메뉴 건너뛰기




Volumn 16, Issue 10, 2005, Pages 4918-4930

Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARTIC ACID; CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHOPROTEIN; PROTEIN SED5; SERINE; SNARE PROTEIN; T SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 26244449794     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-02-0101     Document Type: Article
Times cited : (35)

References (40)
  • 1
    • 0031808667 scopus 로고    scopus 로고
    • Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p
    • Ballensiefen, W., Ossipov, D., and Schmitt, H. D. (1998). Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p. J. Cell Sci. 111, 1507-1520.
    • (1998) J. Cell Sci. , vol.111 , pp. 1507-1520
    • Ballensiefen, W.1    Ossipov, D.2    Schmitt, H.D.3
  • 2
    • 0027997974 scopus 로고
    • Localization of Sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane and cytoplasmic domains
    • Banfield, D. K., Lewis, M. J., Rabouille, C., Warren, G., and Pelham, H. R. (1994). Localization of Sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane and cytoplasmic domains. J. Cell Biol. 127, 357-371.
    • (1994) J. Cell Biol. , vol.127 , pp. 357-371
    • Banfield, D.K.1    Lewis, M.J.2    Rabouille, C.3    Warren, G.4    Pelham, H.R.5
  • 3
    • 0033574449 scopus 로고    scopus 로고
    • Brefeldin A: The advantage of being uncompetitive
    • Chardin, P., and McCormick, F. (1999). Brefeldin A: the advantage of being uncompetitive. Cell 97, 153-155.
    • (1999) Cell , vol.97 , pp. 153-155
    • Chardin, P.1    McCormick, F.2
  • 5
    • 0029042360 scopus 로고
    • Yeast synaptobrevin homologs are modified post-translationally by the addition of palmitate
    • Couve, A., Protopopov, V., and Gerst, J. E. (1995). Yeast synaptobrevin homologs are modified post-translationally by the addition of palmitate. Proc. Natl. Acad. Sci. USA 92, 5987-5991.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5987-5991
    • Couve, A.1    Protopopov, V.2    Gerst, J.E.3
  • 6
    • 0031975699 scopus 로고    scopus 로고
    • The Golgi apparatus: 100 Years of progress and controversy
    • Farquhar, M. G., and Palade, G. E. (1998). The Golgi apparatus: 100 years of progress and controversy. Trends Cell Biol. 8, 2-10.
    • (1998) Trends Cell Biol. , vol.8 , pp. 2-10
    • Farquhar, M.G.1    Palade, G.E.2
  • 7
    • 0030990122 scopus 로고    scopus 로고
    • The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p
    • Fischer von Mollard, G., Nothwehr, S. F., and Stevens, T. H. (1997). The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p. J. Cell Biol. 137, 1511-1524.
    • (1997) J. Cell Biol. , vol.137 , pp. 1511-1524
    • Fischer Von Mollard, G.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 8
    • 0026097957 scopus 로고
    • Localization of components involved in protein transport and processing through the yeast Golgi apparatus
    • Franzusoff, A., Redding, K., Crosby, J., Fuller, R. S., and Schekman, R. (1991). Localization of components involved in protein transport and processing through the yeast Golgi apparatus. J. Cell Biol. 112, 27-37.
    • (1991) J. Cell Biol. , vol.112 , pp. 27-37
    • Franzusoff, A.1    Redding, K.2    Crosby, J.3    Fuller, R.S.4    Schekman, R.5
  • 9
    • 0030475350 scopus 로고    scopus 로고
    • Cell biology: Alternatives to baker's yeast
    • Glick, B. S. (1996). Cell biology: alternatives to baker's yeast. Curr. Biol. 6, 1570-1572.
    • (1996) Curr. Biol. , vol.6 , pp. 1570-1572
    • Glick, B.S.1
  • 10
  • 11
    • 0026756118 scopus 로고
    • SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex
    • Hardwick, K. G., and Pelham, H. R. (1992). SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex. J. Cell Biol. 119, 513-521.
    • (1992) J. Cell Biol. , vol.119 , pp. 513-521
    • Hardwick, K.G.1    Pelham, H.R.2
  • 12
    • 0030969912 scopus 로고    scopus 로고
    • Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment
    • Jedd, G., Mulholland, J., and Segev, N. (1997). Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment. J. Cell Biol. 137, 563-580.
    • (1997) J. Cell Biol. , vol.137 , pp. 563-580
    • Jedd, G.1    Mulholland, J.2    Segev, N.3
  • 14
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis, M. J., and Pelham, H. R. (1996). SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 85, 205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.2
  • 15
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, A., Demarini, D., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J. R. (1998). Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie, A.2    Demarini, D.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 16
    • 0030668326 scopus 로고    scopus 로고
    • Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic
    • Lupashin, V. V., Pokrovskaya, I. D., McNew, J. A., and Waters, M. G. (1997). Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic. Mol. Biol. Cell 8, 2659-2676.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2659-2676
    • Lupashin, V.V.1    Pokrovskaya, I.D.2    McNew, J.A.3    Waters, M.G.4
  • 17
    • 0033006355 scopus 로고    scopus 로고
    • Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis
    • Lustgarten, V., and Gerst, J. E. (1999). Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis. Mol. Cell. Biol. 19, 4480-4494.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4480-4494
    • Lustgarten, V.1    Gerst, J.E.2
  • 18
    • 0035253856 scopus 로고    scopus 로고
    • SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast
    • Marash, M., and Gerst, J. E. (2001). t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast. EMBO J. 20, 411-421.
    • (2001) EMBO J. , vol.20 , pp. 411-421
    • Marash, M.1    Gerst, J.E.2
  • 19
    • 0042470298 scopus 로고    scopus 로고
    • Phosphorylation of the autoinhibitory domain of the Sso t-SNAREs promotes binding of the Vsm1 SNARE regulator in yeast
    • Marash, M., and Gerst, J. E. (2003). Phosphorylation of the autoinhibitory domain of the Sso t-SNAREs promotes binding of the Vsm1 SNARE regulator in yeast. Mol. Biol. Cell 14, 3114-3125.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3114-3125
    • Marash, M.1    Gerst, J.E.2
  • 20
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz, M., Morsomme, P., and Riezman, H. (2001). Protein sorting upon exit from the endoplasmic reticulum. Cell 104, 313-320.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 21
    • 0032516856 scopus 로고    scopus 로고
    • SNAREs and membrane fusion in the Golgi apparatus
    • Nichols, B. J., and Pelham, H. R. (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.2
  • 22
    • 0019424489 scopus 로고
    • Order of events in the yeast secretory pathway
    • Novick, P., Ferro, S., and Schekman, R. (1981). Order of events in the yeast secretory pathway. Cell 25, 461-469.
    • (1981) Cell , vol.25 , pp. 461-469
    • Novick, P.1    Ferro, S.2    Schekman, R.3
  • 24
    • 0031964997 scopus 로고    scopus 로고
    • Getting through the Golgi complex
    • Pelham, H. R. (1998). Getting through the Golgi complex. Trends Cell Biol. 8, 45-49.
    • (1998) Trends Cell Biol. , vol.8 , pp. 45-49
    • Pelham, H.R.1
  • 25
    • 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
  • 26
    • 0034664730 scopus 로고    scopus 로고
    • The debate about transport in the Golgi-two sides of the same coin?
    • Pelham, H. R., and Rothman, J. E. (2000). The debate about transport in the Golgi-two sides of the same coin? Cell 102, 713-719.
    • (2000) Cell , vol.102 , pp. 713-719
    • Pelham, H.R.1    Rothman, J.E.2
  • 27
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia postoris and Saccharomyces cerevisiae
    • Rossanese, O. W., Soderholm, J., Bevis, J., Sears, I. B., O'Connor, J., Williamson, E. K., and Glick, B. S. (1999). Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia postoris and Saccharomyces cerevisiae. J. Cell Biol. 145, 69-81.
    • (1999) J. Cell Biol. , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.2    Bevis, J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Glick, B.S.7
  • 28
    • 0034839401 scopus 로고    scopus 로고
    • Deconstructing the Golgi
    • Rossanese, O. W., and Glick, B. S. (2001). Deconstructing the Golgi. Traffic 2, 589-596.
    • (2001) Traffic , vol.2 , pp. 589-596
    • Rossanese, O.W.1    Glick, B.S.2
  • 29
    • 0035795423 scopus 로고    scopus 로고
    • A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae
    • Rossanese, O. W., Reinke, C. A., Bevis, B. J., Hammond, A. T., Sears, I. B., O'Connor, J., and Glick, B. S. (2001). A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae. J. Cell Biol. 153, 47-62.
    • (2001) J. Cell Biol. , vol.153 , pp. 47-62
    • Rossanese, O.W.1    Reinke, C.A.2    Bevis, B.J.3    Hammond, A.T.4    Sears, I.B.5    O'Connor, J.6    Glick, B.S.7
  • 30
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza, J. C., Hardwick, K. G., Dean, N., and Pelham, H. R. (1990). ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61, 1349-1357.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.4
  • 31
  • 32
    • 0028168008 scopus 로고
    • A Rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Sogaard, M., Tani, K., Ye, R. R., Geromanos, S., Tempst, P., Kirchhausen, T., Rothman, J. E., and Sollner, T. (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
  • 33
    • 0032476574 scopus 로고    scopus 로고
    • Reconstitution of retrograde transport from the Golgi to the ER in vitro
    • Spang, A., and Schekman, R. (1998). Reconstitution of retrograde transport from the Golgi to the ER in vitro. J. Cell Biol. 143, 589-599.
    • (1998) J. Cell Biol. , vol.143 , pp. 589-599
    • Spang, A.1    Schekman, R.2
  • 34
    • 0020181690 scopus 로고
    • Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
    • Stevens, T., Esmon, B., and Schekman, R. (1982). Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole. Cell 30, 439-448.
    • (1982) Cell , vol.30 , pp. 439-448
    • Stevens, T.1    Esmon, B.2    Schekman, R.3
  • 35
    • 0030665269 scopus 로고    scopus 로고
    • Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast
    • Sutterlin, C., Doering, T. L., Schimmoller, F., Schroder, S., and Riezman, H. (1997). Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J. Cell Sci. 110, 2703-2714.
    • (1997) J. Cell Sci. , vol.110 , pp. 2703-2714
    • Sutterlin, C.1    Doering, T.L.2    Schimmoller, F.3    Schroder, S.4    Riezman, H.5
  • 36
    • 0035158866 scopus 로고    scopus 로고
    • Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions
    • Tsui, M. M., Tai, W. C., and Banfield, D. K. (2001). Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions. Mol. Biol. Cell 12, 521-538.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 521-538
    • Tsui, M.M.1    Tai, W.C.2    Banfield, D.K.3
  • 37
    • 0027513757 scopus 로고
    • Brefeldin a causes a defect in secretion in Saccharomyces cerevisiae
    • Vogel, J. P., Lee, J. N., Kirsch, D. R., Rose, M. D., and Sztu, E. S. (1993). Brefeldin A causes a defect in secretion in Saccharomyces cerevisiae. J. Biol. Chem. 268, 3040-3043.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3040-3043
    • Vogel, J.P.1    Lee, J.N.2    Kirsch, D.R.3    Rose, M.D.4    Sztu, E.S.5
  • 38
    • 26244439145 scopus 로고    scopus 로고
    • Regulation of SNARE assembly by protein phosphorylation
    • Weinberger, A., and Gerst, J. E. (2004). Regulation of SNARE assembly by protein phosphorylation. Top. Curr. Genet. 10, 145-170.
    • (2004) Top. Curr. Genet. , vol.10 , pp. 145-170
    • Weinberger, A.1    Gerst, J.E.2
  • 39
    • 0031665836 scopus 로고    scopus 로고
    • The dynamics of Golgi protein traffic visualized in living yeast cells
    • Wooding, S., and Pelham, H.R. (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.R.2
  • 40
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 Binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • Yamaguchi, T., Dulubova, I., Min, S. W., Chen, X., Rizo, J., and Sudhof, T. C. (2002). Sly1 Binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev. Cell 2, 295-305.
    • (2002) Dev. Cell , vol.2 , pp. 295-305
    • Yamaguchi, T.1    Dulubova, I.2    Min, S.W.3    Chen, X.4    Rizo, J.5    Sudhof, T.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.