ESCRT II complex

GO:0000814 · Other · Multiprotein complex · Proposed

An endosomal sorting complex required for transport and functions downstream of ESCRT I complex. It consists of the class E vacuolar protein sorting (Vps) proteins and is required for the membrane recruitment of ESCRT III complex and binds to ubiquitinated cargoes. [GO:0000814]

Synonyms: ESCRT-II complex; endosomal sorting complex required for transport

Part of: endosome membrane (GO:0010008)

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
Vps22 ESCRT-II subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	VPS22	UNKNOWN	Vps22 core constituent of the yeast ESCRT-II sorting complex. `DOI:10.1016/j.devcel.2004.09.003` Teo et al. 2004 solved a Saccharomyces cerevisiae ESCRT-II core structure containing Vps22, Vps25 and the C-terminal region of Vps36.
Vps25 ESCRT-II subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	VPS25	UNKNOWN	Vps25 core constituent of the yeast ESCRT-II sorting complex. `DOI:10.1016/j.devcel.2004.09.003` Teo et al. 2004 solved the Saccharomyces cerevisiae ESCRT-II core as a trilobal complex with two Vps25 copies plus Vps22 and the C-terminal region of Vps36.
Vps36 ESCRT-II subunit	Protein	part of	Reviewed label only (reviewed name; no accession asserted)	VPS36	UNKNOWN	Vps36 core constituent of the yeast ESCRT-II sorting complex. `DOI:10.1016/j.devcel.2004.09.003` Teo et al. 2004 solved a Saccharomyces cerevisiae ESCRT-II core structure containing the C-terminal region of Vps36 together with Vps22 and Vps25.

Taxonomic distribution

NCBITaxon:4932 Saccharomyces cerevisiae — COMMON: Budding-yeast ESCRT-II contains Vps22, Vps25 and Vps36 and acts with ESCRT-I and ESCRT-III in endosomal multivesicular-body sorting. [DOI:10.1016/j.devcel.2004.09.003]

Canonical examples

NCBITaxon:4932 Saccharomyces cerevisiae — Model yeast used to determine the ESCRT-II core architecture and to map direct binding between ESCRT-II and the Vps20 subunit of ESCRT-III. [DOI:10.1016/j.devcel.2004.09.003]

Functions

multivesicular body sorting pathway GO:0071985 — ESCRT-II acts after ESCRT-I in the endosomal MVB pathway and promotes downstream ESCRT-III recruitment during cargo sorting.
- GO:0071985 GO:0071985 denotes the vesicle-mediated transport pathway that moves ubiquitylated transmembrane proteins into multivesicular-body luminal vesicles.
- DOI:10.1016/j.devcel.2009.07.008 Im et al. 2009 mapped the ESCRT-II/VPS20 interface and showed that ESCRT-II directly activates ESCRT-III-driven vesicle budding and scission in vitro.

Mechanism graphs

ESCRT-II recruits ESCRT-III during yeast MVB sorting (FUNCTION)

In Saccharomyces cerevisiae, Vps22, Vps25 and Vps36 form ESCRT-II, which transiently associates with endosomal membranes and initiates ESCRT-III formation during MVB sorting.

Subject	Predicate	Object	Evidence
Vps22 ESCRT-II subunit	is part of	ESCRT II complex	`DOI:10.1016/j.devcel.2004.09.003` Teo et al. 2004 placed Vps22 in the Saccharomyces cerevisiae ESCRT-II core.
Vps25 ESCRT-II subunit	is part of	ESCRT II complex	`DOI:10.1016/j.devcel.2004.09.003` Teo et al. 2004 resolved two Vps25 copies in the Saccharomyces cerevisiae ESCRT-II core.
Vps36 ESCRT-II subunit	is part of	ESCRT II complex	`DOI:10.1016/j.devcel.2004.09.003` Teo et al. 2004 placed the Vps36 C-terminal region in the Saccharomyces cerevisiae ESCRT-II core.
ESCRT II complex	transiently associates with	endosome membrane	`DOI:10.1016/j.devcel.2004.09.003` Teo et al. 2004 described ESCRT-II as part of the sequentially recruited endosomal ESCRT machinery.
ESCRT II complex	recruits	ESCRT III complex	`DOI:10.1016/j.devcel.2009.07.008` Im et al. 2009 mapped the ESCRT-II interaction with the ESCRT-III subunit VPS20.
ESCRT II complex	participates in	multivesicular body sorting pathway	`DOI:10.1016/j.devcel.2009.07.008` Im et al. 2009 connected the ESCRT-II/ESCRT-III interaction to cargo sorting and intralumenal-vesicle scission in MVBs.

Discussions

CURATION_TODO (OPEN): Resolve exact source-neutral InterPro or Pfam groundings for the Vps22, Vps25 and Vps36 ESCRT-II subunit classes. This first ESCRT-II record records the named Saccharomyces cerevisiae Vps22, Vps25 and Vps36 subunits without asserting paralogy boundaries or source-neutral InterPro/Pfam families unless those identifiers are reviewed exactly.
CURATION_TODO (RESOLVED): Do not model Vps4 as a constituent component of ESCRT-II. Vps4 is the AAA ATPase that acts after ESCRT-III assembly, so it is out of scope for the constituent ESCRT-II component list in this first record.
CURATION_TODO (OPEN): Review and curate the one Vps22, two Vps25 and one Vps36 heterotetrameric ESCRT-II stoichiometry. Hierro et al. 2004 resolved the yeast ESCRT-II structural architecture as a Y-shaped heterotetramer. This first ESCRT-II record leaves per-component stoichiometry blank until the exact copy numbers and family-level component boundaries are reviewed together.

Evidence

GO:0000814 Gene Ontology cellular-component term for ESCRT II complex.
GO:0036452 Gene Ontology cellular-component parent term for the ESCRT complex class.
GO:0010008 Gene Ontology cellular-component term for the endosome membrane.
GO:0000815 Gene Ontology cellular-component term for the downstream ESCRT III complex.
GO:0071985 Gene Ontology biological-process term for the multivesicular body sorting pathway.
DOI:10.1038/nature02914 Hierro, Sun, Rusnak, Kim, Prag, Emr and Hurley 2004, Structure of the ESCRT-II endosomal trafficking complex, Nature.
DOI:10.1016/j.devcel.2004.09.003 Teo et al. 2004 resolved the yeast ESCRT-II core and mapped its direct interaction with ESCRT-III/Vps20.
DOI:10.1016/j.devcel.2008.04.004 Im and Hurley 2008 resolved human ESCRT-II structures containing one VPS22, one VPS36 and two VPS25 copies.
DOI:10.1016/j.devcel.2009.07.008 Im et al. 2009 crystallized the ESCRT-II/VPS20 interface and tested ESCRT-II activation of ESCRT-III-driven membrane scission.
DOI:10.1126/science.1161070 Lata et al. 2008 analyzed ESCRT-III assembly and Vps4-mediated ESCRT-III disassembly.

Curation history

2026-09-16T16:05:38Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-09-16T16:06:20Z codex · EXPANDED_RECORD — Added ESCRT-II synonymy, GO parentage and endosome membrane parthood, reviewed-label-only Vps22, Vps25 and Vps36 core subunits, Saccharomyces scope, an MVB sorting function, GO/DOI evidence, a nonmechanistic yeast ESCRT-III recruitment graph, a subunit-grounding TODO, and a resolved Vps4 boundary decision.
2026-09-16T16:06:51Z codex · REFINED_RECORD — Shortened ESCRT-II component role text to avoid repeating each subunit's full label inside its role.
2026-09-16T16:20:19Z codex · ADDRESSED_PR_REVIEW — Addressed PR #1108 review issue #1109 by tracking the Hierro et al. 2004 ESCRT-II heterotetramer architecture as an open stoichiometry curation TODO with structural evidence.
2026-09-21T07:19:16Z codex · REPLACED_UNREADABLE_EVIDENCE — Resolved #1219 by replacing unreadable Babst et al. 2002 ESCRT-II citations with reachable Teo 2004, Im and Hurley 2008, Im et al. 2009, Lata et al. 2008, and Hierro et al. 2004 evidence.
2026-09-21T07:49:02Z codex · ADDRESSED_PR_REVIEW — Resolved #1221 by removing abstract-only Henne et al. 2011 support from ESCRT-II subunit, Vps4-boundary and stoichiometry-specific claims that are now backed by directly reachable Teo 2004, Lata 2008, Im and Hurley 2008, and Hierro 2004 evidence.

Source: data/structures/other/escrt_ii_complex.yaml