Title : Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding.

Pub. Date : 2004 May 1

PMID : 15126635






6 Functional Relationships(s)
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Protein Name
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1 Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. Glycosaminoglycans NEDD4 E3 ubiquitin protein ligase Homo sapiens
2 The Gag proteins of oncoretroviruses possess a PPxY motif that recruits a ubiquitin ligase from the Nedd4 family, whereas those of the human immunodeficiency virus interact through a PTAP motif with Tsg101, a protein of the ESCRT-1 complex. Glycosaminoglycans NEDD4 E3 ubiquitin protein ligase Homo sapiens
3 We show that Nedd4.1, but not Nedd4.2, is recruited by the PPPY motif of Gag and subsequently catalyzes Gag ubiquitination. Glycosaminoglycans NEDD4 E3 ubiquitin protein ligase Homo sapiens
4 We show that Nedd4.1, but not Nedd4.2, is recruited by the PPPY motif of Gag and subsequently catalyzes Gag ubiquitination. Glycosaminoglycans NEDD4 E3 ubiquitin protein ligase Homo sapiens
5 We also demonstrate that Gag interacts first with Nedd4.1 at the plasma membrane and then with Tsg101 in late endosomes/MVBs. Glycosaminoglycans NEDD4 E3 ubiquitin protein ligase Homo sapiens
6 Our findings indicate that Nedd4.1 and Tsg101 act successively in the assembly process of HTLV-1 to ensure proper Gag trafficking through the endocytic pathway up to late endosomes where the late steps of retroviral release occur. Glycosaminoglycans NEDD4 E3 ubiquitin protein ligase Homo sapiens