메뉴 건너뛰기




Volumn 183, Issue 6, 2008, Pages 1089-1100

Binding interactions control SNARE specifi city in vivo

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; GLUTAMINE; PROTEIN SUBUNIT; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; MUTANT PROTEIN; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 58249084924     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200809178     Document Type: Article
Times cited : (15)

References (45)
  • 1
    • 0027527762 scopus 로고
    • Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport
    • Aalto, M.K., H. Ronne, and S. Keranen. 1993. Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport. EMBO J. 12:4095-4104.
    • (1993) EMBO J , vol.12 , pp. 4095-4104
    • Aalto, M.K.1    Ronne, H.2    Keranen, S.3
  • 2
    • 15244340169 scopus 로고    scopus 로고
    • Differential use of endoplasmic reticulum membrane for phagocytosis in J774 macrophages
    • Becker, T., A. Volchuk, and J.E. Rothman. 2005. Differential use of endoplasmic reticulum membrane for phagocytosis in J774 macrophages. Proc. Natl. Acad. Sci. USA. 102:4022-4026.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4022-4026
    • Becker, T.1    Volchuk, A.2    Rothman, J.E.3
  • 3
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • Bock, J.B., H.T. Matern, A.A. Peden, and R.H. Scheller . 2001. A genomic perspective on membrane compartment organization. Nature. 409:839-841.
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 4
    • 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. Keranen, 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.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keranen, S.4    Bankaitis, V.5    Novick, P.6
  • 5
    • 0033606766 scopus 로고    scopus 로고
    • Sec1p binds to SNARE complexes and concentrates at sites of secretion
    • Carr, C.M., E. Grote, M. Munson, F.M. Hughson, and P.J. Novick. 1999. Sec1p binds to SNARE complexes and concentrates at sites of secretion. J. Cell Biol. 146:333-344.
    • (1999) J. Cell Biol , vol.146 , pp. 333-344
    • Carr, C.M.1    Grote, E.2    Munson, M.3    Hughson, F.M.4    Novick, P.J.5
  • 7
    • 1642390110 scopus 로고    scopus 로고
    • Genetic evidence of a role for membrane lipid composition in the regulation of soluble NEM- sensitive factor receptor function in Saccharomyces cerevisiae
    • Coluccio, A., M. Malzone, and A.M. Neiman. 2004. Genetic evidence of a role for membrane lipid composition in the regulation of soluble NEM- sensitive factor receptor function in Saccharomyces cerevisiae. Genetics. 166:89-97.
    • (2004) Genetics , vol.166 , pp. 89-97
    • Coluccio, A.1    Malzone, M.2    Neiman, A.M.3
  • 8
    • 0032430423 scopus 로고    scopus 로고
    • Fasshauer, D., R.B. Sutton, A.T. Brunger , and R. Jahn. 1998. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassif ed as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA. 95:15781-15786.
    • Fasshauer, D., R.B. Sutton, A.T. Brunger , and R. Jahn. 1998. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassif ed as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA. 95:15781-15786.
  • 9
    • 17444393115 scopus 로고    scopus 로고
    • Identif cation of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer
    • Graf, C.T., D. Riedel, H.D. Schmitt, and R. Jahn. 2005. Identif cation of functionally interacting SNAREs by using complementary substitutions in the conserved '0' layer. Mol. Biol. Cell. 16:2263-2274.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2263-2274
    • Graf, C.T.1    Riedel, D.2    Schmitt, H.D.3    Jahn, R.4
  • 10
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs - engines for membrane fusion
    • Jahn, R., and R.H. Scheller. 2006 . SNAREs - engines for membrane fusion. Nat. Rev. Mol. Cell Biol. 7:631-643.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 11
    • 0037081645 scopus 로고    scopus 로고
    • Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation
    • Jantti, J., M.K. Aalto, M. Oyen, L. Sundqvist, S. Keranen, and H. Ronne. 2002. Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation. J. Cell Sci. 115:409-420.
    • (2002) J. Cell Sci , vol.115 , pp. 409-420
    • Jantti, J.1    Aalto, M.K.2    Oyen, M.3    Sundqvist, L.4    Keranen, S.5    Ronne, H.6
  • 12
    • 0033749565 scopus 로고    scopus 로고
    • Testing the 3Q:1R "rule": Mutational analysis of the ionic " zero " layer in the yeast exocytic SNARE complex reveals no requirement for arginine
    • Katz , L. , and P. Brennwald . 2000. Testing the 3Q:1R "rule": mutational analysis of the ionic " zero " layer in the yeast exocytic SNARE complex reveals no requirement for arginine. Mol. Biol. Cell. 11:3849-3858.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3849-3858
    • Katz, L.1    Brennwald, P.2
  • 14
    • 35348819374 scopus 로고    scopus 로고
    • In vitro fusion catalyzed by the sporulation-specif c t-SNARE light-chain Spo20p is stimulated by phosphatidic acid
    • Liu, S., K.A. Wilson, T. Rice-Stitt, A.M. Neiman, and J.A. McNew. 2007. In vitro fusion catalyzed by the sporulation-specif c t-SNARE light-chain Spo20p is stimulated by phosphatidic acid. Traffc. 8:1630-1643.
    • (2007) Traffc , vol.8 , pp. 1630-1643
    • Liu, S.1    Wilson, K.A.2    Rice-Stitt, T.3    Neiman, A.M.4    McNew, J.A.5
  • 15
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modif cation in Saccharomyces cerevisiae
    • Longtine, M.S., A. McKenzie III, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modif cation in Saccharomyces cerevisiae. Yeast. 14:953-961.
    • (1998) Yeast , vol.14 , 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
  • 16
    • 44849125083 scopus 로고    scopus 로고
    • Regulation of SNARE-mediated membrane fusion during exocytosis
    • McNew, J.A. 2008. Regulation of SNARE-mediated membrane fusion during exocytosis. Chem. Rev. 108:1669-1686.
    • (2008) Chem. Rev , vol.108 , pp. 1669-1686
    • McNew, J.A.1
  • 18
    • 29144482644 scopus 로고    scopus 로고
    • A f ssion yeast SNAP-25 homologue, SpSec9, is essential for cytokinesis and sporulation
    • Nakamura, T., J. Kashiwazaki, and C. Shimoda. 2005. A f ssion yeast SNAP-25 homologue, SpSec9, is essential for cytokinesis and sporulation. Cell Struct. Funct. 30:15-24.
    • (2005) Cell Struct. Funct , vol.30 , pp. 15-24
    • Nakamura, T.1    Kashiwazaki, J.2    Shimoda, C.3
  • 19
    • 1642546271 scopus 로고    scopus 로고
    • Nakanishi, H., P. de los Santos, and A.M. Neiman. 2004. Positive and negative regulation of a SNARE protein by control of intracellular localization. Mol. Biol. Cell. 15:1802-1815.
    • Nakanishi, H., P. de los Santos, and A.M. Neiman. 2004. Positive and negative regulation of a SNARE protein by control of intracellular localization. Mol. Biol. Cell. 15:1802-1815.
  • 20
    • 33646804137 scopus 로고    scopus 로고
    • Phospholipase D and the SNARE Sso1p are necessary for vesicle fusion during sporulation in yeast
    • Nakanishi, H., M. Morishita, C.L. Schwartz, A. Coluccio, J. Engebrecht, and A.M. Neiman . 2006 . Phospholipase D and the SNARE Sso1p are necessary for vesicle fusion during sporulation in yeast. J. Cell Sci. 119:1406-1415.
    • (2006) J. Cell Sci , vol.119 , pp. 1406-1415
    • Nakanishi, H.1    Morishita, M.2    Schwartz, C.L.3    Coluccio, A.4    Engebrecht, J.5    Neiman, A.M.6
  • 21
    • 0031940772 scopus 로고    scopus 로고
    • Prospore membrane formation def nes a developmentally regulated branch of the secretory pathway in yeast
    • Neiman, A.M. 1998. Prospore membrane formation def nes a developmentally regulated branch of the secretory pathway in yeast. J. Cell Biol. 140:29-37.
    • (1998) J. Cell Biol , vol.140 , pp. 29-37
    • Neiman, A.M.1
  • 22
    • 29144461519 scopus 로고    scopus 로고
    • Ascospore formation in the yeast Saccharomyces cerevisiae
    • Neiman, A.M. 2005. Ascospore formation in the yeast Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 69:565-584.
    • (2005) Microbiol. Mol. Biol. Rev , vol.69 , pp. 565-584
    • Neiman, A.M.1
  • 23
    • 0033880985 scopus 로고    scopus 로고
    • Identif cation of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiae
    • Neiman, A.M., L. Katz, and P.J. Brennwald. 2000. Identif cation of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiae. Genetics. 155:1643-1655.
    • (2000) Genetics , vol.155 , pp. 1643-1655
    • Neiman, A.M.1    Katz, L.2    Brennwald, P.J.3
  • 24
    • 0024828306 scopus 로고
    • The identif cation of a novel synaptosomalassociated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler, G.A., G.A. Higgins, R.A. Hart, E. Battenberg, M. Billingsley, F.E. Bloom, and M.C. Wilson. 1989. The identif cation of a novel synaptosomalassociated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109:3039-3052.
    • (1989) J. Cell Biol , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, E.4    Billingsley, M.5    Bloom, F.E.6    Wilson, M.C.7
  • 28
    • 1542409030 scopus 로고    scopus 로고
    • The specif city of SNARE- dependent fusion is encoded in the SNARE motif
    • Paumet, F., V. Rahimian, and J.E. Rothman. 2004. The specif city of SNARE- dependent fusion is encoded in the SNARE motif. Proc. Natl. Acad. Sci. USA. 101:3376-3380.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3376-3380
    • Paumet, F.1    Rahimian, V.2    Rothman, J.E.3
  • 29
    • 0033602030 scopus 로고    scopus 로고
    • SNAREs and the secretory pathway-lessons from yeast
    • Pelham, H.R. 1999. SNAREs and the secretory pathway-lessons from yeast. Exp. Cell Res. 247:1-8.
    • (1999) Exp. Cell Res , vol.247 , pp. 1-8
    • Pelham, H.R.1
  • 31
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • Protopopov, V., B. Govindan, P. Novick, and J.E. Gerst. 1993. Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell. 74:855-861.
    • (1993) Cell , vol.74 , pp. 855-861
    • Protopopov, V.1    Govindan, B.2    Novick, P.3    Gerst, J.E.4
  • 32
    • 0003529272 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Rose, M.D., and G.R. Fink. 1990. Methods in Yeast Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1990) Methods in Yeast Genetics
    • Rose, M.D.1    Fink, G.R.2
  • 33
    • 0034525357 scopus 로고    scopus 로고
    • The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive factor adaptor protein receptors
    • Sanderfoot, A.A., F.F. Assaad, and N.V. Raikhel. 2000. The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive factor adaptor protein receptors. Plant Physiol. 124:1558-1569.
    • (2000) Plant Physiol , vol.124 , pp. 1558-1569
    • Sanderfoot, A.A.1    Assaad, F.F.2    Raikhel, N.V.3
  • 34
    • 0035807871 scopus 로고    scopus 로고
    • The ionic layer is required for eff cient dissociation of the SNARE complex by a-SNAP and NSF
    • Scales, S.J., B.Y. Yoo, and R.H. Scheller . 2001 . The ionic layer is required for eff cient dissociation of the SNARE complex by a-SNAP and NSF. Proc. Natl. Acad. Sci. USA. 98:14262-14267.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14262-14267
    • Scales, S.J.1    Yoo, B.Y.2    Scheller, R.H.3
  • 35
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for eff cient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter . 1989 . A system of shuttle vectors and yeast host strains designed for eff cient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 36
    • 0028168008 scopus 로고
    • A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Sogaard, M., K. Tani, R.R. Ye, S. Geromanos, P. Tempst, T. Kirchhausen, J.E. Rothman , and T. Sollner . 1994 . A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell. 78:937-948.
    • (1994) Cell , vol.78 , pp. 937-948
    • Sogaard, M.1    Tani, K.2    Ye, R.R.3    Geromanos, S.4    Tempst, P.5    Kirchhausen, T.6    Rothman, J.E.7    Sollner, T.8
  • 39
    • 38149026393 scopus 로고    scopus 로고
    • The structure of the yeast plasma membrane SNARE complex reveals destabilizing waterf lled cavities
    • Strop, P., S.E. Kaiser, M. Vrljic, and A.T. Brunger. 2008. The structure of the yeast plasma membrane SNARE complex reveals destabilizing waterf lled cavities. J. Biol. Chem. 283:1113-1119.
    • (2008) J. Biol. Chem , vol.283 , pp. 1113-1119
    • Strop, P.1    Kaiser, S.E.2    Vrljic, M.3    Brunger, A.T.4
  • 40
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton, R.B., D. Fasshauer, R. Jahn, and A.T. Brunger. 1998. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature. 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 42
    • 0032404442 scopus 로고    scopus 로고
    • A model for structural similarity between different SNARE complexes based on sequence relationships
    • Weimbs, T., K. Mostov, S.H. Low, and K. Hofmann. 1998.A model for structural similarity between different SNARE complexes based on sequence relationships. Trends Cell Biol. 8:260-262.
    • (1998) Trends Cell Biol , vol.8 , pp. 260-262
    • Weimbs, T.1    Mostov, K.2    Low, S.H.3    Hofmann, K.4
  • 44
    • 0030947344 scopus 로고    scopus 로고
    • Molecular evidence for an ancient duplication of the entire yeast genome
    • Wolfe, K.H., and D.C. Shields. 1997. Molecular evidence for an ancient duplication of the entire yeast genome. Nature. 387:708-713.
    • (1997) Nature , vol.387 , pp. 708-713
    • Wolfe, K.H.1    Shields, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.