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Published online 28 December 2004. doi:10.1083/jcb.200408155
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 1, 89-101
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Article

HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway



Juan Martin-Serrano, Scott W. Eastman, Wayne Chung, and Paul D. Bieniasz

Aaron Diamond AIDS Research Center and The Rockefeller University, New York, NY 10021

Correspondence to Paul D. Bieniasz: pbienias{at}adarc.org

Many enveloped viruses exploit the class E vacuolar protein-sorting (VPS) pathway to bud from cells, and use peptide motifs to recruit specific class E VPS factors. Homologous to E6AP COOH terminus (HECT) ubiquitin ligases have been implicated as cofactors for PPXY motif–dependent budding, but precisely which members of this family are responsible, and how they access the VPS pathway is unclear. Here, we show that PPXY-dependent viral budding is unusually sensitive to inhibitory fragments derived from specific HECT ubiquitin ligases, namely WWP1 and WWP2. We also show that WWP1, WWP2, or Itch ubiquitin ligase recruitment promotes PPXY-dependent virion release, and that this function requires that the HECT ubiquitin ligase domain be catalytically active. Finally, we show that several mammalian HECT ubiquitin ligases, including WWP1, WWP2, and Itch are recruited to class E compartments induced by dominant negative forms of the class E VPS ATPase, VPS4. These data indicate that specific HECT ubiquitin ligases can link PPXY motifs to the VPS pathway to induce viral budding.

J. Martin-Serrano's current address is Dept. of Infectious Diseases, Guy's, King's and St. Thomas' School of Medicine, King's College London, UK.

Abbreviations used in this paper: EbVP40, Ebola virus VP40; ENaC, epithelial Na+ channel; ESCRT, endosomal sorting complex required for transport; HECT, homologous to E6AP COOH terminus; MLV, murine leukemia virus; MVB, multivesicular body; RSV, Rous sarcoma virus; VPS, vacuolar protein-sorting.


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