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Article

VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase.

The Journal of biological chemistry - 30 Dec 2005

Gerega Alexandra, Rockel Beate, Peters Jürgen, Tamura Tomohiro, Baumeister Wolfgang, Zwickl Peter

Abstract excerpt

The Thermoplasma VCP-like ATPase from Thermoplasma acidophilum (VAT) ATPase is a member of the two-domain AAA ATPases and homologous to the mammalian p97/VCP and NSF proteins. We show here that the VAT ATPase complex unfolds green fluorescent protein (GFP) labeled with the ssrA-degradation tag. Increasing the Mg2+ concentration derepresses the ATPase activity and concomitantly stimulates the unfolding activity of...

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Source

Identifiers

PMID: 16236712
DOI: 10.1074/jbc.M510592200

Genes

VCP
NSF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase.PMID 16236712Read ↗

Mutations in p97/VCP induce unfolding activity.Semantic proximity Read ↗

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Allosteric activation of VCP, a AAA unfoldase, by small molecule mimicrySemantic proximity Read ↗

ATPase activity of p97/valosin-containing protein is regulated by oxidative modification of the evolutionally conserved cysteine 522 residue in Walker A motif.Semantic proximity Read ↗

Characterization of the aggregation-prevention activity of p97/valosin-containing protein.Semantic proximity Read ↗

VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase.Semantic proximity Read ↗

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