Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1938456 | Biochemical and Biophysical Research Communications | 2007 | 6 Pages |
Abstract
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 βTrCP, a component of the Skp1-Cullin-F box (SCF) ubiquitin ligase complex, that interacts with phosphorylated Vpu molecules. Vpu, unlike other ligands of βTrCP, 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 βTrCP, is stable and, unlike wild-type Vpu, is not polyubiquitinated. These results suggest that βTrCP is involved in Vpu polyubiquitination.
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Authors
Nadia Belaïdouni, Christelle Marchal, Richard Benarous, Corinne Besnard-Guérin,