Detailed analysis of the interaction of yeast COG complex1

Cell Structure and Function

Volumn 43, Issue 2, 2018, Pages 119-127

  Ishii, Midori ^a,b   Lupashin, Vladimir V ^c   Nakano, Akihiko ^a,b  

^a Institute of Physical and Chemical Research   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

Author keywords

COG complex; Membrane trafficking; Multi subunit tethering complex; The Golgi apparatus; Yeast

Indexed keywords

ARTICLE; CONGENITAL DISORDER OF GLYCOSYLATION; CONSERVED OLIGOMERIC GOLGI COMPLEX; CONTROLLED STUDY; CYTOSOL; FUNGUS MUTANT; GOLGI COMPLEX; IMMUNOPRECIPITATION; MITOCHONDRION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; YEAST CELL; GLYCOSYLATION; HUMAN; METABOLISM; PROTEIN ANALYSIS; PROTEIN SUBUNIT; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE;

COG1 PROTEIN, S CEREVISIAE; COG3 PROTEIN, S CEREVISIAE; COG6 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; VESICULAR TRANSPORT ADAPTOR PROTEIN; VESICULAR TRANSPORT PROTEIN;

ADAPTOR PROTEINS, VESICULAR TRANSPORT; CONGENITAL DISORDERS OF GLYCOSYLATION; GLYCOSYLATION; GOLGI APPARATUS; HUMANS; PROTEIN INTERACTION MAPS; PROTEIN SUBUNITS; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; VESICULAR TRANSPORT PROTEINS;

EID: 85051000867     PISSN: 03867196     EISSN: 13473700     Source Type: Journal    
DOI: 10.1247/csf.18014     Document Type: Article

References (34)

1. Anderson, N.S., Mukherjee, I., Bentivoglio, C.M., and Barlowe, C. 2017. The golgin protein Coy1 functions in intra- Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs. Mol. Biol. Cell, 28: 2686–2700.
2. Bailey Blackburn, J., Pokrovskaya, I., Fisher, P., Ungar, D., and Lupashin, V.V. 2016. COG Complex Complexities: Detailed Characterization of a Complete Set of HEK293T Cells Lacking Individual COG Subunits. Front. Cell Dev. Biol., 4: 23.
3. Bonifacino, J.S. and Glick, B.S. 2004. The mechanisms of vesicle budding and fusion. Cell, 116: 153–166.
4. Brachmann, C.B., Davies, A., Cost, G.J., Caputo, E., Li, J., Hieter, P., and Boeke, J.D. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCRmediated gene disruption and other applications. Yeast, 14: 115–132.
5. Bruinsma, P., Spelbrink, R.G., and Nothwehr, S.F. 2004. Retrograde transport of the mannosyltransferase Och1p to the early Golgi requires a component of the COG transport complex. J. Biol. Chem., 279: 39814–39823.
6. Cai, H., Reinisch, K., and Ferro-Novick, S. 2007. Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev. Cell, 12: 671–682.
7. Fotso, P., Koryakina, Y., Pavliv, O., Tsiomenko, A.B., and Lupashin, V.V. 2005. Cog1p plays a central role in the organization of the yeast conserved oligomeric Golgi complex. J. Biol. Chem., 280: 27613–27623.
8. Freeze, H.H. and Ng, B.G. 2011. Golgi glycosylation and human inherited diseases. Cold Spring Harb. Perspect. Biol., 3: a005371.
9. Fridy, P.C., Li, Y., Keegan, S., Thompson, M.K., Nudelman, I., Scheid, J.F., Oeffinger, M., Nussenzweig, M.C., Fenyo, D., Chait, B.T., and Rout, M.P. 2014. A robust pipeline for rapid production of versatile nanobody repertoires. Nat. Methods, 11: 1253–1260.
10. Glick, B.S. and Nakano, A. 2009. Membrane traffic within the Golgi apparatus. Annu. Rev. Cell Dev. Biol., 25: 113–132.
11. Glick, B.S. and Luini, A. 2011. Models for Golgi traffic: a critical assessment. Cold Spring Harb. Perspect. Biol., 3: a005215.
12. Ishii, M., Suda, Y., Kurokawa, K., and Nakano, A. 2016. COPI is essential for Golgi cisternal maturation and dynamics. J. Cell Sci., 129: 3251–3261.
13. Kurokawa, K., Ishii, M., Suda, Y., Ichihara, A., and Nakano, A. 2013. Live cell visualization of Golgi membrane dynamics by superresolution confocal live imaging microscopy. Method. Cell Biol., 118: 235–242.
14. Kurokawa, K., Okamoto, M., and Nakano, A. 2014. Contact of cis-Golgi with ER exit sites executes cargo capture and delivery from the ER. Nat. Commun., 5: 3653.
15. Lees, J.A., Yip, C.K., Walz, T., and Hughson, F.M. 2010. Molecular organization of the COG vesicle tethering complex. Nat. Struct. Mol. Biol., 17: 1292–1297.
16. Luo, G., Zhang, J., and Guo, W. 2014. The role of Sec3p in secretory vesicle targeting and exocyst complex assembly. Mol. Biol. Cell, 25: 3813–3822.
17. Mozdy, A.D., McCaffery, J.M., and Shaw, J.M. 2000. Dnm1p GTPasemediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol., 151: 367–380.
18. Munro, S. 1998. Localization of proteins to the Golgi apparatus. Trends Cell Biol., 8: 11–15.
19. Nakano, A. and Luini, A. 2010. Passage through the Golgi. Curr. Opin. Cell Biol., 22: 471–478.
20. Oka, T., Vasile, E., Penman, M., Novina, C.D., Dykxhoorn, D.M., Ungar, D., Hughson, F.M., and Krieger, M. 2005. Genetic analysis of the subunit organization and function of the conserved oligomeric golgi (COG) complex: studies of COG5- and COG7-deficient mammalian cells. J. Biol. Chem., 280: 32736–32745.
21. Orlean, P. 2012. Architecture and biosynthesis of the Saccharomyces cerevisiae cell wall. Genetics, 192: 775–818.
22. Papanikou, E., Day, K.J., Austin, J., and Glick, B.S. 2015. COPI selectively drives maturation of the early Golgi. Elife, 4.
23. Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., Tinevez, J.Y., White, D.J., Hartenstein, V., Eliceiri, K., Tomancak, P., and Cardona, A. 2012. Fiji: an open-source platform for biologicalimage analysis. Nat. Methods, 9: 676–682.
24. Sengupta, D., Truschel, S., Bachert, C., and Linstedt, A.D. 2009. Organ‐elle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network. J. Cell Biol., 186: 41–55.
25. Shestakova, A., Suvorova, E., Pavliv, O., Khaidakova, G., and Lupashin, V. 2007. Interaction of the conserved oligomeric Golgi complex with t- SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability. J. Cell Biol., 179: 1179–1192.
26. Suvorova, E.S., Duden, R., and Lupashin, V.V. 2002. 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.
27. Ungar, D., Oka, T., Brittle, E.E., Vasile, E., Lupashin, V.V., Chatterton, J.E., Heuser, J.E., Krieger, M., and Waters, M.G. 2002. Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function. J. Cell Biol., 157: 405–415.
28. Ungar, D., Oka, T., Vasile, E., Krieger, M., and Hughson, F.M. 2005. Subunit architecture of the conserved oligomeric Golgi complex. J. Biol. Chem., 280: 32729–32735.
29. VanRheenen, S.M., Cao, X., Lupashin, V.V., Barlowe, C., and Waters, M.G. 1998. Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking. J. Cell Biol., 141: 1107–1119.
30. VanRheenen, S.M., Cao, X., Sapperstein, S.K., Chiang, E.C., Lupashin, V.V., Barlowe, C., and Waters, M.G. 1999. Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p. J. Cell Biol., 147: 729–742.
31. Whyte, J.R. and Munro, S. 2001. 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.
32. Willett, R., Kudlyk, T., Pokrovskaya, I., Schonherr, R., Ungar, D., Duden, R., and Lupashin, V. 2013. COG complexes form spatial landmarks for distinct SNARE complexes. Nat. Commun., 4: 1553.
33. Willett, R., Blackburn, J.B., Climer, L., Pokrovskaya, I., Kudlyk, T., Wang, W., and Lupashin, V. 2016. COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex. Sci. Rep., 6: 29139.
34. Wuestehube, L.J., Duden, R., Eun, A., Hamamoto, S., Korn, P., Ram, R., and Schekman, R. 1996. New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex. Genetics, 142: 393–406.