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Volumn 115, Issue 18, 2002, Pages 3683-3691

Binding of Sly1 to Sed5 enhances formation of the yeast early Golgi SNARE complex

Author keywords

Saccharomyces cerevisiae; Sec1 family protein; Sly1 protein; SNARE complex; Vesicle fusion

Indexed keywords

MEMBRANE PROTEIN; MUTANT PROTEIN; RECOMBINANT PROTEIN; REGULATOR PROTEIN; SLY1 PROTEIN; SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 0037106580     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00027     Document Type: Article
Times cited : (28)

References (46)
  • 1
    • 0026516633 scopus 로고
    • A family of proteins involved in intracellular transport
    • Aalto, M. K., Keranen, S. and Ronne, H. (1992). A family of proteins involved in intracellular transport. Cell 68, 181-182.
    • (1992) Cell , vol.68 , pp. 181-182
    • Aalto, M.K.1    Keranen, S.2    Ronne, H.3
  • 2
    • 0030807931 scopus 로고    scopus 로고
    • Coupled ER to Golgi transport reconstituted with purified cytosotic proteins
    • Barlowe, C. (1997). Coupled ER to Golgi transport reconstituted with purified cytosotic proteins. J. Cell Biol. 139, 1097-1108.
    • (1997) J. Cell Biol , vol.139 , pp. 1097-1108
    • Barlowe, C.1
  • 3
    • 0035796402 scopus 로고    scopus 로고
    • Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation
    • Bryant, N. J. and James, D. E. (2001). Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation. EMBO J. 20, 3380-3388.
    • (2001) EMBO J , vol.20 , pp. 3380-3388
    • Bryant, N.J.1    James, D.E.2
  • 4
    • 0034599993 scopus 로고    scopus 로고
    • Asymmetric requirements for a rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes
    • Cao, X. and Barlowe, C. (2000). Asymmetric requirements for a rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes. J. Cell Biol. 149, 55-65.
    • (2000) J. Cell Biol , vol.149 , pp. 55-65
    • Cao, X.1    Barlowe, C.2
  • 5
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao, X., Ballew, N. and Barlowe, C. (1998). Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J. 17, 2156-2165.
    • (1998) EMBO J , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 6
    • 0035119963 scopus 로고    scopus 로고
    • The taming of the SNARE
    • Carr, C. M. (2001). The taming of the SNARE. Nature Struct. Biol. 8, 186-188.
    • (2001) Nature Struct. Biol , vol.8 , pp. 186-188
    • Carr, C.M.1
  • 7
    • 0033606766 scopus 로고    scopus 로고
    • Sec1p binds to SNARE complexes and concentrates at sites of secretion
    • Carr, C. M., Grote, E., Munson, M., Hughson, F. M. and Novick, P. J. (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
  • 8
    • 0034629013 scopus 로고    scopus 로고
    • Proteins in the early Golgi compartment of Saccharomyces cerevisiae immunoisolated by Sed5p
    • Cho, J.-H., Noda, Y. and Yoda, K. (2000). Proteins in the early Golgi compartment of Saccharomyces cerevisiae immunoisolated by Sed5p. FEBS Lett. 469, 151-154.
    • (2000) FEBS Lett , vol.469 , pp. 151-154
    • Cho, J.-H.1    Noda, Y.2    Yoda, K.3
  • 9
    • 0025977723 scopus 로고
    • Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily
    • Dascher, C., Ossig, R., Gallwitz, D. and Schmitt, H. D. (1991). Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily. Mol. Cell. Biol. 11, 872-885.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 872-885
    • Dascher, C.1    Ossig, R.2    Gallwitz, D.3    Schmitt, H.D.4
  • 10
    • 0031567602 scopus 로고    scopus 로고
    • High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking
    • Grabowski, G. and Gallwitz, D. (1997). High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking. FEBS Lett. 411, 169-172.
    • (1997) FEBS Lett , vol.411 , pp. 169-172
    • Grabowski, G.1    Gallwitz, D.2
  • 11
    • 0034675859 scopus 로고    scopus 로고
    • Ordering the final events in yeast exocytosis
    • Grote, E., Carr, C. M. and Novick, P. J. (2000). Ordering the final events in yeast exocytosis. J. Cell Biol. 151, 439-451.
    • (2000) J. Cell Biol , vol.151 , pp. 439-451
    • Grote, E.1    Carr, C.M.2    Novick, P.J.3
  • 12
    • 0030021851 scopus 로고    scopus 로고
    • The Sec 1 family: A novel family of proteins involved in synaptic transmission and general secretion
    • Halachmi, N. and Lev, Z. (1996). The Sec 1 family: A novel family of proteins involved in synaptic transmission and general secretion. J. Neurochem. 66, 889-897.
    • (1996) J. Neurochem , vol.66 , pp. 889-897
    • Halachmi, N.1    Lev, Z.2
  • 13
    • 0031590859 scopus 로고    scopus 로고
    • Novel membrane protein complexes for protein glycosylation in the yeast Golgi apparatus
    • Hashimoto, H. and Yoda, K. (1997). Novel membrane protein complexes for protein glycosylation in the yeast Golgi apparatus. Biochem. Biophys. Res. Commun. 241, 682-686.
    • (1997) Biochem. Biophys. Res. Commun , vol.241 , pp. 682-686
    • Hashimoto, H.1    Yoda, K.2
  • 14
    • 0027364502 scopus 로고
    • Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin
    • Hata, Y., Slaughter, C. A. and Sudhof, T. C. (1993). Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. Nature 366, 347-351.
    • (1993) Nature , vol.366 , pp. 347-351
    • Hata, Y.1    Slaughter, C.A.2    Sudhof, T.C.3
  • 15
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi, T., McMahon, H., Yamasaki, S., Binz, T., Hata, Y., Sudhof, T. C. and Niemann, H. (1994). Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13, 5051-5061.
    • (1994) EMBO J , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Sudhof, T.C.6    Niemann, H.7
  • 16
    • 0033694345 scopus 로고    scopus 로고
    • Sec1/Munc18 proteins: Mediators of membrane fusion moving to center stage
    • Jahn, R. (2000). Sec1/Munc18 proteins: Mediators of membrane fusion moving to center stage. Cell 27, 201-204.
    • (2000) Cell , vol.27 , pp. 201-204
    • Jahn, R.1
  • 17
    • 0031898053 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism
    • Kagiwada, S., Hosaka, K., Murata, M., Nikawa, J. and Takatsuki, A. (1998). The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism. J. Bacteriol. 180, 1700-1708.
    • (1998) J. Bacteriol , vol.180 , pp. 1700-1708
    • Kagiwada, S.1    Hosaka, K.2    Murata, M.3    Nikawa, J.4    Takatsuki, A.5
  • 18
    • 0029889105 scopus 로고    scopus 로고
    • Calcium and SLY genes suppress the temperature-sensitive secretion defect of Saccharomyces cerevisiae usol mutant
    • Kito, M., Seog, D.-H., Igarashi, K., Kambe-Honjo, H., Yoda, K. and Yamasaki, M. (1996). Calcium and SLY genes suppress the temperature-sensitive secretion defect of Saccharomyces cerevisiae usol mutant. Biochem. Biophys. Res. Commun. 220, 653-657.
    • (1996) Biochem. Biophys. Res. Commun , vol.220 , pp. 653-657
    • Kito, M.1    Seog, D.-H.2    Igarashi, K.3    Kambe-Honjo, H.4    Yoda, K.5    Yamasaki, M.6
  • 19
    • 0032544324 scopus 로고    scopus 로고
    • Protein-Protein interactions of the yeast Golgi t-SNARE Sed5 protein distinct from its neural plasma membrane cognate Syntaxin 1
    • Kosodo, Y., Noda, Y. and Yoda, K. (1998). Protein-Protein interactions of the yeast Golgi t-SNARE Sed5 protein distinct from its neural plasma membrane cognate Syntaxin 1. Biochem. Biophys. Res. Commun. 250, 212-216.
    • (1998) Biochem. Biophys. Res. Commun , vol.250 , pp. 212-216
    • Kosodo, Y.1    Noda, Y.2    Yoda, K.3
  • 20
    • 0034742404 scopus 로고    scopus 로고
    • Multicopy suppressors of the sly1 temperature-sensitive mutation in the ER-Golgi vesicular transport in Saccharomyces cerevisiae
    • Kosodo, Y., Imai, K., Hirata, A., Noda, Y., Takatsuki, A., Adachi, H. and Yoda, K. (2001). Multicopy suppressors of the sly1 temperature-sensitive mutation in the ER-Golgi vesicular transport in Saccharomyces cerevisiae. Yeast 18, 1-13.
    • (2001) Yeast , vol.18 , pp. 1-13
    • Kosodo, Y.1    Imai, K.2    Hirata, A.3    Noda, Y.4    Takatsuki, A.5    Adachi, H.6    Yoda, K.7
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0035805642 scopus 로고    scopus 로고
    • The transmembrane domain of syntaxin 1A is critical for cytoplasmic domain protein-protein interactions
    • Lewis, J. L., Dong, M., Earles, C. A. and Chapman, E. R. (2001). The transmembrane domain of syntaxin 1A is critical for cytoplasmic domain protein-protein interactions. J. Biol. Chem. 276, 15458-15465.
    • (2001) J. Biol. Chem , vol.276 , pp. 15458-15465
    • Lewis, J.L.1    Dong, M.2    Earles, C.A.3    Chapman, E.R.4
  • 23
    • 0030062831 scopus 로고    scopus 로고
    • Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes
    • Lupashin, V. V., Hamamoto, S. and Schekman, R. W. (1996). Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes. J. Cell Biol. 132, 277-289.
    • (1996) J. Cell Biol , vol.132 , pp. 277-289
    • Lupashin, V.V.1    Hamamoto, S.2    Schekman, R.W.3
  • 24
    • 0029898291 scopus 로고    scopus 로고
    • Yeast src homology region 3 domain-binding proteins involved in bud formation
    • Matsui, Y., Matsui, R., Akada, R. and Toh-e, A. (1996). Yeast src homology region 3 domain-binding proteins involved in bud formation. J. Cell Biol. 133, 865-878.
    • (1996) J. Cell Biol , vol.133 , pp. 865-878
    • Matsui, Y.1    Matsui, R.2    Akada, R.3    Toh-e, A.4
  • 26
    • 0034704771 scopus 로고    scopus 로고
    • Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
    • Misura, K. M. S., Scheller, R. H. and Weis, W. I. (2000). Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex. Nature 404, 355-362.
    • (2000) Nature , vol.404 , pp. 355-362
    • Misura, K.M.S.1    Scheller, R.H.2    Weis, W.I.3
  • 27
    • 0028215997 scopus 로고
    • Continued functioning of the secretory pathway is essential for ribosome synthesis
    • Mizuta, K. and Warner, J. R. (1994). Continued functioning of the secretory pathway is essential for ribosome synthesis. Mol. Cell. Biol. 14, 2493-2502.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 2493-2502
    • Mizuta, K.1    Warner, J.R.2
  • 28
    • 0032516856 scopus 로고    scopus 로고
    • SNAREs and membrane fusion in the Golgi apparatus
    • Nichols, B. J. and Pelham, H. R. B. (1998). SNAREs and membrane fusion in the Golgi apparatus. Biochim. Biophys. Acta 1404, 9-31.
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 9-31
    • Nichols, B.J.1    Pelham, H.R.B.2
  • 29
    • 0025891541 scopus 로고
    • The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport
    • Ossig, R., Dascher, C., Trepte, H. H., Schmitt, H. D. and Gallwitz, D. (1991). The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol. Cell. Biol. 11, 2980-2993.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 2980-2993
    • Ossig, R.1    Dascher, C.2    Trepte, H.H.3    Schmitt, H.D.4    Gallwitz, D.5
  • 30
    • 0037071544 scopus 로고    scopus 로고
    • Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes
    • Peng, R. and Gallwitz, D. (2002). Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes. J. Cell Biol. 157, 645-655.
    • (2002) J. Cell Biol , vol.157 , pp. 645-655
    • Peng, R.1    Gallwitz, D.2
  • 32
    • 0028143698 scopus 로고
    • Mechanism of intracellular protein transport
    • Rothman, J. E. (1994). Mechanism of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 33
    • 0030858498 scopus 로고    scopus 로고
    • The synaptobrevin-related domains of Bos1p and Sec22p bind to the syntaxin-like region of Sed5p
    • Sacher, M., Stone, S. and Ferro-Novick, S. (1997). The synaptobrevin-related domains of Bos1p and Sec22p bind to the syntaxin-like region of Sed5p. J. Biol. Chem. 272, 17134-17138.
    • (1997) J. Biol. Chem , vol.272 , pp. 17134-17138
    • Sacher, M.1    Stone, S.2    Ferro-Novick, S.3
  • 35
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • Schneiter, R., Brugger, B., Sandhoff, R., Zellnig, G., Leber, A., Lampl, M., Athenstaedt, K., Hrastnik, C., Eder, S., Daum, G. et al. (1999). Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane. J. Cell Biol. 146, 741-754.
    • (1999) J. Cell Biol , vol.146 , pp. 741-754
    • Schneiter, R.1    Brugger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6    Athenstaedt, K.7    Hrastnik, C.8    Eder, S.9    Daum, G.10
  • 36
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S. and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 38
    • 0028168008 scopus 로고
    • A Rab protein is required for the assembly of SNARE complex in the docking of transport vesicles
    • Søgaard, M., Tani, K., Ye, R. R., Geromanos, S., Tempst, P., Kirchhausen, T., Rothman, J. E. and Söllner, T. (1994). A Rab protein is required for the assembly of SNARE complex in the docking of transport vesicles. Cell 78, 937-948.
    • (1994) Cell , vol.78 , pp. 937-948
    • Søgaard, M.1    Tani, K.2    Ye, R.R.3    Geromanos, S.4    Tempst, P.5    Kirchhausen, T.6    Rothman, J.E.7    Söllner, T.8
  • 39
    • 0032978370 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting
    • Tall, G. G., Hiroko, H., DeWald, D. B. and Horazdovsky, B. F. (1999). The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting. Mol. Biol. Cell 10, 1873-1889.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1873-1889
    • Tall, G.G.1    Hiroko, H.2    DeWald, D.B.3    Horazdovsky, B.F.4
  • 40
    • 0034679831 scopus 로고    scopus 로고
    • Discrimination of GLUT4 vesicle trafficking from fusion using a temperature-sensitive Munc18c mutant
    • Thurmond, D. C. and Pessin, J. E. (2000). Discrimination of GLUT4 vesicle trafficking from fusion using a temperature-sensitive Munc18c mutant. EMBO J. 19, 3565-3575.
    • (2000) EMBO J , vol.19 , pp. 3565-3575
    • Thurmond, D.C.1    Pessin, J.E.2
  • 43
    • 0031665836 scopus 로고    scopus 로고
    • The dynamics of Golgi protein traffic visualized in living yeast cells
    • Wooding, S. and Pelham, H. (1998). The dynamics of Golgi protein traffic visualized in living yeast cells. Mol. Biol. Cell 9, 2667-2680.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2667-2680
    • Wooding, S.1    Pelham, H.2
  • 44
    • 0034735539 scopus 로고    scopus 로고
    • New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
    • Wurmser, A. E., Sato, T. K. and Emr, S. D. (2000). New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J. Cell. Biol. 151, 551-562.
    • (2000) J. Cell. Biol , vol.151 , pp. 551-562
    • Wurmser, A.E.1    Sato, T.K.2    Emr, S.D.3
  • 46
    • 0035116167 scopus 로고    scopus 로고
    • Vesicular transport and the Golgi apparatus in yeast
    • Yoda, K. and Noda, Y. (2001). Vesicular transport and the Golgi apparatus in yeast. J. Biosci. Bioeng. 91, 1-11.
    • (2001) J. Biosci. Bioeng , vol.91 , pp. 1-11
    • Yoda, K.1    Noda, Y.2


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