| http://purl.uniprot.org/citations/12663786 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12663786 | http://www.w3.org/2000/01/rdf-schema#comment | "Retroviral late-budding (L) domains are required for the efficient release of nascent virions. The three known types of L domain, designated according to essential tetrapeptide motifs (PTAP, PPXY, or YPDL), each bind distinct cellular cofactors. We and others have demonstrated that recruitment of an ESCRT-I subunit, Tsg101, a component of the class E vacuolar protein sorting (VPS) machinery, is required for the budding of viruses, such as human immunodeficiency virus type 1 (HIV-1) and Ebola virus, that encode a PTAP-type L domain, but subsequent events remain undefined. In this study, we demonstrate that VPS28, a second component of ESCRT-I, binds to a sequence close to the Tsg101 C terminus and is therefore recruited to the plasma membrane by HIV-1 Gag. In addition, we show that Tsg101 exhibits a multimerization activity. Using a complementation assay in which Tsg101 is artificially recruited to sites of HIV-1 assembly, we demonstrate that the integrity of the VPS28 binding site within Tsg101 is required for particle budding. In addition, mutation of a putative leucine zipper or residues important for Tsg101 multimerization also impairs the ability of Tsg101 to support HIV-1 budding. A minimal multimerizing Tsg101 domain is a dominant negative inhibitor of PTAP-mediated HIV-1 budding but does not inhibit YPDL-type or PPXY-type L-domain function. Nevertheless, YDPL-type L-domain activity is inhibited by expression of a catalytically inactive mutant of the class E VPS ATPase VPS4. These results indicate that all three classes of retroviral L domains require a functioning class E VPS pathway in order to effect budding. However, the PTAP-type L domain appears to be unique in its requirement for an intact, or nearly intact, ESCRT-I complex."xsd:string |
| http://purl.uniprot.org/citations/12663786 | http://purl.org/dc/terms/identifier | "doi:10.1128/jvi.77.8.4794-4804.2003"xsd:string |
| http://purl.uniprot.org/citations/12663786 | http://purl.uniprot.org/core/author | "Bieniasz P.D."xsd:string |
| http://purl.uniprot.org/citations/12663786 | http://purl.uniprot.org/core/author | "Martin-Serrano J."xsd:string |
| http://purl.uniprot.org/citations/12663786 | http://purl.uniprot.org/core/author | "Zang T."xsd:string |
| http://purl.uniprot.org/citations/12663786 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12663786 | http://purl.uniprot.org/core/name | "J Virol"xsd:string |
| http://purl.uniprot.org/citations/12663786 | http://purl.uniprot.org/core/pages | "4794-4804"xsd:string |
| http://purl.uniprot.org/citations/12663786 | http://purl.uniprot.org/core/title | "Role of ESCRT-I in retroviral budding."xsd:string |
| http://purl.uniprot.org/citations/12663786 | http://purl.uniprot.org/core/volume | "77"xsd:string |
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