, L., O. Pertz, and K.M. Hahn. 2008. Design and optimization of genetically encoded fluorescent biosensors: GTPase biosensors. Methods Cell Biol. 85:63-81. http://dx.doi.org/10.1016/S0091-679X(08)85004-2
    • (2008) Methods Cell Biol. , vol.85 , pp. 63-81
    • Hodgson, L.1    Pertz, O.2    Hahn, K.M.3
  • 20
    • 84859760140 scopus 로고    scopus 로고
    • Negative feedback enhances robustness in the yeast polarity establishment circuit
    • Howell, A.S., M. Jin, C.F. Wu, T.R. Zyla, T.C. Elston, and D.J. Lew. 2012. Negative feedback enhances robustness in the yeast polarity establishment circuit. Cell. 149:322-333. http://dx.doi.org/10.1016/j.cell.2012.03.012
    • (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
  • 21
    • 0344394312 scopus 로고    scopus 로고
    • Scaffold-mediated symmetry breaking by Cdc42p
    • Irazoqui, J.E., A.S. Gladfelter, and D.J. Lew. 2003. Scaffold-mediated symmetry breaking by Cdc42p. Nat. Cell Biol. 5:1062-1070. http://dx.doi.org/10.1038/ncb1068
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1062-1070
    • Irazoqui, J.E.1    Gladfelter, A.S.2    Lew, D.J.3
  • 22
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 23
    • 0035421216 scopus 로고    scopus 로고
    • Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions
    • Ito, T., Y. Matsui, T. Ago, K. Ota, and H. Sumimoto. 2001. Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions. EMBO J. 20:3938-3946. http://dx.doi.org/10.1093/emboj/20.15.3938
    • (2001) EMBO J. , vol.20 , pp. 3938-3946
    • Ito, T.1    Matsui, Y.2    Ago, T.3    Ota, K.4    Sumimoto, H.5
  • 24
    • 0036724188 scopus 로고    scopus 로고
    • Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells
    • Itoh, R.E., K. Kurokawa, Y. Ohba, H. Yoshizaki, N. Mochizuki, and M. Matsuda. 2002. Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells. Mol. Cell. Biol. 22:6582-6591. http://dx.doi.org/10.1128/MCB.22.18.6582-6591.2002
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6582-6591
    • Itoh, R.E.1    Kurokawa, K.2    Ohba, Y.3    Yoshizaki, H.4    Mochizuki, N.5    Matsuda, M.6
  • 25
    • 84874359444 scopus 로고    scopus 로고
    • Robust polarity establishment occurs via an endocytosis-based cortical corralling mechanism
    • Jose, M., S. Tollis, D. Nair, J.-B. Sibarita, and D. McCusker. 2013. Robust polarity establishment occurs via an endocytosis-based cortical corralling mechanism. J. Cell Biol. 200:407-418. http://dx.doi.org/10.1083/jcb.201206081
    • (2013) J. Cell Biol. , vol.200 , pp. 407-418
    • Jose, M.1    Tollis, S.2    Nair, D.3    Sibarita, J.-B.4    McCusker, D.5
  • 26
    • 77956253990 scopus 로고    scopus 로고
    • The Rsr1/Bud1 GTPase interacts with itself and the Cdc42 GTPase during bud-site selection and polarity establishment in budding yeast
    • Kang, P.J., L. Béven, S. Hariharan, and H.-O. Park. 2010. The Rsr1/Bud1 GTPase interacts with itself and the Cdc42 GTPase during bud-site selection and polarity establishment in budding yeast. Mol. Biol. Cell. 21:3007-3016. http://dx.doi.org/10.1091/mbc. E10-03-0232
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 3007-3016
    • Kang, P.J.1    Béven, L.2    Hariharan, S.3    Park, H.-O.4
  • 27
    • 0030799904 scopus 로고    scopus 로고
    • Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae
    • Koch, G., K. Tanaka, T. Masuda, W. Yamochi, H. Nonaka, and Y. Takai. 1997. Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae. Oncogene. 15:417-422. http://dx.doi.org/10.1038/sj.onc.1201194
    • (1997) Oncogene. , vol.15 , pp. 417-422
    • Koch, G.1    Tanaka, K.2    Masuda, T.3    Yamochi, W.4    Nonaka, H.5    Takai, Y.6
  • 28
    • 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, K.G., L. Beven, E. Angerman, A.H.Y. Tong, C. Boone, and H.-O. Park. 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. 14:4958-4970. http://dx.doi.org/10.1091/mbc. E03-06-0426
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 4958-4970
    • Kozminski, K.G.1    Beven, L.2    Angerman, E.3    Tong, A.H.Y.4    Boone, C.5    Park, H.-O.6
  • 29
    • 56349125826 scopus 로고    scopus 로고
    • Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex
    • Kozubowski, L., K. Saito, J.M. Johnson, A.S. Howell, T.R. Zyla, and D.J. Lew. 2008. Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex. Curr. Biol. 18:1719-1726. http://dx.doi.org/10.1016/j.cub.2008.09.060
    • (2008) Curr. Biol. , vol.18 , pp. 1719-1726
    • Kozubowski, L.1    Saito, K.2    Johnson, J.M.3    Howell, A.S.4    Zyla, T.R.5    Lew, D.J.6
  • 30
    • 84861552972 scopus 로고    scopus 로고
    • Network crosstalk dynamically changes during neutrophil polarization
    • Ku, C.-J., Y. Wang, O.D. Weiner, S.J. Altschuler, and L.F. Wu. 2012. Network crosstalk dynamically changes during neutrophil polarization. Cell. 149:1073-1083. http://dx.doi.org/10.1016/j.cell.2012.03.044
    • (2012) Cell. , vol.149 , pp. 1073-1083
    • Ku, C.-J.1    Wang, Y.2    Weiner, O.D.3    Altschuler, S.J.4    Wu, L.F.5
  • 31
    • 0034486070 scopus 로고    scopus 로고
    • The identification of conserved interactions within the SH3 domain by alignment of sequences and structures
    • Larson, S.M., and A.R. Davidson. 2000. The identification of conserved interactions within the SH3 domain by alignment of sequences and structures. Protein Sci. 9:2170-2180. http://dx.doi.org/10.1110/ps.9.11.2170
    • (2000) Protein Sci. , vol.9 , pp. 2170-2180
    • Larson, S.M.1    Davidson, A.R.2
  • 32
    • 0032090603 scopus 로고    scopus 로고
    • An iterative algorithm for minimum cross entropy thresholding
    • Li, C.H., and P.K.S. Tam. 1998. An iterative algorithm for minimum cross entropy thresholding. Pattern Recognit. Lett. 18:771-776. http://dx.doi.org/10.1016/S0167-8655(98)00057-9
    • (1998) Pattern Recognit. Lett. , vol.18 , pp. 771-776
    • Li, C.H.1    Tam, P.K.S.2
  • 33
    • 54549102288 scopus 로고    scopus 로고
    • Beyond polymer polarity: how the cytoskeleton builds a polarized cell
    • Li, R., and G.G. Gundersen. 2008. Beyond polymer polarity: how the cytoskeleton builds a polarized cell. Nat. Rev. Mol. Cell Biol. 9:860-873. http://dx.doi.org/10.1038/nrm2522
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 860-873
    • Li, R.1    Gundersen, G.G.2
  • 34
    • 34147175165 scopus 로고    scopus 로고
    • Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity
    • Marco, E., R. Wedlich-Soldner, R. Li, S.J. Altschuler, and L.F. Wu. 2007. Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity. Cell. 129:411-422. http://dx.doi.org/10.1016/j.cell.2007.02.043
    • (2007) Cell. , vol.129 , pp. 411-422
    • Marco, E.1    Wedlich-Soldner, R.2    Li, R.3    Altschuler, S.J.4    Wu, L.F.5
  • 35
    • 77955501804 scopus 로고    scopus 로고
    • Widely conserved signaling pathways in the establishment of cell polarity
    • McCaffrey, L.M., and I.G. Macara. 2009. Widely conserved signaling pathways in the establishment of cell polarity. Cold Spring Harb. Perspect. Biol. 1:a001370. http://dx.doi.org/10.1101/cshperspect.a001370
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1
    • McCaffrey, L.M.1    Macara, I.G.2
  • 36
    • 80052734197 scopus 로고    scopus 로고
    • Asymptotic and bifurcation analysis of wave-pinning in a reaction-diffusion model for cell plarization
    • Mori, Y., A. Jilkine, and L. Edelstein-Keshet. 2011. Asymptotic and bifurcation analysis of wave-pinning in a reaction-diffusion model for cell plarization. SIAM J. Appl. Math. 71:1401-1427. http://dx.doi.org/10.1137/10079118X
    • (2011) SIAM J. Appl. Math. , vol.71 , pp. 1401-1427
    • Mori, Y.1    Jilkine, A.2    Edelstein-Keshet, L.3
  • 37
    • 60749120831 scopus 로고    scopus 로고
    • Calling heads from tails: the role of mathematical modeling in understanding cell polarization
    • Onsum, M.D., and C.V. Rao. 2009. Calling heads from tails: the role of mathematical modeling in understanding cell polarization. Curr. Opin. Cell Biol. 21:74-81. http://dx.doi.org/10.1016/j.ceb.2009.01.001
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 74-81
    • Onsum, M.D.1    Rao, C.V.2
  • 38
    • 34347352254 scopus 로고    scopus 로고
    • A mass conserved reaction-diffusion system captures properties of cell polarity
    • Otsuji, M., S. Ishihara, C. Co, K. Kaibuchi, A. Mochizuki, and S. Kuroda. 2007. A mass conserved reaction-diffusion system captures properties of cell polarity. PLOS Comput. Biol. 3:e108. http://dx.doi.org/10.1371/journal.pcbi.0030108
    • (2007) PLOS Comput. Biol. , vol.3
    • Otsuji, M.1    Ishihara, S.2    Co, C.3    Kaibuchi, K.4    Mochizuki, A.5    Kuroda, S.6
  • 39
    • 26444469935 scopus 로고    scopus 로고
    • A system of counteracting feedback loops regulates Cdc42p activity during spontaneous cell polarization
    • Ozbudak, E.M., A. Becskei, and A. van Oudenaarden. 2005. A system of counteracting feedback loops regulates Cdc42p activity during spontaneous cell polarization. Dev. Cell. 9:565-571. http://dx.doi.org/10.1016/j.devcel.2005.08.014
    • (2005) Dev. Cell. , vol.9 , pp. 565-571
    • Ozbudak, E.M.1    Becskei, A.2    van Oudenaarden, A.3
  • 40
    • 33947398366 scopus 로고    scopus 로고
    • Central roles of small GTPases in the development of cell polarity in yeast and beyond
    • Park, H.-O., and E. Bi. 2007. Central roles of small GTPases in the development of cell polarity in yeast and beyond. Microbiol. Mol. Biol. Rev. 71:48-96. http://dx.doi.org/10.1128/MMBR.00028-06
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 48-96
    • Park, H.-O.1    Bi, E.2
  • 41
    • 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, H.-O., E. Bi, J.R. Pringle, and I. Herskowitz. 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. 94:4463-4468. http://dx.doi.org/10.1073/pnas.94.9.4463
    • (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
  • 42
    • 0037178792 scopus 로고    scopus 로고
    • Localization of the Rsr1/Bud1 GTPase involved in selection of a proper growth site in yeast
    • Park, H.-O., P.J. Kang, and A.W. Rachfal. 2002. Localization of the Rsr1/Bud1 GTPase involved in selection of a proper growth site in yeast. J. Biol. Chem. 277:26721-26724. http://dx.doi.org/10.1074/jbc. C200245200
    • (2002) J. Biol. Chem. , vol.277 , pp. 26721-26724
    • Park, H.-O.1    Kang, P.J.2    Rachfal, A.W.3
  • 43
    • 0028148453 scopus 로고
    • Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast
    • Peterson, J., Y. Zheng, L. Bender, A. Myers, R. Cerione, and A. Bender. 1994. Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast. J. Cell Biol. 127:1395-1406. http://dx.doi.org/10.1083/jcb.127.5.1395
    • (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
  • 44
    • 0029995116 scopus 로고    scopus 로고
    • Selection of axial growth sites in yeast requires Axl2p, a novel plasma membrane glycoprotein
    • Roemer, T., K. Madden, J. Chang, and M. Snyder. 1996. Selection of axial growth sites in yeast requires Axl2p, a novel plasma membrane glycoprotein. Genes Dev. 10:777-793. http://dx.doi.org/10.1101/gad.10.7.777
    • (1996) Genes Dev. , vol.10 , pp. 777-793
    • Roemer, T.1    Madden, K.2    Chang, J.3    Snyder, M.4
  • 45
    • 84864939929 scopus 로고    scopus 로고
    • Weakly nonlinear analysis of symmetry breaking in cell polarity models
    • Rubinstein, B., B.D. Slaughter, and R. Li. 2012. Weakly nonlinear analysis of symmetry breaking in cell polarity models. Phys. Biol. 9:045006. http://dx.doi.org/10.1088/1478-3975/9/4/045006
    • (2012) Phys. Biol. , vol.9 , pp. 045006
    • Rubinstein, B.1    Slaughter, B.D.2    Li, R.3
  • 46
    • 0033553672 scopus 로고    scopus 로고
    • O-Glycosylation of Axl2/Bud10p by Pmt4p is required for its stability, localization, and function in daughter cells
    • Sanders, S.L., M. Gentzsch, W. Tanner, and I. Herskowitz. 1999. O-Glycosylation of Axl2/Bud10p by Pmt4p is required for its stability, localization, and function in daughter cells. J. Cell Biol. 145:1177-1188. http://dx.doi.org/10.1083/jcb.145.6.1177
    • (1999) J. Cell Biol. , vol.145 , pp. 1177-1188
    • Sanders, S.L.1    Gentzsch, M.2    Tanner, W.3    Herskowitz, I.4
  • 47
    • 84861165097 scopus 로고    scopus 로고
    • Mechanistic mathematical model of polarity in yeast
    • Savage, N.S., A.T. Layton, and D.J. Lew. 2012. Mechanistic mathematical model of polarity in yeast. Mol. Biol. Cell. 23:1998-2013. http://dx.doi.org/10.1091/mbc. E11-10-0837
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 1998-2013
    • Savage, N.S.1    Layton, A.T.2    Lew, D.J.3
  • 48
    • 77955657497 scopus 로고    scopus 로고
    • Cell-length-dependent microtubule accumulation during polarization
    • Seetapun, D., and D.J. Odde. 2010. Cell-length-dependent microtubule accumulation during polarization. Curr. Biol. 20:979-988. http://dx.doi.org/10.1016/j.cub.2010.04.040
    • (2010) Curr. Biol. , vol.20 , pp. 979-988
    • Seetapun, D.1    Odde, D.J.2
  • 49
    • 1842472163 scopus 로고    scopus 로고
    • The nucleotide exchange factor Cdc24p may be regulated by auto-inhibition
    • Shimada, Y., P. Wiget, M.-P. Gulli, E. Bi, and M. Peter. 2004. The nucleotide exchange factor Cdc24p may be regulated by auto-inhibition. EMBO J. 23:1051-1062. http://dx.doi.org/10.1038/sj.emboj.7600124
    • (2004) EMBO J. , vol.23 , pp. 1051-1062
    • Shimada, Y.1    Wiget, P.2    Gulli, M.-P.3    Bi, E.4    Peter, M.5
  • 50
    • 71649099053 scopus 로고    scopus 로고
    • Dual modes of cdc42 recycling fine-tune polarized morphogenesis
    • Slaughter, B.D., A. Das, J.W. Schwartz, B. Rubinstein, and R. Li. 2009. Dual modes of cdc42 recycling fine-tune polarized morphogenesis. Dev. Cell. 17:823-835. http://dx.doi.org/10.1016/j.devcel.2009.10.022
    • (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
  • 51
    • 84878594706 scopus 로고    scopus 로고
    • Non-uniform membrane diffusion enables steady-state cell polarization via vesicular trafficking
    • Slaughter, B.D., J.R. Unruh, A. Das, S.E. Smith, B. Rubinstein, and R. Li. 2013. Non-uniform membrane diffusion enables steady-state cell polarization via vesicular trafficking. Nat Commun. 4:1380. http://dx.doi.org/10.1038/ncomms2370
    • (2013) Nat Commun. , vol.4 , pp. 1380
    • Slaughter, B.D.1    Unruh, J.R.2    Das, A.3    Smith, S.E.4    Rubinstein, B.5    Li, R.6
  • 52
    • 51349126086 scopus 로고    scopus 로고
    • The Rho GDI Rdi1 regulates Rho GTPases by distinct mechanisms
    • Tiedje, C., I. Sakwa, U. Just, and T. Höfken. 2008. The Rho GDI Rdi1 regulates Rho GTPases by distinct mechanisms. Mol. Biol. Cell. 19:2885-2896. http://dx.doi.org/10.1091/mbc. E07-11-1152
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 2885-2896
    • Tiedje, C.1    Sakwa, I.2    Just, U.3    Höfken, T.4
  • 53
    • 1242339667 scopus 로고    scopus 로고
    • Insight into molecular interactions between two PB1 domains
    • van Drogen-Petit, A., C. Zwahlen, M. Peter, and A.M.J.J. Bonvin. 2004. Insight into molecular interactions between two PB1 domains. J. Mol. Biol. 336:1195-1210. http://dx.doi.org/10.1016/j.jmb.2003.12.062
    • (2004) J. Mol. Biol. , vol.336 , pp. 1195-1210
    • van Drogen-Petit, A.1    Zwahlen, C.2    Peter, M.3    Bonvin, A.M.J.J.4
  • 54
    • 68749086088 scopus 로고    scopus 로고
    • Multisite phosphorylation of the guanine nucleotide exchange factor Cdc24 during yeast cell polarization
    • Wai, S.C., S.A. Gerber, and R. Li. 2009. Multisite phosphorylation of the guanine nucleotide exchange factor Cdc24 during yeast cell polarization. PLoS ONE. 4:e6563. http://dx.doi.org/10.1371/journal.pone.0006563
    • (2009) PLoS ONE. , vol.4
    • Wai, S.C.1    Gerber, S.A.2    Li, R.3
  • 55
    • 0037458909 scopus 로고    scopus 로고
    • Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase
    • Wedlich-Soldner, R., S. Altschuler, L. Wu, and R. Li. 2003. Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase. Science. 299:1231-1235. http://dx.doi.org/10.1126/science.1080944
    • (2003) Science. , vol.299 , pp. 1231-1235
    • Wedlich-Soldner, R.1    Altschuler, S.2    Wu, L.3    Li, R.4
  • 56
    • 4544295912 scopus 로고    scopus 로고
    • Robust cell polarity is a dynamic state established by coupling transport and GTPase signaling
    • Wedlich-Soldner, R., S.C. Wai, T. Schmidt, and R. Li. 2004. Robust cell polarity is a dynamic state established by coupling transport and GTPase signaling. J. Cell Biol. 166:889-900. http://dx.doi.org/10.1083/jcb.200405061
    • (2004) J. Cell Biol. , vol.166 , pp. 889-900
    • Wedlich-Soldner, R.1    Wai, S.C.2    Schmidt, T.3    Li, R.4
  • 58
    • 0028955710 scopus 로고
    • Interactions among proteins involved in bud-site selection and bud-site assembly in Saccharomyces cerevisiae
    • Zheng, Y., A. Bender, and R.A. Cerione. 1995. Interactions among proteins involved in bud-site selection and bud-site assembly in Saccharomyces cerevisiae. J. Biol. Chem. 270:626-630. http://dx.doi.org/10.1074/jbc.270.2.626
    • (1995) J. Biol. Chem. , vol.270 , pp. 626-630
    • Zheng, Y.1    Bender, A.2    Cerione, R.A.3


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