The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Ubiquitin is part of the retrovirus budding machinery
Open accessAbstract
Retroviruses contain relatively large amounts of ubiquitin, but the significance of this finding has been unknown. Here, we show that drugs that are known to reduce the level of free ubiquitin in the cell dramatically reduced the release of Rous sarcoma virus, an avian retrovirus. This effect was suppressed by overexpressing ubiquitin and also by directly fusing ubiquitin to the C terminus of Gag, the viral protein that directs budding and particle release. The block to budding was found to be at the plasma membrane, and electron microscopy revealed that the reduced level of ubiquitin results in a failure of mature virus particles to separate from each other and from the plasma membrane during budding. These data indicate that ubiquitin is actually part of the budding machinery.
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In the citing paper
“HIV Gag and other retroviruses are modified with ubiquitin in their p6 domains, and a C-terminal ubiquitin-Gag fusion construct mimicking a true p6 domain modification, can stimulate and rescue defective virus release [22,23].”
From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [22]
In the citing paper
“ubiquitination of Gag is a common feature among retroviruses, intricately associated with retroviral budding/release”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Patnaik et al. 2000
Citations
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Cited by
Sorted by citations
Signals for Sorting of Transmembrane Proteins to Endosomes and Lysosomes
Bonifacino, J. S., & Traub, L. M. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161800 · Cited by 2,040
Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00506-2 · Cited by 1,369
Protein regulation by monoubiquitin
Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,227
Martin-Serrano, J., Zang, T., & Bieniasz, P. D. (2001) · Nature Medicine · doi:10.1038/nm1201-1313 · Cited by 710
Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55 Gag
VerPlank, L., Bouamr, F., LaGrassa, T. J., Agresta, B., Kikonyogo, A., Leis, J., & Carter, C. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.131059198 · Cited by 584
Metadata
- Authors
- Patnaik, A., Chau, V., & Wills, J. W.
- Affiliations
- Pennsylvania State University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2000-11-21
- Volume
- 97
- Issue
- 24
- Pages
- 13069-13074
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC27179
- OpenAlex
- W2060316418
- Cited by
- 292
- References
- 46
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 7 · 2021: 5 · 2020: 6 · 2019: 7 · 2018: 7 · 2017: 6 · 2016: 4 · 2015: 7 · 2014: 9 · 2013: 8 · 2012: 6
- FWCI
- 11.58
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (R01CA047482, CA-47482, R37CA047482)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Keywords
- ubiquitin, Rous sarcoma virus, Gag protein, viral particle release, plasma membrane, viral assembly, avian retroviruses
- MeSH terms
- Acetylcysteine, Animals, Avian Sarcoma Viruses, Cell Line, Cell Membrane, Cysteine Endopeptidases, Endocytosis, Leupeptins, Multienzyme Complexes, Oligopeptides, Protease Inhibitors, Quail, Recombinant Fusion Proteins, Ubiquitins, Virus Replication, Gene Products, gag, Proteasome Endopeptidase Complex
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