ArticleProceedings of the National Academy of Sciences of the United States of America2014
Cog5-Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- COG Complex in Golgi Trafficking and Glycosylation.Sub-cellular biochemistry · 2026Review
- Characterization of a missense variant in COG5 in a Tunisian patient with COG5-CDG syndrome and insights into the effect of non-synonymous variants on COG5 protein.Journal of human genetics · 2024Article
- Structure of a membrane tethering complex incorporating multiple SNAREs.Nature structural & molecular biology · 2024Article
- Epigenetic link between Agent Orange exposure and type 2 diabetes in Korean veterans.Frontiers in endocrinology · 2024Article
- Genetic interaction network has a very limited impact on the evolutionary trajectories in continuous culture-grown populations of yeast.BMC ecology and evolution · 2021Article
- COG5 variants lead to complex early onset retinal degeneration, upregulation of PERK and DNA damage.Scientific reports · 2020Article
- Golgi inCOGnito: From vesicle tethering to human disease.Biochimica et biophysica acta. General subjects · 2020Review
- Membrane detachment is not essential for COG complex function.Molecular biology of the cell · 2018Article
- Conserved Oligomeric Golgi and Neuronal Vesicular Trafficking.Handbook of experimental pharmacology · 2018Review
- Molecular architecture of the complete COG tethering complex.Nature structural & molecular biology · 2016Article
- COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex.Scientific reports · 2016Article
- COG Complex Complexities: Detailed Characterization of a Complete Set of HEK293T Cells Lacking Individual COG Subunits.Frontiers in cell and developmental biology · 2016Article
- Identification of Rab41/6d Effectors Provides an Explanation for the Differential Effects of Rab41/6d and Rab6a/a' on Golgi Organization.Frontiers in cell and developmental biology · 2016Article
- Bridging the Gap between Glycosylation and Vesicle Traffic.Frontiers in cell and developmental biology · 2016Review
- Creating Knockouts of Conserved Oligomeric Golgi Complex Subunits Using CRISPR-Mediated Gene Editing Paired with a Selection Strategy Based on Glycosylation Defects Associated with Impaired COG Complex Function.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Tethering Complexes in the Arabidopsis Endomembrane System.Frontiers in cell and developmental biology · 2016Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The conserved oligomeric Golgi (COG) complex is required, along with SNARE and Sec1/Munc18 (SM) proteins, for vesicle docking and fusion at the Golgi. COG, like other multisubunit tethering complexes (MTCs), is thought to function as a scaffold and/or chaperone to direct the assembly of productive SNARE complexes at the sites of membrane fusion. Reflecting this essential role, mutations in the COG complex can cause congenital disorders of glycosylation. A deeper understanding of COG function and dysfunction will likely depend on elucidating its molecular structure. Despite some progress toward this goal, including EM studies of COG lobe A (subunits 1-4) and higher-resolution structures of portions of Cog2 and Cog4, the structures of COG's eight subunits and the principles governing their assembly are mostly unknown. Here, we report the crystal structure of a complex between two lobe B subunits, Cog5 and Cog7. The structure reveals that Cog5 is a member of the complexes associated with tethering containing helical rods (CATCHR) fold family, with homology to subunits of other MTCs including the Dsl1, exocyst, and Golgi-associated retrograde protein (GARP) complexes. The Cog5-Cog7 interaction is analyzed in relation to the Dsl1 complex, the only other CATCHR-family MTC for which subunit interactions have been characterized in detail. Biochemical and functional studies validate the physiological relevance of the observed Cog5-Cog7 interface, indicate that it is conserved from yeast to humans, and demonstrate that its disruption in human cells causes defects in trafficking and glycosylation.
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