COG complex

GO:0017119 · Other · Multiprotein complex · Proposed

A multisubunit tethering complex of the CATCHR family (complexes associated with tethering containing helical rods) that has a role in tethering vesicles to the Golgi prior to fusion. Composed of 8 subunits COG1-8. [GO:0017119]

Synonyms: conserved oligomeric Golgi complex; Golgi transport complex; Sec34/35 complex

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

Component	Type	Part of / acts on	Grounding	Genes	Essential	Role
Cog1 COG subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	COG1	UNKNOWN	Lobe-A constituent of the eight-subunit COG vesicle-tethering complex. `DOI:10.1083/jcb.200202016` Ungar et al. 2002 unified the mammalian Golgi transport, ldlCp and Sec34 complexes as the eight-subunit conserved oligomeric Golgi complex. `DOI:10.1074/jbc.M400662200` Loh and Hong 2004 compared the mammalian COG subunits with their yeast counterparts and mapped pairwise interactions within the complex.
Cog2 COG subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	COG2	UNKNOWN	Lobe-A constituent of the eight-subunit COG vesicle-tethering complex. `DOI:10.1083/jcb.200202016` Ungar et al. 2002 unified the mammalian Golgi transport, ldlCp and Sec34 complexes as the eight-subunit conserved oligomeric Golgi complex. `DOI:10.1074/jbc.M400662200` Loh and Hong 2004 compared the mammalian COG subunits with their yeast counterparts and mapped pairwise interactions within the complex.
Cog3 COG subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	COG3	UNKNOWN	Lobe-A constituent of the eight-subunit COG vesicle-tethering complex. `DOI:10.1083/jcb.200202016` Ungar et al. 2002 unified the mammalian Golgi transport, ldlCp and Sec34 complexes as the eight-subunit conserved oligomeric Golgi complex. `DOI:10.1074/jbc.M400662200` Loh and Hong 2004 compared the mammalian COG subunits with their yeast counterparts and mapped pairwise interactions within the complex.
Cog4 COG subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	COG4	UNKNOWN	Lobe-A constituent of the eight-subunit COG vesicle-tethering complex. `DOI:10.1083/jcb.200202016` Ungar et al. 2002 unified the mammalian Golgi transport, ldlCp and Sec34 complexes as the eight-subunit conserved oligomeric Golgi complex. `DOI:10.1074/jbc.M400662200` Loh and Hong 2004 compared the mammalian COG subunits with their yeast counterparts and mapped pairwise interactions within the complex.
Cog5 COG subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	COG5	UNKNOWN	Lobe-B constituent of the eight-subunit COG vesicle-tethering complex. `DOI:10.1083/jcb.200202016` Ungar et al. 2002 unified the mammalian Golgi transport, ldlCp and Sec34 complexes as the eight-subunit conserved oligomeric Golgi complex. `DOI:10.1074/jbc.M400662200` Loh and Hong 2004 compared the mammalian COG subunits with their yeast counterparts and mapped pairwise interactions within the complex.
Cog6 COG subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	COG6	UNKNOWN	Lobe-B constituent of the eight-subunit COG vesicle-tethering complex. `DOI:10.1083/jcb.200202016` Ungar et al. 2002 unified the mammalian Golgi transport, ldlCp and Sec34 complexes as the eight-subunit conserved oligomeric Golgi complex. `DOI:10.1074/jbc.M400662200` Loh and Hong 2004 compared the mammalian COG subunits with their yeast counterparts and mapped pairwise interactions within the complex.
Cog7 COG subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	COG7	UNKNOWN	Lobe-B constituent of the eight-subunit COG vesicle-tethering complex. `DOI:10.1083/jcb.200202016` Ungar et al. 2002 unified the mammalian Golgi transport, ldlCp and Sec34 complexes as the eight-subunit conserved oligomeric Golgi complex. `DOI:10.1074/jbc.M400662200` Loh and Hong 2004 compared the mammalian COG subunits with their yeast counterparts and mapped pairwise interactions within the complex.
Cog8 COG subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	COG8	UNKNOWN	Lobe-B constituent of the eight-subunit COG vesicle-tethering complex. `DOI:10.1083/jcb.200202016` Ungar et al. 2002 unified the mammalian Golgi transport, ldlCp and Sec34 complexes as the eight-subunit conserved oligomeric Golgi complex. `DOI:10.1074/jbc.M400662200` Loh and Hong 2004 compared the mammalian COG subunits with their yeast counterparts and mapped pairwise interactions within the complex.

Taxonomic distribution

NCBITaxon:4932 Saccharomyces cerevisiae — COMMON: Budding yeast has an intact hetero-octameric COG vesicle-tethering complex associated with the Golgi apparatus. [DOI:10.1038/nsmb.3263]

Canonical examples

NCBITaxon:4932 Saccharomyces cerevisiae — Budding-yeast model in which the complete hetero-octameric COG tethering complex was purified and imaged by negative-stain electron microscopy. [DOI:10.1038/nsmb.3263]

Functions

Golgi vesicle transport GO:0048193 — COG acts as a Golgi vesicle tethering complex during retrograde vesicular traffic within and to the Golgi apparatus.
- GO:0048193 GO:0048193 denotes vesicle-mediated movement into, out of or within the Golgi apparatus.
- DOI:10.1247/csf.18014 Ishii, Lupashin and Nakano 2018 studied yeast COG subunit interactions in the context of Golgi membrane trafficking.

Mechanism graphs

COG supports Golgi vesicle tethering (FUNCTION)

In Saccharomyces cerevisiae, Cog1 through Cog8 form a hetero-octameric COG complex associated with Golgi membrane trafficking.

Subject	Predicate	Object	Evidence
Cog1 COG subunit	is part of	COG complex	`DOI:10.1083/jcb.200202016` Ungar et al. 2002 named Cog1 through Cog8 as COG complex subunits. `DOI:10.1038/nsmb.3263` Ha et al. 2016 purified and imaged the complete hetero-octameric COG complex from Saccharomyces cerevisiae.
Cog2 COG subunit	is part of	COG complex	`DOI:10.1083/jcb.200202016` Ungar et al. 2002 named Cog1 through Cog8 as COG complex subunits. `DOI:10.1038/nsmb.3263` Ha et al. 2016 purified and imaged the complete hetero-octameric COG complex from Saccharomyces cerevisiae.
Cog3 COG subunit	is part of	COG complex	`DOI:10.1083/jcb.200202016` Ungar et al. 2002 named Cog1 through Cog8 as COG complex subunits. `DOI:10.1038/nsmb.3263` Ha et al. 2016 purified and imaged the complete hetero-octameric COG complex from Saccharomyces cerevisiae.
Cog4 COG subunit	is part of	COG complex	`DOI:10.1083/jcb.200202016` Ungar et al. 2002 named Cog1 through Cog8 as COG complex subunits. `DOI:10.1038/nsmb.3263` Ha et al. 2016 purified and imaged the complete hetero-octameric COG complex from Saccharomyces cerevisiae.
Cog5 COG subunit	is part of	COG complex	`DOI:10.1083/jcb.200202016` Ungar et al. 2002 named Cog1 through Cog8 as COG complex subunits. `DOI:10.1038/nsmb.3263` Ha et al. 2016 purified and imaged the complete hetero-octameric COG complex from Saccharomyces cerevisiae.
Cog6 COG subunit	is part of	COG complex	`DOI:10.1083/jcb.200202016` Ungar et al. 2002 named Cog1 through Cog8 as COG complex subunits. `DOI:10.1038/nsmb.3263` Ha et al. 2016 purified and imaged the complete hetero-octameric COG complex from Saccharomyces cerevisiae.
Cog7 COG subunit	is part of	COG complex	`DOI:10.1083/jcb.200202016` Ungar et al. 2002 named Cog1 through Cog8 as COG complex subunits. `DOI:10.1038/nsmb.3263` Ha et al. 2016 purified and imaged the complete hetero-octameric COG complex from Saccharomyces cerevisiae.
Cog8 COG subunit	is part of	COG complex	`DOI:10.1083/jcb.200202016` Ungar et al. 2002 named Cog1 through Cog8 as COG complex subunits. `DOI:10.1038/nsmb.3263` Ha et al. 2016 purified and imaged the complete hetero-octameric COG complex from Saccharomyces cerevisiae.
COG complex	participates in	Golgi vesicle transport	`DOI:10.1247/csf.18014` Ishii, Lupashin and Nakano 2018 studied COG as a yeast multi-subunit tethering complex acting in Golgi membrane trafficking.

Discussions

CURATION_TODO (OPEN): Resolve exact source-neutral family groundings for the eight COG subunits. This first COG record names the Cog1-Cog8 constituent subunits but leaves InterPro, Pfam, or Complex Portal grounding unset until exact orthology and paralogy boundaries are reviewed per subunit.
CURATION_TODO (RESOLVED): Do not model COPI coats or Golgi SNAREs as constituent COG components. COG physically and functionally interacts with COPI coats and Golgi SNARE proteins, but its constituent subunits are Cog1 through Cog8.

Evidence

GO:0017119 Gene Ontology cellular-component term for the COG complex.
GO:0099023 Gene Ontology cellular-component parent term for vesicle tethering complexes.
GO:0048193 Gene Ontology biological-process term for Golgi vesicle transport.
DOI:10.1083/jcb.200202016 Ungar et al. 2002, Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function, Journal of Cell Biology.
DOI:10.1074/jbc.M400662200 Loh and Hong 2004, The binary interacting network of the conserved oligomeric Golgi tethering complex, Journal of Biological Chemistry.
DOI:10.1038/nsmb.3263 Ha et al. 2016, Molecular architecture of the complete COG tethering complex, Nature Structural and Molecular Biology.
DOI:10.1247/csf.18014 Ishii, Lupashin and Nakano 2018, Detailed Analysis of the Interaction of Yeast COG Complex, Cell Structure and Function.
DOI:10.1083/jcb.200412003 Zolov and Lupashin 2005, Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells, Journal of Cell Biology.

Curation history

2026-09-16T19:28:32Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-09-16T19:29:20Z codex · EXPANDED_RECORD — Added COG synonymy, vesicle-tethering parentage, reviewed-label-only Cog1-Cog8 components, Saccharomyces cerevisiae scope, a Golgi vesicle transport function, GO/DOI evidence, a nonmechanistic yeast Golgi tethering graph, a subunit-grounding TODO, and a resolved COPI/SNARE boundary decision.
2026-09-16T19:30:01Z codex · REFINED_RECORD — Tightened Cog1-Cog8 role text, added an explicit COG-to-Golgi graph edge, and promoted the Zolov and Lupashin COPI/SNARE boundary citation to record-level evidence.
2026-09-16T19:38:30Z codex · ADDRESSED_PR_REVIEW — Resolved PR #1122 issue #1123 by adding Ha et al. 2016 yeast evidence to the Cog1-Cog8 graph parthood edges and removing the mammalian-backed COG-to-Golgi localization edge from the yeast graph.

Source: data/structures/other/cog_complex.yaml