The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
The Human Endosomal Sorting Complex Required for Transport (ESCRT-I) and Its Role in HIV-1 Budding
Open accessAbstract
Efficient human immunodeficiency virus type 1 (HIV-1) budding requires an interaction between the PTAP late domain in the viral p6(Gag) protein and the cellular protein TSG101. In yeast, Vps23p/TSG101 binds both Vps28p and Vps37p to form the soluble ESCRT-I complex, which functions in sorting ubiquitylated protein cargoes into multivesicular bodies. Human cells also contain ESCRT-I, but the VPS37 component(s) have not been identified. Bioinformatics and yeast two-hybrid screening methods were therefore used to identify four novel human proteins (VPS37A-D) that share weak but significant sequence similarity with yeast Vps37p and to demonstrate that VPS37A and VPS37B bind TSG101. Detailed studies produced four lines of evidence that human VPS37B is a Vps37p ortholog. 1) TSG101 bound to several different sites on VPS37B, including a putative coiled-coil region and a PTAP motif. 2) TSG101 and VPS28 co-immunoprecipitated with VPS37B-FLAG, and the three proteins comigrated together in soluble complexes of the correct size for human ESCRT-I ( approximately 350 kDa). 3) Like TGS101, VPS37B became trapped on aberrant endosomal compartments in the presence of VPS4A proteins lacking ATPase activity. 4) Finally, VPS37B could recruit TSG101/ESCRT-I activity and thereby rescue the budding of both mutant Gag particles and HIV-1 viruses lacking native late domains. Further studies of ESCRT-I revealed that TSG101 mutations that inhibited PTAP or VPS28 binding blocked HIV-1 budding. Taken together, these experiments define new components of the human ESCRT-I complex and characterize several TSG101 protein/protein interactions required for HIV-1 budding and infectivity.
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Cites
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Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
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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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Proteolytic refolding of the HIV‐1 capsid protein amino‐terminus facilitates viral core assembly
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Role of ESCRT-I in Retroviral Budding
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Cited by
The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
Raiborg, C., & Stenmark, H. (2009) · Nature · doi:10.1038/nature07961 · Cited by 1,359
Localizing Recent Adaptive Evolution in the Human Genome.
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Theos, A. C., Truschel, S. T., Tenza, D., Hurbain, I., Harper, D. C., Berson, J. F., Thomas, P. C., Raposo, G., & Marks, M. S. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.01.012 · Cited by 263
Teo, H., Gill, D. J., Sun, J., Perisic, O., Veprintsev, D. B., Vallis, Y., Emr, S. D., & Williams, R. L. (2006) · Cell · doi:10.1016/j.cell.2006.01.047 · Cited by 242
Endosomal and non-endosomal functions of ESCRT proteins
Slagsvold, T., Pattni, K., Malerød, L., & Stenmark, H. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.04.004 · Cited by 238
Metadata
- Authors
- Stuchell, M. D., Garrus, J. E., Müller, B., Stray, K. M., Ghaffarian, S., McKinnon, R., Kräusslich, H.-G., Morham, S. G., & Sundquist, W. I.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-08
- Volume
- 279
- Issue
- 34
- Pages
- 36059-36071
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2032660967
- Cited by
- 173
- References
- 10
- FWCI
- 6.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Stuchell, M. D., Garrus, J. E., Müller, B., Stray, K. M., Ghaffarian, S., McKinnon, R., Kräusslich, H.-G., Morham, S. G., & Sundquist, W. I. (2004). The Human Endosomal Sorting Complex Required for Transport (ESCRT-I) and Its Role in HIV-1 Budding. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m405226200
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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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