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Article

Assembly with the Cul4A-DDB1DCAF1 ubiquitin ligase protects HIV-1 Vpr from proteasomal degradation.

The Journal of biological chemistry - 1 Aug 2008

Le Rouzic Erwann, Morel Marina, Ayinde Diana, Belaïdouni Nadia, Letienne Justine, Transy Catherine, Margottin-Goguet Florence

Abstract excerpt

Many viruses subvert the host ubiquitin-proteasome system to optimize their life cycle. We recently documented such a mechanism for the human immunodeficiency virus type 1 Vpr protein, which promotes cell cycle arrest by recruiting the DCAF1 adaptor of the Cul4A-DDB1 ubiquitin ligase, a finding now confirmed by several groups. Here we examined the impact of Cul4A-DDB1(DCAF1) on Vpr stability. We show that the...

Read the complete abstract on PubMed

Topics

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Share to Cell Cycle
Share to Cullin Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to G2 Phase

Share to Gene Silencing

Share to Proteasome Endopeptidase Complex

Share to RNA, Small Interfering

Share to Virus Replication

Share to vpr Gene Products, Human Immunodeficiency Virus

Source

Identifiers

PMID: 18524771
DOI: 10.1074/jbc.M710298200

Genes

DCAF1
DDB1

Variants

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.

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Assembly with the Cul4A-DDB1DCAF1 ubiquitin ligase protects HIV-1 Vpr from proteasomal degradation.PMID 18524771Read ↗

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