메뉴 건너뛰기




Volumn 21, Issue 7, 2010, Pages 1253-1262

The yeast formin bnr1p has two localization regions that show spatially and temporally distinct association with septin structures

Author keywords

[No Author keywords available]

Indexed keywords

BNR1P L1 PROTEIN; BNR1P L2 PROTEIN; PROTEIN; SEPTIN; UNCLASSIFIED DRUG;

EID: 77950685176     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E09-10-0861     Document Type: Article
Times cited : (25)

References (35)
  • 1
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxy1-terminal Diaphanous-related formin homology protein autoregulfltory domain
    • Alberts, A. S. (2001). Identification of a carboxy1-terminal Diaphanous-related formin homology protein autoregulfltory domain. J. Biol. Chem. 276, 28242830.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 3
    • 0034009550 scopus 로고    scopus 로고
    • Regulation of cytokinesis by the Elm1 protein kinase in Saccharomyces cerevisiae
    • Bouquin, N., Barrai, Y., Courbeyrette, R., Blondel, M., Snyder, M., and Mann, C. (2000). Regulation of cytokinesis by the Elm1 protein kinase in Saccharomyces cerevisiae. J. Cell Sci. 113(Pt 8), 1435-1445.
    • (2000) J. Cell Sci. , vol.113 , Issue.PT 8 , pp. 1435-1445
    • Bouquin, N.1    Barrai, Y.2    Courbeyrette, R.3    Blondel, M.4    Snyder, M.5    Mann, C.6
  • 4
    • 34248170173 scopus 로고    scopus 로고
    • Yeast formins Bnil and Bnrl utilize different modes of cortical interaction during the assembly of actin cables
    • Buttery, S. M., Yoshida, S., and Pellman, D. (2007). Yeast formins Bnil and Bnrl utilize different modes of cortical interaction during the assembly of actin cables. Mol. Biol. Cell 18, 1826-1838.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1826-1838
    • Buttery, S.M.1    Yoshida, S.2    Pellman, D.3
  • 5
    • 0030958087 scopus 로고    scopus 로고
    • Cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • DOI 10.1083/jcb.137.1.169
    • Chang, F., Drubin, D., and Nurse, P. (1997). cdcl2p, a protein required for cytokinesis in fission, yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 137, 169-182. (Pubitemid 27167304)
    • (1997) Journal of Cell Biology , vol.137 , Issue.1 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 6
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista, M., Pruyne, D., Amberg, D. C., Boone, C., and Bretscher, A. (2002). Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4, 32-41.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 7
    • 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., and Takai, Y. (1998). Rholp-Bnilp-Spa2p interactions: implication in localization, of Bnilp 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
  • 8
    • 44949183635 scopus 로고    scopus 로고
    • Analysis of unregulated formin activity reveals how yeast can balance F-actin assembly between different microfilament-based organizations
    • Gao, L., and Bretscher, A. (2008). Analysis of unregulated formin activity reveals how yeast can balance F-actin assembly between different microfilament-based organizations. Mol. Biol. Cell 19, 1474-1484.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1474-1484
    • Gao, L.1    Bretscher, A.2
  • 9
    • 66249091620 scopus 로고    scopus 로고
    • Polarized growth in budding yeast in the absence of a localized formin
    • Gao, L., and 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
  • 11
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode, B. L., and Eck, M. J. (2007). Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 76, 593-627.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 12
    • 11144281883 scopus 로고    scopus 로고
    • Phylogenetic analysis of the formin homology 2 domain
    • Higgs, H. N., and Peterson, K. J. (2005). Phylogenetic analysis of the formin homology 2 domain. Mol. Biol. Cell 16, 1-13.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1-13
    • Higgs, H.N.1    Peterson, K.J.2
  • 14
    • 0033604447 scopus 로고    scopus 로고
    • An FH domain-containing Bnr1p is a multifunctional protein interacting with a variety of cytoskeletal proteins in Saccharomyces cerevisiae
    • Kikyo, M., Tanaka, K., Kamei, T., Ozaki, K., Fujiwara, T., Inoue, E., Takita, Y., Ohya, Y., and Takai, Y. (1999). An FH domain-containing Bnr1p is a multifunctional protein, interacting with a variety of cytoskeletal proteins in Saccharomyces cerevisiae. Oncogene 18, 7046-7054. (Pubitemid 30028875)
    • (1999) Oncogene , vol.18 , Issue.50 , pp. 7046-7054
    • Kikyo, M.1    Tanaka, K.2    Kamei, T.3    Ozaki, K.4    Fujiwara, T.5    Inoue, E.6    Takita, Y.7    Ohya, Y.8    Takai, Y.9
  • 15
    • 1342310742 scopus 로고    scopus 로고
    • Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
    • Kobielak, A., Pasolli, H. A., and Fuchs, E. (2004). Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables. Nat. Cell Biol. 6, 21-30.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 21-30
    • Kobielak, A.1    Pasolli, H.A.2    Fuchs, E.3
  • 16
    • 0344309014 scopus 로고    scopus 로고
    • The morphogenesis checkpoint: How yeast cells watch their figures
    • Lew, D. J. (2003). The morphogenesis checkpoint: how yeast cells watch their figures. Curr. Opin. Cell Biol. 15, 648-653.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 648-653
    • Lew, D.J.1
  • 17
    • 14844288286 scopus 로고    scopus 로고
    • Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDial
    • Li, F., and Higgs, H. N. (2005). Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDial. J. Biol. Chem. 280, 6986-6992.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6986-6992
    • Li, F.1    Higgs, H.N.2
  • 18
    • 0026737743 scopus 로고
    • Construction of a GAL1-regulated yeast cDNA expression library and its application to the identification of genes whose overexpression causes lethality in yeast
    • Liu, H., Krizek, J., and Bretscher, A. (1992). Construction of a GAL1-regulated yeast cDNA expression library and its application to the identification of genes whose overexpression causes lethality in yeast. Genetics 132, 665-673.
    • (1992) Genetics , vol.132 , pp. 665-673
    • Liu, H.1    Krizek, J.2    Bretscher, A.3
  • 19
    • 0032476712 scopus 로고    scopus 로고
    • Role of the yeast gin4p protein kinase in septin assembly and the relationship between septin assembly and septin function
    • DOI 10.1083/jcb.143.3.719
    • Longtine, M. S., Fares, H., and Pringle, J. R. (1998). Role of the yeast Gin4p protein kinase in septin assembly and the relationship between septin assembly and septin function. J. Cell Biol. 143, 719-736. (Pubitemid 28512567)
    • (1998) Journal of Cell Biology , vol.143 , Issue.3 , pp. 719-736
    • Longtine, M.S.1    Fares, H.2    Pringle, J.R.3
  • 20
    • 0034739839 scopus 로고    scopus 로고
    • Cell cycle programs of gene expression control morphogenetic protein localization
    • DOI 10.1083/jcb.151.7.1501
    • Lord, M., Yang, M. C., Mischke, M., and Chant, J. (2000). Cell cycle programs of gene expression control morphogenetic protein localization. J. Cell Biol. 152, 1501-1512. (Pubitemid 32047598)
    • (2000) Journal of Cell Biology , vol.151 , Issue.7 , pp. 1501-1511
    • Lord, M.1    Yang, M.C.2    Mischke, M.3    Chant, J.4
  • 21
    • 32044470440 scopus 로고    scopus 로고
    • Structure of the autoinhibitory switch in formin mDia1
    • DOI 10.1016/j.str.2005.12.003, PII S0969212606000451
    • Nezami, A. G., Poy, F., and Eck, M. J. (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
  • 22
    • 3242877719 scopus 로고    scopus 로고
    • Dissection of septin actin interactions using actin overexpression in Saccharomyces cerevisiae
    • Norden, C., Liakopoulos, D., and Barral, Y. (2004). Dissection of septin actin interactions using actin overexpression in Saccharomyces cerevisiae. Mol. Microbiol. 53, 469-483.
    • (2004) Mol. Microbiol. , vol.53 , pp. 469-483
    • Norden, C.1    Liakopoulos, D.2    Barral, Y.3
  • 23
    • 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, D. R., Machius, M., and Rosen, M. K. (2005). Structural basis of Rho GTPase-mediated activation of the formin mDial. 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
  • 24
    • 0035137208 scopus 로고    scopus 로고
    • Dynamic localization and function of Bnilp at the sites of directed growth in Saccharomyces cerevisiae
    • Ozaki-Kuroda, K., Yamamoto, Y., Nohara, H., Kinoshita, M., Fujiwara, T., Irie, K., and Takai, Y. (2001). Dynamic localization and function of Bnilp at the sites of directed growth in Saccharomyces cerevisiae. Mol. Cell. Biol. 21, 827-839.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 827-839
    • Ozaki-Kuroda, K.1    Yamamoto, Y.2    Nohara, H.3    Kinoshita, M.4    Fujiwara, T.5    Irie, K.6    Takai, Y.7
  • 25
    • 12544253725 scopus 로고    scopus 로고
    • The Rho family GTPase Rif induces filopodia through mDia2
    • Pellegrin, S., and Mellor, H. (2005). The Rho family GTPase Rif induces filopodia through mDia2. Curr. Biol. 25, 129-133.
    • (2005) Curr. Biol. , vol.25 , pp. 129-133
    • Pellegrin, S.1    Mellor, H.2
  • 26
    • 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., and 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
  • 27
    • 6344275302 scopus 로고    scopus 로고
    • Stable and dynamic axes of polarity use distinct formin isoforms in budding yeast
    • Pruyne, D., Gao, L., Bi, E., and Bretscher, A. (2004a). Stable and dynamic axes of polarity use distinct formin isoforms in budding yeast. Mol. Biol. Cell 15, 4971-4989.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4971-4989
    • Pruyne, D.1    Gao, L.2    Bi, E.3    Bretscher, A.4
  • 29
    • 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, M. R., and 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
  • 31
    • 33748123994 scopus 로고    scopus 로고
    • Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLα and mDia1
    • DOI 10.1083/jcb.200605006
    • Seth, A., Otomo, C., and Rosen, M. K. (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
  • 32
    • 0033986962 scopus 로고    scopus 로고
    • Essential function of the polo box of Cdc5 in subcellular localization and induction of cytokinetic structures
    • Song, S., Grenfell, T. Z., Garfield, S., Erikson, R. L., and Lee, K. S. (2000). Essential function of the polo box of Cdc5 in subcellular localization and induction of cytokinetic structures. Mol. Cell. Biol. 20, 286-298.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 286-298
    • Song, S.1    Grenfell, T.Z.2    Garfield, S.3    Erikson, R.L.4    Lee, K.S.5
  • 33
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe, N., Kato, T., Fujita, A., Ishizaki, T., and Narumiya, S. (1999). Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1, 136-143.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 34
    • 63349093757 scopus 로고    scopus 로고
    • Antagonistic regulation of Fus2p nuclear localization by pheromone signaling and the cell cycle
    • Ydenberg, C. A., and Rose, M. D. (2009). Antagonistic regulation of Fus2p nuclear localization by pheromone signaling and the cell cycle. J. Cell Biol 184, 409-422.
    • (2009) J. Cell Biol , vol.184 , pp. 409-422
    • Ydenberg, C.A.1    Rose, M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.