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Volumn 207, Issue 1, 2014, Pages 59-72

Bem1p contributes to secretory pathway polarization through a direct interaction with Exo70p

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; EXOCYST; FUNGAL PROTEIN; PROTEIN BEM 1P; PROTEIN EXO 70P; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; BEM1 PROTEIN, S CEREVISIAE; CDC10 PROTEIN, S CEREVISIAE; CDC24 PROTEIN, S CEREVISIAE; CELL CYCLE PROTEIN; CYCLIN DEPENDENT KINASE; EXO70 PROTEIN, S CEREVISIAE; GIN4 PROTEIN, S CEREVISIAE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; ISOPROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PROTEIN BINDING; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHO3 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SEC15 PROTEIN, S CEREVISIAE; SEC3 PROTEIN, S CEREVISIAE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; VESICULAR TRANSPORT PROTEIN;

EID: 84908371646     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201404122     Document Type: Article
Times cited : (25)

References (39)
  • 1
    • 0032740682 scopus 로고    scopus 로고
    • The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity
    • Adamo, J.E., G. Rossi, and P. Brennwald. 1999. The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity. Mol. Biol. Cell. 10:4121-4133. http://dx.doi.org/10.1091/mbc.10.12.4121.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4121-4133
    • Adamo, J.E.1    Rossi, G.2    Brennwald, P.3
  • 3
    • 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
  • 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. 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.4    Zyla, T.R.5    Lew, D.J.6
  • 5
    • 10344263403 scopus 로고    scopus 로고
    • Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p
    • Boyd, C., T. Hughes, M. Pypaert, and P. Novick. 2004. Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p. J. Cell Biol. 167:889-901. http://dx.doi.org/ 10.1083/jcb.200408124.
    • (2004) J. Cell Biol , vol.167 , pp. 889-901
    • Boyd, C.1    Hughes, T.2    Pypaert, M.3    Novick, P.4
  • 6
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • Brennwald, P., B. Kearns, K. Champion, S. Keränen, V. Bankaitis, and P. Novick. 1994. Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell. 79:245-258. http://dx.doi.org/10.1016/0092-8674(94)90194-5.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keränen, S.4    Bankaitis, V.5    Novick, P.6
  • 7
    • 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
  • 8
    • 0034947026 scopus 로고    scopus 로고
    • Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
    • Cheever, M.L., T.K. Sato, T. de Beer, T.G. Kutateladze, S.D. Emr, and M. Overduin. 2001. Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nat. Cell Biol. 3:613-618. http:// dx.doi.org/10.1038/35083000.
    • (2001) Nat. Cell Biol , vol.3 , pp. 613-618
    • Cheever, M.L.1    Sato, T.K.2    de Beer, T.3    Kutateladze, T.G.4    Emr, S.D.5    Overduin, M.6
  • 9
    • 84863195175 scopus 로고    scopus 로고
    • ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p
    • Chen, S., P. Novick, and S. Ferro-Novick. 2012. ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p. Nat. Cell Biol. 14:707-716. http://dx.doi.org/10.1038/ncb2523.
    • (2012) Nat. Cell Biol , vol.14 , pp. 707-716
    • Chen, S.1    Novick, P.2    Ferro-Novick, S.3
  • 11
    • 28544432477 scopus 로고    scopus 로고
    • The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
    • Dong, G., A.H. Hutagalung, C. Fu, P. Novick, and K.M. Reinisch. 2005. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat. Struct. Mol. Biol. 12:1094-1100. http:// dx.doi.org/10.1038/nsmb1017.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 1094-1100
    • Dong, G.1    Hutagalung, A.H.2    Fu, C.3    Novick, P.4    Reinisch, K.M.5
  • 12
    • 84872110455 scopus 로고    scopus 로고
    • Tracking shallow chemical gradients by actin-driven wandering of the polarization site
    • Dyer, J.M., N.S. Savage, M. Jin, T.R. Zyla, T.C. Elston, and D.J. Lew. 2013. Tracking shallow chemical gradients by actin-driven wandering of the polarization site. Curr. Biol. 23:32-41. http://dx.doi.org/10.1016/j.cub.2012.11.014.
    • (2013) Curr. Biol , vol.23 , pp. 32-41
    • Dyer, J.M.1    Savage, N.S.2    Jin, M.3    Zyla, T.R.4    Elston, T.C.5    Lew, D.J.6
  • 13
    • 0032548828 scopus 로고    scopus 로고
    • Sec3p is a spatial landmark for polarized secretion in budding yeast
    • Finger, F.P., T.E. Hughes, and P. Novick. 1998. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell. 92:559-571. http://dx.doi.org/10.1016/S0092-8674(00)80948-4.
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.P.1    Hughes, T.E.2    Novick, P.3
  • 14
    • 33645235856 scopus 로고    scopus 로고
    • The polarityestablishment component Bem1p interacts with the exocyst complex through the Sec15p subunit
    • France, Y.E., C. Boyd, J. Coleman, and P.J. Novick. 2006. The polarityestablishment component Bem1p interacts with the exocyst complex through the Sec15p subunit. J. Cell Sci. 119:876-888. http://dx.doi. org/10.1242/jcs.02849.
    • (2006) J. Cell Sci , vol.119 , pp. 876-888
    • France, Y.E.1    Boyd, C.2    Coleman, J.3    Novick, P.J.4
  • 15
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo, W., D. Roth, C. Walch-Solimena, and P. Novick. 1999. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J. 18:1071-1080. http://dx.doi.org/10.1093/emboj/18.4.1071.
    • (1999) EMBO J , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 16
    • 0035067186 scopus 로고    scopus 로고
    • Spatial regulation of the exocyst complex by Rho1 GTPase
    • Guo, W., F. Tamanoi, and P. Novick. 2001. Spatial regulation of the exocyst complex by Rho1 GTPase. Nat. Cell Biol. 3:353-360. http://dx.doi.org/10.1038/35070029.
    • (2001) Nat. Cell Biol , vol.3 , pp. 353-360
    • Guo, W.1    Tamanoi, F.2    Novick, P.3
  • 17
    • 0028787438 scopus 로고
    • Parallel secretory pathways to the cell surface in yeast
    • Harsay, E., and A. Bretscher. 1995. Parallel secretory pathways to the cell surface in yeast. J. Cell Biol. 131:297-310. http://dx.doi.org/10.1083/jcb.131.2.297.
    • (1995) J. Cell Biol , vol.131 , pp. 297-310
    • Harsay, E.1    Bretscher, A.2
  • 18
    • 34648823113 scopus 로고    scopus 로고
    • Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane
    • He, B., F. Xi, X. Zhang, J. Zhang, and W. Guo. 2007. Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane. EMBO J. 26:4053-4065. http://dx.doi.org/10.1038/sj.emboj.7601834.
    • (2007) EMBO J , vol.26 , pp. 4053-4065
    • He, B.1    Xi, F.2    Zhang, X.3    Zhang, J.4    Guo, W.5
  • 19
    • 0032103420 scopus 로고    scopus 로고
    • Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments
    • Hsu, S.C., C.D. Hazuka, R. Roth, D.L. Foletti, J. Heuser, and R.H. Scheller. 1998. Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron. 20:1111-1122. http://dx.doi.org/10.1016/S0896-6273(00)80493-6.
    • (1998) Neuron , vol.20 , pp. 1111-1122
    • Hsu, S.C.1    Hazuka, C.D.2    Roth, R.3    Foletti, D.L.4    Heuser, J.5    Scheller, R.H.6
  • 20
    • 63049085700 scopus 로고    scopus 로고
    • An internal domain of Exo70p is required for actin-independent localization and mediates assembly of specific exocyst components
    • Hutagalung, A.H., J. Coleman, M. Pypaert, and P.J. Novick. 2009. An internal domain of Exo70p is required for actin-independent localization and mediates assembly of specific exocyst components. Mol. Biol. Cell. 20:153-163. http://dx.doi.org/10.1091/mbc.E08-02-0157.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 153-163
    • Hutagalung, A.H.1    Coleman, J.2    Pypaert, M.3    Novick, P.J.4
  • 21
    • 33746939368 scopus 로고    scopus 로고
    • Homologues of oxysterolbinding proteins affect Cdc42p-and Rho1p-mediated cell polarization in Saccharomyces cerevisiae
    • Kozminski, K.G., G. Alfaro, S. Dighe, and C.T. Beh. 2006. Homologues of oxysterolbinding proteins affect Cdc42p-and Rho1p-mediated cell polarization in Saccharomyces cerevisiae. Traffic. 7:1224-1242. http://dx.doi.org/10.1111/j.1600-0854.2006.00467.x.
    • (2006) Traffic , vol.7 , pp. 1224-1242
    • Kozminski, K.G.1    Alfaro, G.2    Dighe, S.3    Beh, C.T.4
  • 22
    • 3042542941 scopus 로고    scopus 로고
    • Sec22p export from the endoplasmic reticulum is independent of SNARE pairing
    • Liu, Y., J.J. Flanagan, and C. Barlowe. 2004. Sec22p export from the endoplasmic reticulum is independent of SNARE pairing. J. Biol. Chem. 279: 27225-27232. http://dx.doi.org/10.1074/jbc.M312122200.
    • (2004) J. Biol. Chem , vol.279 , pp. 27225-27232
    • Liu, Y.1    Flanagan, J.J.2    Barlowe, C.3
  • 24
    • 0032476712 scopus 로고    scopus 로고
    • Role of the yeast Gin4p protein kinase in septin assembly and the relationship between septin assembly and septin function
    • Longtine, M.S., H. Fares, and J.R. Pringle. 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. http://dx.doi.org/10.1083/jcb.143.3.719.
    • (1998) J. Cell Biol , vol.143 , pp. 719-736
    • Longtine, M.S.1    Fares, H.2    Pringle, J.R.3
  • 25
    • 0035985207 scopus 로고    scopus 로고
    • Cell cycledependent assembly of a Gin4-septin complex
    • Mortensen, E.M., H. McDonald, J. Yates III, and D.R. Kellogg. 2002. Cell cycledependent assembly of a Gin4-septin complex. Mol. Biol. Cell. 13:2091-2105. http://dx.doi.org/10.1091/mbc.01-10-0500.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2091-2105
    • Mortensen, E.M.1    McDonald, H.2    Yates III, J.3    Kellogg, D.R.4
  • 26
    • 33745841364 scopus 로고    scopus 로고
    • The exocyst defrocked, a framework of rods revealed
    • Munson, M., and P. Novick. 2006. The exocyst defrocked, a framework of rods revealed. Nat. Struct. Mol. Biol. 13:577-581. http://dx.doi.org/10.1038/ nsmb1097.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 577-581
    • Munson, M.1    Novick, P.2
  • 27
    • 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
  • 28
    • 78650143890 scopus 로고    scopus 로고
    • A guide to simple and informative binding assays
    • Pollard, T.D. 2010. A guide to simple and informative binding assays. Mol. Biol. Cell. 21:4061-4067. http://dx.doi.org/10.1091/mbc.E10-08-0683.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4061-4067
    • Pollard, T.D.1
  • 29
    • 0032938745 scopus 로고    scopus 로고
    • Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70
    • Robinson, N.G., L. Guo, J. Imai, A. Toh-E, Y. Matsui, and F. Tamanoi. 1999. Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol. Cell. Biol. 19:3580-3587.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 3580-3587
    • Robinson, N.G.1    Guo, L.2    Imai, J.3    Toh, E.A.4    Matsui, Y.5    Tamanoi, F.6
  • 30
    • 84884239046 scopus 로고    scopus 로고
    • The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p
    • Shen, D., H. Yuan, A. Hutagalung, A. Verma, D. Kümmel, X. Wu, K. Reinisch, J.A. McNew, and P. Novick. 2013. The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p. J. Cell Biol. 202:509-526. http://dx.doi.org/10.1083/jcb.201211148.
    • (2013) J. Cell Biol , vol.202 , pp. 509-526
    • Shen, D.1    Yuan, H.2    Hutagalung, A.3    Verma, A.4    Kümmel, D.5    Wu, X.6    Reinisch, K.7    McNew, J.A.8    Novick, P.9
  • 31
    • 84890284248 scopus 로고    scopus 로고
    • Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners
    • Stalder, D., E. Mizuno-Yamasaki, M. Ghassemian, and P.J. Novick. 2013. Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners. Proc. Natl. Acad. Sci. USA. 110:19995-20002. http://dx.doi.org/10.1073/pnas.1320029110.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 19995-20002
    • Stalder, D.1    Mizuno-Yamasaki, E.2    Ghassemian, M.3    Novick, P.J.4
  • 32
    • 0029843493 scopus 로고    scopus 로고
    • The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush, D.R., T. Maurice, D. Roth, and P. Novick. 1996. The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 15:6483-6494.
    • (1996) EMBO J , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 33
    • 76049118573 scopus 로고    scopus 로고
    • The Exo70 subunit of the exocyst is an effector for both Cdc42 and Rho3 function in polarized exocytosis
    • Wu, H., C. Turner, J. Gardner, B. Temple, and P. Brennwald. 2010. The Exo70 subunit of the exocyst is an effector for both Cdc42 and Rho3 function in polarized exocytosis. Mol. Biol. Cell. 21:430-442. http://dx.doi.org/ 10.1091/mbc.E09-06-0501.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 430-442
    • Wu, H.1    Turner, C.2    Gardner, J.3    Temple, B.4    Brennwald, P.5
  • 34
    • 33846995468 scopus 로고    scopus 로고
    • A novel Cdc42-interacting domain of the yeast polarity establishment protein Bem1. Implications for modulation of mating pheromone signaling
    • Yamaguchi, Y., K. Ota, and T. Ito. 2007. A novel Cdc42-interacting domain of the yeast polarity establishment protein Bem1. Implications for modulation of mating pheromone signaling. J. Biol. Chem. 282:29-38. http:// dx.doi.org/10.1074/jbc.M609308200.
    • (2007) J. Biol. Chem , vol.282 , pp. 29-38
    • Yamaguchi, Y.1    Ota, K.2    Ito, T.3
  • 36
    • 1242284588 scopus 로고    scopus 로고
    • Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells
    • Yeaman, C., K.K. Grindstaff, and W.J. Nelson. 2004. Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells. J. Cell Sci. 117:559-570. http://dx.doi.org/ 10.1242/jcs.00893.
    • (2004) J. Cell Sci , vol.117 , pp. 559-570
    • Yeaman, C.1    Grindstaff, K.K.2    Nelson, W.J.3
  • 37
    • 14844310335 scopus 로고    scopus 로고
    • Cyclical regulation of the exocyst and cell polarity determinants for polarized cell growth
    • Zajac, A., X. Sun, J. Zhang, and W. Guo. 2005. Cyclical regulation of the exocyst and cell polarity determinants for polarized cell growth. Mol. Biol. Cell. 16:1500-1512. http://dx.doi.org/10.1091/mbc.E04-10-0896.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1500-1512
    • Zajac, A.1    Sun, X.2    Zhang, J.3    Guo, W.4
  • 38
    • 0035861749 scopus 로고    scopus 로고
    • Cdc42 interacts with the exocyst and regulates polarized secretion
    • Zhang, X., E. Bi, P. Novick, L. Du, K.G. Kozminski, J.H. Lipschutz, and W. Guo. 2001. Cdc42 interacts with the exocyst and regulates polarized secretion. J. Biol. Chem. 276:46745-46750. http://dx.doi.org/10.1074/jbc.M107464200.
    • (2001) J. Biol. Chem , vol.276 , pp. 46745-46750
    • Zhang, X.1    Bi, E.2    Novick, P.3    Du, L.4    Kozminski, K.G.5    Lipschutz, J.H.6    Guo, W.7
  • 39
    • 38349030651 scopus 로고    scopus 로고
    • Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
    • Zhang, X., K. Orlando, B. He, F. Xi, J. Zhang, A. Zajac, and W. Guo. 2008. Membrane association and functional regulation of Sec3 by phospholipids and Cdc42. J. Cell Biol. 180:145-158. http://dx.doi.org/10.1083/ jcb.200704128.
    • (2008) J. Cell Biol , vol.180 , pp. 145-158
    • Zhang, X.1    Orlando, K.2    He, B.3    Xi, F.4    Zhang, J.5    Zajac, A.6    Guo, W.7


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