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Volumn 4, Issue , 2013, Pages

COG complexes form spatial landmarks for distinct SNARE complexes

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; COG4 PROTEIN; COG8 PROTEIN; GS27 PROTEIN; SNAP29 PROTEIN; SNARE PROTEIN; STX16 PROTEIN; STX5 PROTEIN; STX6 PROTEIN; UNCLASSIFIED DRUG;

EID: 84875886094     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2535     Document Type: Article
Times cited : (74)

References (41)
  • 1
    • 0842324801 scopus 로고    scopus 로고
    • The Mechanisms of Vesicle Budding and Fusion
    • DOI 10.1016/S0092-8674(03)01079-1
    • Bonifacino, J. S. & Glick, B. S. The mechanisms of vesicle budding and fusion. Cell 116, 153-166 (2004). (Pubitemid 38167309)
    • (2004) Cell , vol.116 , Issue.2 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 2
    • 84867141973 scopus 로고    scopus 로고
    • Retrograde vesicle transport in the Golgi
    • Cottam, N. P. & Ungar, D. Retrograde vesicle transport in the Golgi. Protoplasma 249, 943-955 (2011).
    • (2011) Protoplasma , vol.249 , pp. 943-955
    • Cottam, N.P.1    Ungar, D.2
  • 3
    • 78049368534 scopus 로고    scopus 로고
    • Tethering factors as organizers of intracellular vesicular traffic
    • Yu, I. M. & Hughson, F. M. Tethering factors as organizers of intracellular vesicular traffic. Annu. Rev. Cell Dev. Biol. 26, 137-156 (2010).
    • (2010) Annu. Rev. Cell Dev. Biol , vol.26 , pp. 137-156
    • Yu, I.M.1    Hughson, F.M.2
  • 4
    • 78650138725 scopus 로고    scopus 로고
    • An update on transport vesicle tethering
    • Brown, F. C. & Pfeffer, S. R. An update on transport vesicle tethering. Mol. Membr. Biol. 27, 457-461 (2010).
    • (2010) Mol. Membr. Biol , vol.27 , pp. 457-461
    • Brown, F.C.1    Pfeffer, S.R.2
  • 6
    • 79960557412 scopus 로고    scopus 로고
    • Membrane dynamics and fusion at late endosomes and vacuoles-Rab regulation, multisubunit tethering complexes and SNAREs
    • Epp, N., Rethmeier, R., Kramer, L. & Ungermann, C. Membrane dynamics and fusion at late endosomes and vacuoles-Rab regulation, multisubunit tethering complexes and SNAREs. Eur. J. Cell Biol. 90, 779-785 (2011).
    • (2011) Eur. J. Cell Biol , vol.90 , pp. 779-785
    • Epp, N.1    Rethmeier, R.2    Kramer, L.3    Ungermann, C.4
  • 8
    • 0035489304 scopus 로고    scopus 로고
    • The Sec34/35 Golgi Transport Complex Is Related to the Exocyst, Defining a Family of Complexes Involved in Multiple Steps of Membrane Traffic
    • DOI 10.1016/S1534-5807(01)00063-6, PII S1534580701000636
    • Whyte, J. R. & Munro, S. The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Dev. Cell 1, 527-537 (2001). (Pubitemid 33586104)
    • (2001) Developmental Cell , vol.1 , Issue.4 , pp. 527-537
    • Whyte, J.R.C.1    Munro, S.2
  • 10
    • 23044502309 scopus 로고    scopus 로고
    • Cog1p plays a central role in the organization of the yeast conserved oligomeric Golgi complex
    • DOI 10.1074/jbc.M504597200
    • Fotso, P., Koryakina, Y., Pavliv, O., Tsiomenko, A. B. & Lupashin, V. V. Cog1p plays a central role in the organization of the yeast conserved oligomeric golgi complex. J. Biol. Chem. 280, 27613-27623 (2005). (Pubitemid 41076873)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 27613-27623
    • Fotso, P.1    Koryakina, Y.2    Pavliv, O.3    Tsiomenko, A.B.4    Lupashin, V.V.5
  • 11
    • 25444486756 scopus 로고    scopus 로고
    • Subunit architecture of the conserved oligomeric Golgi complex
    • DOI 10.1074/jbc.M504590200
    • Ungar, D., Oka, T., Vasile, E., Krieger, M. & Hughson, F. M. Subunit architecture of the conserved oligomeric golgi complex. J. Biol. Chem. 280, 32729-32735 (2005). (Pubitemid 41368318)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.38 , pp. 32729-32735
    • Ungar, D.1    Oka, T.2    Vasile, E.3    Krieger, M.4    Hughson, F.M.5
  • 12
    • 81855168333 scopus 로고    scopus 로고
    • Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery
    • Pokrovskaya, I. D. et al. Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery. Glycobiology 21, 1554-1569 (2011).
    • (2011) Glycobiology , vol.21 , pp. 1554-1569
    • Pokrovskaya, I.D.1
  • 13
    • 70349165974 scopus 로고    scopus 로고
    • COG defects birth and rise!
    • Foulquier, F. COG defects, birth and rise! Biochim Biophys Acta 1792, 896-902 (2009).
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 896-902
    • Foulquier, F.1
  • 14
    • 0037071543 scopus 로고    scopus 로고
    • The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins
    • DOI 10.1083/jcb.200111081
    • Suvorova, E. S., Duden, R. & Lupashin, V. V. The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J. Cell Biol. 157, 631-643 (2002). (Pubitemid 34839791)
    • (2002) Journal of Cell Biology , vol.157 , Issue.4 , pp. 631-643
    • Suvorova, E.S.1    Duden, R.2    Lupashin, V.V.3
  • 15
    • 37249008781 scopus 로고    scopus 로고
    • Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability
    • DOI 10.1083/jcb.200705145
    • Shestakova, A., Suvorova, E., Pavliv, O., Khaidakova, G. & Lupashin, V. Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability. J. Cell Biol. 179, 1179-1192 (2007). (Pubitemid 350277737)
    • (2007) Journal of Cell Biology , vol.179 , Issue.6 , pp. 1179-1192
    • Shestakova, A.1    Suvorova, E.2    Pavliv, O.3    Khaidakova, G.4    Lupashin, V.5
  • 16
    • 80052572363 scopus 로고    scopus 로고
    • The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport
    • Laufman, O., Hong, W. & Lev, S. The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport. J. Cell Biol. 194, 459-472 (2011).
    • (2011) J. Cell Biol , vol.194 , pp. 459-472
    • Laufman, O.1    Hong, W.2    Lev, S.3
  • 17
    • 67650475442 scopus 로고    scopus 로고
    • Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network
    • Sengupta, D., Truschel, S., Bachert, C. & Linstedt, A. D. Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network. J. Cell Biol. 186, 41-55 (2009).
    • (2009) J. Cell Biol , vol.186 , pp. 41-55
    • Sengupta, D.1    Truschel, S.2    Bachert, C.3    Linstedt, A.D.4
  • 18
    • 84872045592 scopus 로고    scopus 로고
    • COG6 interacts with a subset of the Golgi SNAREs and is important for the Golgi complex integrity
    • Kudlyk, T., Willett, R., Pokrovskaya, I. D. & Lupashin, V. COG6 interacts with a subset of the Golgi SNAREs and is important for the Golgi complex integrity. Traffic 14, 194-204 (2012).
    • (2012) Traffic , vol.14 , pp. 194-204
    • Kudlyk, T.1    Willett, R.2    Pokrovskaya, I.D.3    Lupashin, V.4
  • 19
    • 67651166603 scopus 로고    scopus 로고
    • Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing
    • Laufman, O., Kedan, A., Hong, W. & Lev, S. Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing. EMBO J. 28, 2006-2017 (2009).
    • (2009) EMBO J , vol.28 , pp. 2006-2017
    • Laufman, O.1    Kedan, A.2    Hong, W.3    Lev, S.4
  • 21
    • 14744272136 scopus 로고    scopus 로고
    • Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells
    • DOI 10.1083/jcb.200412003
    • Zolov, S. N. & Lupashin, V. V. Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. J. Cell Biol. 168, 747-759 (2005). (Pubitemid 40328159)
    • (2005) Journal of Cell Biology , vol.168 , Issue.5 , pp. 747-759
    • Zolov, S.N.1    Lupashin, V.V.2
  • 23
    • 70350378203 scopus 로고    scopus 로고
    • The COG complex Rab6 and COPI define a novel Golgi retrograde trafficking pathway that is exploited by SubAB toxin
    • Smith, R. D. et al. The COG complex, Rab6 and COPI define a novel Golgi retrograde trafficking pathway that is exploited by SubAB toxin. Traffic 10, 1502-1517 (2009).
    • (2009) Traffic , vol.10 , pp. 1502-1517
    • Smith, R.D.1
  • 25
    • 77956527512 scopus 로고    scopus 로고
    • Syntaxin 16: Unraveling cellular physiology through a ubiquitous SNARE molecule
    • Chen, Y., Gan, B. Q. & Tang, B. L. Syntaxin 16: unraveling cellular physiology through a ubiquitous SNARE molecule. J. Cell Physiol. 225, 326-332 (2010).
    • (2010) J. Cell Physiol , vol.225 , pp. 326-332
    • Chen, Y.1    Gan, B.Q.2    Tang, B.L.3
  • 26
    • 0037341432 scopus 로고    scopus 로고
    • GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: Involvement of an acidic targeting motif
    • DOI 10.1091/mbc.E02-06-0315
    • Shewan, A. M. et al. GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in syntaxins 6 and 16 but not TGN38: involvement of an acidic targeting motif. Mol. Biol. Cell 14, 973-986 (2003). (Pubitemid 36337446)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.3 , pp. 973-986
    • Shewan, A.M.1    Van Dam, E.M.2    Martin, S.3    Luen, T.B.4    Hong, W.5    Bryant, N.J.6    James, D.E.7
  • 27
    • 70349319578 scopus 로고    scopus 로고
    • Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network
    • Perez-Victoria, F. J. & Bonifacino, J. S. Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network. Mol. Cell Biol. 29, 5251-5263 (2009).
    • (2009) Mol. Cell Biol , vol.29 , pp. 5251-5263
    • Perez-Victoria, F.J.1    Bonifacino, J.S.2
  • 28
    • 17644416413 scopus 로고    scopus 로고
    • Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p
    • DOI 10.1021/bi048008z
    • Sivaram, M. V., Saporita, J. A., Furgason, M. L., Boettcher, A. J. & Munson, M. Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p. Biochemistry 44, 6302-6311 (2005). (Pubitemid 40570724)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6302-6311
    • Sivaram, M.V.S.1    Saporita, J.A.2    Furgason, M.L.M.3    Boettcher, A.J.4    Munson, M.5
  • 29
    • 24344480456 scopus 로고    scopus 로고
    • Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast
    • DOI 10.1091/mbc.E05-01-0056
    • Kraynack, B. A. et al. Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast. Mol. Biol. Cell 16, 3963-3977 (2005). (Pubitemid 41262870)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.9 , pp. 3963-3977
    • Kraynack, B.A.1    Chan, A.2    Rosenthal, E.3    Essid, M.4    Umansky, B.5    Waters, M.G.6    Schmitt, H.D.7
  • 31
    • 84858022403 scopus 로고    scopus 로고
    • Quantitative proteomic and genetic analyses of the schizophrenia susceptibility factor dysbindin identify novel roles of the biogenesis of lysosome-related organelles complex 1
    • Gokhale, A. et al. Quantitative proteomic and genetic analyses of the schizophrenia susceptibility factor dysbindin identify novel roles of the biogenesis of lysosome-related organelles complex 1. J. Neurosci. 32, 3697-3711 (2012).
    • (2012) J. Neurosci , vol.32 , pp. 3697-3711
    • Gokhale, A.1
  • 32
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • DOI 10.1016/0092-8674(93)90376-2
    • Söllner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H. & Rothman, J. E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418 (1993). (Pubitemid 23335067)
    • (1993) Cell , vol.75 , Issue.3 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 33
    • 0034648797 scopus 로고    scopus 로고
    • Topological restriction of SNARE-dependent membrane fusion (see comments
    • Parlati, F. et al. Topological restriction of SNARE-dependent membrane fusion (see comments). Nature 407, 194-198 (2000).
    • (2000) Nature , vol.407 , pp. 194-198
    • Parlati, F.1
  • 34
    • 77958163770 scopus 로고    scopus 로고
    • Fast vesicle fusion in living cells requires at least three SNARE complexes
    • Mohrmann, R., de Wit, H., Verhage, M., Neher, E. & Sorensen, J. B. Fast vesicle fusion in living cells requires at least three SNARE complexes. Science 330, 502-505 (2010).
    • (2010) Science , vol.330 , pp. 502-505
    • Mohrmann, R.1    De Wit, H.2    Verhage, M.3    Neher, E.4    Sorensen, J.B.5
  • 36
    • 69049098806 scopus 로고    scopus 로고
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum
    • Giorgi, C., De Stefani, D., Bononi, A., Rizzuto, R. & Pinton, P. Structural and functional link between the mitochondrial network and the endoplasmic reticulum. Int. J. Biochem. Cell Biol. 41, 1817-1827 (2009).
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , pp. 1817-1827
    • Giorgi, C.1    De Stefani, D.2    Bononi, A.3    Rizzuto, R.4    Pinton, P.5
  • 37
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito, O. M. & Scorrano, L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456, 605-610 (2008).
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 38
    • 80054844842 scopus 로고    scopus 로고
    • ER tubules mark sites of mitochondrial division
    • Friedman, J. R. et al. ER tubules mark sites of mitochondrial division. Science 334, 358-362 (2011).
    • (2011) Science , vol.334 , pp. 358-362
    • Friedman, J.R.1
  • 39
    • 26944465716 scopus 로고    scopus 로고
    • The steady-state distribution of glycosyltransferases between the Golgi apparatus and the endoplasmic reticulum is approximately 90:10
    • DOI 10.1111/j.1600-0854.2005.00333.x
    • Rhee, S. W., Starr, T., Forsten-Williams, K. & Storrie, B. The steady-state distribution of glycosyltransferases between the Golgi apparatus and the endoplasmic reticulum is approximately 90:10. Traffic 6, 978-990 (2005). (Pubitemid 41472457)
    • (2005) Traffic , vol.6 , Issue.11 , pp. 978-990
    • Rhee, S.W.1    Starr, T.2    Forsten-Williams, K.3    Storrie, B.4
  • 40
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., Halladay, J. & Craig, E. A. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144, 1425-1436 (1996).
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 41
    • 48249118352 scopus 로고    scopus 로고
    • Cytoplasmic lipid droplets are translocated into the lumen of the Chlamydia trachomatis parasitophorous vacuole
    • Cocchiaro, J. L., Kumar, Y., Fischer, E. R., Hackstadt, T. & Valdivia, R. H. Cytoplasmic lipid droplets are translocated into the lumen of the Chlamydia trachomatis parasitophorous vacuole. Proc. Natl Acad. Sci. USA 105, 9379-9384 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9379-9384
    • Cocchiaro, J.L.1    Kumar, Y.2    Fischer, E.R.3    Hackstadt, T.4    Valdivia, R.H.5


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