title: IntraGolgi distribution of the Conserved Oligomeric Golgi (COG) complex.
abstract: The Conserved Oligomeric Golgi (COG) complex is an eight-subunit (Cog1-8) peripheral Golgi protein involved in membrane trafficking and glycoconjugate synthesis. COG appears to participate in retrograde vesicular transport and is required to maintain normal Golgi structure and function. COG mutations interfere with normal transport, distribution, and/or stability of Golgi proteins associated with glycoconjugate synthesis and trafficking, and lead to failure of spermatogenesis in Drosophila melanogaster, misdirected migration of gonadal distal tip cells in Caenorhabditis elegans, and type II congenital disorders of glycosylation in humans. The mechanism by which COG influences Golgi structure and function is unclear. Immunogold electron microscopy was used to visualize the intraGolgi distribution of a functional, hemagglutinin epitope-labeled COG subunit, Cog1-HA, that complements the Cog1-deficiency in Cog1-null Chinese hamster ovary cells. COG was found to be localized primarily on or in close proximity to the tips and rims of the Golgi's cisternae and their associated vesicles and on vesicles and vesiculo-tubular structures seen on both the cis and trans-Golgi Network faces of the cisternal stacks, in some cases on COPI containing vesicles. These findings support the proposal that COG is directly involved in controlling vesicular retrograde transport of Golgi resident proteins throughout the Golgi apparatus.
authors.affiliation: Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors.forename: Eliza
authors.initials: E
authors.lastname: Vasile
authors.forename: Toshihiko
authors.initials: T
authors.lastname: Oka
authors.forename: Maria
authors.initials: M
authors.lastname: Ericsson
authors.forename: Nobuhiro
authors.initials: N
authors.lastname: Nakamura
authors.forename: Monty
authors.initials: M
authors.lastname: Krieger
mesh_terms: D033942:Adaptor Proteins, Vesicular Transport / Q000172:deficiency / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D016466:CHO Cells; D002478:Cells, Cultured; D020755:Coat Protein Complex I / Q000648:ultrastructure; D006224:Cricetinae; D003412:Cricetulus; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000378:metabolism; D006801:Humans; D009154:Mutation / Q000235:genetics; D010446:Peptide Fragments / Q000378:metabolism; D010641:Phenotype; D021381:Protein Transport; D021601:trans-Golgi Network / Q000648:ultrastructure
chemical_list: D033942:Adaptor Proteins, Vesicular Transport; C486489:COG1 protein, human; D020755:Coat Protein Complex I; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D010446:Peptide Fragments; C475510:tyrosyl-prolyl-tyrosyl-aspartyl-valyl-prolyl-aspartyl-tyrosyl-alanine