ESCRT IV complex

GO:1990621 · Other · Multiprotein complex · Proposed

An ESCRT complex that has AAA-ATPase activity and is involved in ESCRT-mediated intralumenal vesicle formation and the final stages of cytokinesis. The complex catalyzes disassembly of the ESCRT III filament around the neck of the budding vesicle in an ATP-driven reaction, resulting in membrane scission and recycling of the ESCRT III components back to the cytosol. In yeast, it is formed by the AAA ATPase Vps4 and its cofactor Vta1. [GO:1990621]

Synonyms: ESCRT-IV; Vps4-Vta1 complex; Vps4 complex

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

Components

Component	Type	Part of / acts on	Grounding	Genes	Stoichiometry	Essential	Role
Vps4 AAA ATPase	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	VPS4		UNKNOWN	ATPase constituent that assembles with Vta1 and powers ESCRT-III disassembly and recycling. `PMID:20696398` Yang and Hurley 2010 solved a yeast Vta1/Vps4 interface structure and modeled Vta1 with Vps4 during ESCRT-III disassembly. `DOI:10.1016/j.devcel.2011.05.015` Henne, Buchkovich and Emr 2011 reviewed Vps4 as the AAA ATPase that disassembles ESCRT-III during ESCRT recycling.
Vta1 Vps4 cofactor	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	VTA1		UNKNOWN	Vps4 cofactor that binds the Vps4 beta domain and stabilizes Vps4-Vta1 assemblies used for ESCRT-III disassembly. `PMID:20696398` Yang and Hurley 2010 determined the dimeric Vta1 VSL domain bound to Vps4 domains and modeled the Vps4-Vta1 ESCRT recycling assembly.

Taxonomic distribution

NCBITaxon:4932 Saccharomyces cerevisiae — COMMON: Budding yeast uses a Vps4 AAA ATPase and Vta1 cofactor complex to recycle ESCRT-III from endosomal membranes. [PMID:20696398]

Canonical examples

NCBITaxon:4932 Saccharomyces cerevisiae — Structural model in which Yang and Hurley solved the Vta1-Vps4 interface used by the ESCRT recycling ATPase. [PMID:20696398]

Functions

intralumenal vesicle formation GO:0070676 — ESCRT-IV recycles ESCRT-III from endosomal membranes as ESCRT machinery drives intralumenal-vesicle formation.
- GO:1990621 GO defines ESCRT IV as an ESCRT complex involved in ESCRT-mediated intralumenal vesicle formation.
- DOI:10.1016/j.devcel.2011.05.015 Henne, Buchkovich and Emr 2011 reviewed Vps4-mediated disassembly as the ESCRT recycling step in MVB sorting.
ATP hydrolysis activity GO:0016887 — The Vps4 ATPase subunit hydrolyzes ATP to remodel and recycle ESCRT-III assemblies.
- GO:1990621 GO defines ESCRT IV as an ESCRT complex with AAA-ATPase activity.
- PMID:20696398 Yang and Hurley 2010 modeled Vta1-stabilized Vps4 assemblies that use ATPase activity for ESCRT-III disassembly.

Mechanism graphs

Vps4-Vta1 recycles ESCRT-III in yeast (FUNCTION)

In Saccharomyces cerevisiae, Vta1 binds Vps4 in the ESCRT-IV complex, which disassembles ESCRT-III assemblies after membrane remodeling in the MVB pathway.

Subject	Predicate	Object	Evidence
Vps4 AAA ATPase	is part of	ESCRT IV complex	`GO:1990621` GO defines yeast ESCRT IV as formed by Vps4 and Vta1. `PMID:20696398` Yang and Hurley 2010 crystallized yeast Vps4 domains with Vta1.
Vta1 Vps4 cofactor	is part of	ESCRT IV complex	`GO:1990621` GO defines yeast ESCRT IV as formed by Vps4 and Vta1. `PMID:20696398` Yang and Hurley 2010 crystallized yeast Vta1 with Vps4 domains.
Vta1 Vps4 cofactor	stabilizes	Vps4 AAA ATPase	`PMID:20696398` Yang and Hurley 2010 modeled Vta1 as a stabilizing component of Vps4-Vta1 complexes.
ESCRT IV complex	disassembles	ESCRT III complex	`GO:1990621` GO defines ESCRT IV as catalyzing ESCRT III filament disassembly. `DOI:10.1016/j.devcel.2011.05.015` Henne, Buchkovich and Emr 2011 reviewed Vps4 recycling of ESCRT-III as the late ESCRT step.
ESCRT IV complex	releases	cytosolic ESCRT-III subunits	`GO:1990621` GO defines ESCRT IV as recycling ESCRT III components back to the cytosol.
ESCRT IV complex	participates in	intralumenal vesicle formation	`GO:1990621` GO defines ESCRT IV as involved in ESCRT-mediated intralumenal vesicle formation. `PMID:20696398` Yang and Hurley 2010 studied Vps4 and Vta1 in the context of ESCRT-III recycling.

Discussions

CURATION_TODO (OPEN): Resolve exact source-neutral InterPro or Pfam groundings for the Vps4 AAA ATPase and Vta1 cofactor component classes. This first ESCRT IV complex record records the named budding-yeast Vps4 and Vta1 proteins without asserting paralogy boundaries or family accessions that have not been reviewed exactly.
INTERPRETATION (RESOLVED): Keep Did2, Ist1, Vps60 and Doa4 regulation outside the first ESCRT IV component boundary. The GO ESCRT IV definition identifies Vps4 and Vta1 as the yeast complex boundary. Henne, Buchkovich and Emr 2011 review additional regulators that modulate ESCRT-III disassembly or deubiquitination, but they are not asserted here as stable ESCRT IV constituents.

Evidence

GO:1990621 Gene Ontology cellular-component term for ESCRT IV complex.
GO:0036452 OLS places ESCRT IV complex under the ESCRT complex.
GO:0070676 Gene Ontology biological-process term for intralumenal vesicle formation at endosomal membranes.
GO:0016887 Gene Ontology molecular-function term for ATP hydrolysis activity.
PMID:20696398 Yang and Hurley 2010, Structural role of the Vps4-Vta1 interface in ESCRT-III recycling, Structure.
DOI:10.1016/j.devcel.2011.05.015 Henne, Buchkovich and Emr 2011, The ESCRT Pathway, Developmental Cell.

Curation history

2026-09-24T01:07:30Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-09-24T01:09:27Z codex · EXPANDED_RECORD — Added ESCRT-IV synonymy and GO parentage, reviewed-label-only Vps4 and Vta1 components, Saccharomyces scope, intralumenal-vesicle formation and ATPase functions, GO/PMID/DOI evidence, a yeast ESCRT-III recycling graph, and a regulator-boundary discussion.
2026-09-24T01:18:49Z codex · FIX_DISCUSSION_ANCHOR — Removed the invalid section-level attaches_to value from the ESCRT-IV accessory-factor boundary discussion.

Source: data/structures/other/escrt_iv_complex.yaml