Involvement of the betaTrCP in the ubiquitination and stability of the HIV-1 Vpu protein

The human immunodeficiency virus type 1 (HIV-1) Vpu protein binds to the CD4 receptor and targets it to the proteasome for degradation. This process requires the recruitment of human betaTrCP, a component of the Skp1-Cullin-F box (SCF) ubiquitin ligase complex, that interacts with phosphorylated Vpu...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-06, Vol.357 (3), p.688-693
Main Authors: Belaïdouni, Nadia, Marchal, Christelle, Benarous, Richard, Besnard-Guérin, Corinne
Format: Article
Language:English
Subjects:
beta-Transducin Repeat-Containing Proteins - genetics
beta-Transducin Repeat-Containing Proteins - metabolism
Blotting, Western
Cell Line
Cysteine Proteinase Inhibitors - pharmacology
HeLa Cells
Human Immunodeficiency Virus Proteins
Humans
Leupeptins - pharmacology
Mutation
Phosphorylation
Proteasome Endopeptidase Complex - metabolism
Proteasome Inhibitors
Transfection
Ubiquitin - metabolism
Viral Regulatory and Accessory Proteins - genetics
Viral Regulatory and Accessory Proteins - metabolism
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The human immunodeficiency virus type 1 (HIV-1) Vpu protein binds to the CD4 receptor and targets it to the proteasome for degradation. This process requires the recruitment of human betaTrCP, a component of the Skp1-Cullin-F box (SCF) ubiquitin ligase complex, that interacts with phosphorylated Vpu molecules. Vpu, unlike other ligands of betaTrCP, has never been reported to be degraded. We provide evidence that Vpu, itself, is ubiquitinated and targeted for degradation by the proteasome. We demonstrate that the mutant Vpu2.6, which cannot interact with betaTrCP, is stable and, unlike wild-type Vpu, is not polyubiquitinated. These results suggest that betaTrCP is involved in Vpu polyubiquitination.
ISSN:0006-291X