vacuolar membrane

GO:0005774 · Membrane organelle · Membrane · Proposed

The lipid bilayer surrounding the vacuole and separating its contents from the cytoplasm of the cell. [GO:0005774]

Part of: vacuole (GO:0005773)

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
vacuolar membrane lipid bilayer	Lipid	part of	Reviewed label only (reviewed name; no accession asserted)			ESSENTIAL	Bounding lipid bilayer that separates the vacuolar lumen from the cytosol. `GO:0005774` GO:0005774 identifies the vacuolar membrane as the lipid bilayer surrounding a vacuole. `GO:0005775` GO:0005775 identifies the vacuolar lumen enclosed by the vacuolar membrane.

Taxonomic distribution

NCBITaxon:4932 Saccharomyces cerevisiae — COMMON: Budding yeast vacuoles are bounded by vacuolar membranes that carry V-ATPase acidification machinery. [DOI:10.1016/j.bbamcr.2008.08.003]

Canonical examples

NCBITaxon:4932 Saccharomyces cerevisiae — Budding-yeast model whose vacuolar membrane contains the Vac8p partner for Nvj1p-mediated nucleus-vacuole junctions. [DOI:10.1091/mbc.11.7.2445]

Functions

vacuolar acidification GO:0007035 — Vacuolar membranes host proton-pumping V-ATPase complexes that raise the hydrogen-ion concentration in the vacuolar lumen.
- GO:0007035 GO:0007035 denotes processes that lower vacuolar pH by raising the vacuolar hydrogen-ion concentration.
- DOI:10.1128/MMBR.70.1.177-191.2006 Kane 2006 reviews yeast V-ATPase proton pumping at organelle membranes.
nucleus-vacuole junction formation — Yeast vacuolar membranes supply Vac8p for direct binding to Nvj1p on the nuclear outer membrane.
- DOI:10.1091/mbc.11.7.2445 Pan et al. 2000 showed that Saccharomyces cerevisiae Nvj1p and Vac8p directly interact to form nucleus-vacuole junctions.

Mechanism graphs

Yeast vacuolar membranes acidify and contact the nucleus (FUNCTION)

In budding yeast, the vacuolar membrane encloses the vacuole, hosts V-ATPase acidification machinery, and carries Vac8p for Nvj1p-mediated contact with the nuclear outer membrane.

Subject	Predicate	Object	Evidence
vacuolar membrane	is part of	vacuole	`GO:0005774` GO:0005774 identifies the vacuolar membrane. `GO:0005773` GO:0005773 identifies the containing vacuole.
vacuolar membrane	bounds	vacuolar lumen	`GO:0005774` GO:0005774 defines the surrounding vacuolar membrane. `GO:0005775` GO:0005775 identifies the vacuolar lumen.
vacuolar proton-transporting V-type ATPase complex	resides in	vacuolar membrane	`GO:0016471` GO:0016471 defines the V-type ATPase complex by its vacuolar-membrane location. `DOI:10.1128/MMBR.70.1.177-191.2006` Kane 2006 reviews vacuolar H+-ATPase-dependent organelle acidification in yeast.
vacuolar proton-transporting V-type ATPase complex	participates in	vacuolar acidification	`GO:0007035` GO:0007035 denotes processes that acidify the vacuole. `DOI:10.1016/j.bbamcr.2008.08.003` Li and Kane 2009 review V-ATPase-dependent acidification of the yeast lysosome-like vacuole.
Vac8p	localizes to	vacuolar membrane	`DOI:10.1091/mbc.11.7.2445` Pan et al. 2000 identified Vac8p as the vacuolar Nvj1p partner that forms nucleus-vacuole junctions.
Nvj1p	localizes to	nuclear outer membrane	`DOI:10.1091/mbc.11.7.2445` Pan et al. 2000 identified Nvj1p as an outer nuclear membrane protein at nucleus-vacuole junctions.
vacuolar membrane	contacts	nuclear outer membrane	`DOI:10.1091/mbc.11.7.2445` Pan et al. 2000 showed that direct Vac8p/Nvj1p interaction forms junctions between the yeast vacuole and nucleus.
Nvj1p	interacts with	Vac8p	`DOI:10.1091/mbc.11.7.2445` Pan et al. 2000 found that Nvj1p directly interacts with Vac8p to form nucleus-vacuole junctions.

Discussions

CURATION_TODO (OPEN): Resolve exact source-neutral groundings for the generic vacuolar lipid bilayer and for yeast Vac8p and Nvj1p. GO:0005774 identifies the complete vacuolar membrane and the yeast contact-site literature identifies Vac8p and Nvj1p by protein name, but this pass did not verify exact CHEBI, UniProtKB, or family-level identifiers for those entities.
INTERPRETATION (RESOLVED): Keep vacuolar V-ATPase and Vac8p as functional graph participants rather than asserting them as generic vacuolar membrane components. GO:0005774 denotes the broad lipid bilayer surrounding a vacuole. Vacuolar V-ATPase and Vac8p are localized actors in the cited yeast examples, but this generic membrane record does not yet curate a taxon-agnostic protein cohort for every vacuolar membrane.

Evidence

GO:0005774 Gene Ontology cellular-component term for vacuolar membrane.
GO:0031090 Gene Ontology cellular-component parent term for organelle membrane.
GO:0005773 Gene Ontology cellular-component term for the containing vacuole.
GO:0005775 Gene Ontology cellular-component term for the vacuolar lumen.
GO:0016471 Gene Ontology cellular-component term for the vacuolar proton-transporting V-type ATPase complex.
GO:0007035 Gene Ontology biological-process term for vacuolar acidification.
GO:0005640 Gene Ontology cellular-component term for the nuclear outer membrane contacted by the vacuole at yeast nucleus-vacuole junctions.
DOI:10.1016/j.bbamcr.2008.08.003 Li and Kane 2009, The yeast lysosome-like vacuole: Endpoint and crossroads, Biochimica et Biophysica Acta.
DOI:10.1128/MMBR.70.1.177-191.2006 Kane 2006, The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase, Microbiology and Molecular Biology Reviews.
DOI:10.1091/mbc.11.7.2445 Pan et al. 2000, Nucleus-Vacuole Junctions in Saccharomyces cerevisiae Are Formed Through the Direct Interaction of Vac8p with Nvj1p, Molecular Biology of the Cell.

Curation history

2026-09-15T07:28:12Z codex · CREATED_RECORD — Scaffolded by scripts/new_record.py
2026-09-15T07:29:04Z codex · EXPANDED_RECORD — Added organelle-membrane parentage, vacuole parthood, a reviewed-label-only lipid-bilayer component, Saccharomyces scope, acidification and nucleus-vacuole-junction functions, GO/DOI evidence, a nonmechanistic membrane function graph, and a lipid/protein grounding TODO.
2026-09-15T07:29:38Z codex · TIGHTENED_EVIDENCE — Corrected the vacuolar-acidification directionality and narrowed the Saccharomyces distribution note to claims supported by Li and Kane 2009.
2026-09-15T07:39:25Z codex · REVIEW_FIX — Addressed review issues #947 and #948 by adding a vacuolar-to-nuclear-outer-membrane contact edge and a resolved V-ATPase/Vac8p component-boundary interpretation.

Source: data/structures/membrane_organelle/vacuolar_membrane.yaml