The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway
Open accessAbstract
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.
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Cites
Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
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Self-citationEffect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
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Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55 Gag
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Ubiquitin is part of the retrovirus budding machinery
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Role of ESCRT-I in Retroviral Budding
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Self-citationPuffer, B. A., Parent, L. J., Wills, J. W., & Montelaro, R. C. (1997) · Journal of Virology · doi:10.1128/jvi.71.9.6541-6546.1997 · Cited by 217
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Cited by
Vietri, M., Radulovic, M., & Stenmark, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0177-4 · Cited by 962
Virus budding and the ESCRT pathway
Votteler, J., & Sundquist, W. I. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.08.012 · Cited by 547
The HECT Family of E3 Ubiquitin Ligases: Multiple Players in Cancer Development
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Davison, A. J. (2010) · Veterinary Microbiology · doi:10.1016/j.vetmic.2010.02.014 · Cited by 359
Plasma Membrane Is the Site of Productive HIV-1 Particle Assembly
Jouvenet, N., Neil, S. J. D., Bess, C., Johnson, M. C., Virgen, C. A., Simon, S. M., & Bieniasz, P. D. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040435 · Cited by 357
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Metadata
- Authors
- Martin-Serrano, J., Eastman, S. W., Chung, W., & Bieniasz, P. D.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2004-12-28
- Volume
- 168
- Issue
- 1
- Pages
- 89-101
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2042966315
- Cited by
- 202
- References
- 9
- FWCI
- 5.10
- Type
- journal article
- Language
- en
- Open access
- green
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- Martin-Serrano, J., Eastman, S. W., Chung, W., & Bieniasz, P. D. (2005). HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200408155
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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