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Papers In Press, published online ahead of print October 14, 2003
Des maladies infectieuses, Unity 567 INSERM, Cochin Institute, Paris 75014
Corresponding Author: benarous{at}cochin.inserm.fr
The human immunodeficiency virus type 1 (HIV-1) Vpu protein acts as an adaptor for the proteasomal degradation of CD4 by recruiting CD4 and bTrCP, the receptor component of the multi subunit SCF-bTrCP E3 ubiquitin ligase complex. We showed that the expres sion of a Vpu-GFP fusion protein prevented the proteosomal degradation of bTrCP substrates such as b-catenin, IKBa and ATF4, which are normally directly targeted to the proteasome for degradation. b-catenin was translocated into the nucleus, whereas the TNF-induced nuclear translocation of NFKB was impaired. b-catenin was also upregulated in cells producing Vpu+ HIV-1 but not in cells producing Vpu-deficient viruses. The overexpression of ATF4 also provoked accumulation of b-catenin, but to a lower level than that resulting from the expression of Vpu. Finally, the expression of Vpu induces the exclusion of bTrCP from the nucleus. These data suggest that Vpu is a strong competitive inhibitor of bTrCP that impairs the degradation of SCFbTrCPsubstrates as l ong as Vpu has an intact phosphorylation motif and can bind to bTrCP. wt
J. Biol. Chem, 10.1074/jbc.M308068200
Submitted on July 24, 2003
Revised on October 1, 2003
Accepted on October 14, 2003
HIV-1 Vpu sequesters bTrCP in the cytoplasm and provokes the accumulation of b-catenin and others SCF-bTrCP substrates
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