exomer complex
A protein complex that acts as a selective cargo adaptor mediating the selective transport of specific membrane proteins from the trans-Golgi network (TGN) to the plasma membrane. [GO:0034044]
Synonyms: Chs5/6 complex
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| Chs5 exomer scaffold subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | CHS5 | UNKNOWN | Scaffold subunit that assembles with Chs6-family ChAP cargo-binding subunits to form the yeast exomer complex.
| |
| Chs6 exomer ChAP subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | CHS6 | UNKNOWN | Chs5-Arf1-binding protein and cargo-binding subunit that helps select Chs3 for exomer-mediated export.
| |
| Bch1 exomer ChAP subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | BCH1 | UNKNOWN | Chs5-Arf1-binding protein that redundantly supports Chs3 association with Bud7 in the yeast exomer complex.
| |
| Bud7 exomer ChAP subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | BUD7 | UNKNOWN | Chs5-Arf1-binding protein that redundantly supports Chs3 association with Bch1 in the yeast exomer complex.
| |
| Bch2 exomer ChAP subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | BCH2 | UNKNOWN | Chs5-Arf1-binding protein represented among the ChAP cargo-binding subunits of yeast exomer.
|
Taxonomic distribution
NCBITaxon:4932Saccharomyces cerevisiae — COMMON: Budding yeast has a Chs5/ChAP exomer complex that mediates selected cargo export from the trans-Golgi network to the plasma membrane. [DOI:10.1083/jcb.200605106]
Canonical examples
NCBITaxon:4932Saccharomyces cerevisiae — Budding-yeast model in which Chs5 and the ChAP subunits were assigned to the exomer cargo-adaptor complex. [DOI:10.1091/mbc.e06-03-0210]
Functions
- Golgi to plasma membrane transport
GO:0006893— Exomer mediates selective export of specific membrane-protein cargoes from the trans-Golgi network to the plasma membrane.GO:0006893GO:0006893 denotes vesicle-mediated transport from the trans-Golgi network to the plasma membrane.DOI:10.1083/jcb.200605106Wang et al. 2006 named exomer as a yeast coat complex for select trans-Golgi-network-to-plasma-membrane transport.
Mechanism graphs
Chs5 and ChAP subunits assemble exomer for TGN export (ASSEMBLY)
In Saccharomyces cerevisiae, the Chs5 scaffold assembles with Chs6-family ChAP cargo-binding subunits to form exomer, which supports selected export from the trans-Golgi network to the plasma membrane.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| Arf1 GTPase | supports membrane recruitment of | exomer complex |
|
| Chs5 exomer scaffold subunit | assembles with | Chs6 exomer ChAP subunit |
|
| Chs5 exomer scaffold subunit | assembles with | Bch1 exomer ChAP subunit |
|
| Chs5 exomer scaffold subunit | assembles with | Bud7 exomer ChAP subunit |
|
| Chs5 exomer scaffold subunit | assembles with | Bch2 exomer ChAP subunit |
|
| Chs5 exomer scaffold subunit | localizes to | trans-Golgi network |
|
| Chs5 exomer scaffold subunit | is part of | exomer complex |
|
| Chs6 exomer ChAP subunit | is part of | exomer complex |
|
| Bch1 exomer ChAP subunit | is part of | exomer complex |
|
| Bud7 exomer ChAP subunit | is part of | exomer complex |
|
| Bch2 exomer ChAP subunit | is part of | exomer complex |
|
| exomer complex | participates in | Golgi to plasma membrane transport |
|
Discussions
- CURATION_TODO (OPEN): Resolve exact source-neutral InterPro, Pfam, or NCBIfam groundings for the five yeast exomer subunit classes. This first exomer record names the yeast Chs5, Chs6, Bch1, Bud7 and Bch2 constituent subunits but leaves InterPro, Pfam, or NCBIfam grounding unset until exact orthology and paralogy boundaries are reviewed per subunit.
- CURATION_TODO (RESOLVED): Do not model Arf1 as a constituent exomer subunit. Arf1 binds ChAPs and supports exomer membrane association for Golgi export, but the curated exomer identity is the stable Chs5/ChAP cargo-adaptor complex rather than its recruiting Arf-family GTPase.
Evidence
GO:0034044Gene Ontology cellular-component term for the exomer complex.GO:0032991Gene Ontology cellular-component parent term for protein-containing complexes.GO:0006893Gene Ontology biological-process term for Golgi-to-plasma-membrane transport.DOI:10.1038/sj.emboj.7601007Trautwein et al. 2006, Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi, The EMBO Journal.DOI:10.1083/jcb.200605106Wang, Hamamoto, Orci and Schekman 2006, Exomer: a coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast, Journal of Cell Biology.DOI:10.1091/mbc.e06-03-0210Sanchatjate and Schekman 2006, Chs5/6 complex: a multiprotein complex that interacts with and conveys chitin synthase III from the trans-Golgi network to the cell surface, Molecular Biology of the Cell.DOI:10.15252/embr.201540795Huranova, Muruganandam, Weiss and Spang 2016, Dynamic assembly of the exomer secretory vesicle cargo adaptor subunits, EMBO Reports.
Curation history
2026-09-18T07:32:14Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-18T07:33:22Zcodex · EXPANDED_RECORD — Added exomer protein-complex parentage, the Chs5/6 synonym, reviewed-label-only yeast Chs5 and ChAP components, Saccharomyces scope, a Golgi-to-plasma-membrane transport function, GO/DOI evidence, a nonmechanistic exomer assembly graph, and subunit grounding plus Arf1-boundary discussions.2026-09-18T07:33:55Zcodex · REFORMATTED_RECORD — Expanded shared YAML evidence aliases into plain repeated mappings.2026-09-18T07:47:07Zcodex · FIXED_DISCUSSION_ANCHOR — Retargeted the Arf1 boundary discussion from the invalid whole components section to the five concrete exomer component anchors.2026-09-18T07:57:56Zcodex · REFINED_ARF1_EDGE — #1132: Retargeted the Arf1 graph edge from Chs5-specific recruitment to whole-exomer membrane recruitment and cited Wang et al. 2006 for the Arf1-dependent membrane-binding evidence.