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Article

Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations.

Nature cell biology - 7 Aug 2011

Ritz Danilo, Vuk Maja, Kirchner Philipp, Bug Monika, Schütz Sabina, Hayer Arnold, Bremer Sebastian, Lusk Caleb, Baloh Robert H, Lee Houkeun, Glatter Timo, Gstaiger Matthias, Aebersold Ruedi, Weihl Conrad C, Meyer Hemmo

Abstract excerpt

The AAA-ATPase VCP (also known as p97) cooperates with distinct cofactors to process ubiquitylated proteins in different cellular pathways. VCP missense mutations cause a systemic degenerative disease in humans, but the molecular pathogenesis is unclear. We used an unbiased mass spectrometry approach and identified a VCP complex with the UBXD1 cofactor, which binds to the plasma membrane protein caveolin-1 (CAV1)...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 21822278
DOI: 10.1038/ncb2301
PMCID: PMC3246400

Genes

VCP
CAV1
SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations.PMID 21822278Read ↗

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