vpu antagonizes bst-2–mediated restriction of hiv-1 release via β-trcp and endo-lysosomal trafficking通过β-trcp vpu对抗bst-2-mediated限制hiv - 1释放和endo-lysosomal走私.pdfVIP

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vpu antagonizes bst-2–mediated restriction of hiv-1 release via β-trcp and endo-lysosomal trafficking通过β-trcp vpu对抗bst-2-mediated限制hiv - 1释放和endo-lysosomal走私.pdf

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vpu antagonizes bst-2–mediated restriction of hiv-1 release via β-trcp and endo-lysosomal trafficking通过β-trcp vpu对抗bst-2-mediated限制hiv - 1释放和endo-lysosomal走私

Vpu Antagonizes BST-2–Mediated Restriction of HIV-1 Release via b-TrCP and Endo-Lysosomal Trafficking 1 1 1 1 1 2 Richard S. Mitchell , Chris Katsura , Mark A. Skasko , Katie Fitzpatrick , David Lau , Autumn Ruiz , 2 3,4 5 1,6 Edward B. Stephens , Florence Margottin-Goguet , Richard Benarous , John C. Guatelli * 1 Department of Medicine, University of California San Diego, La Jolla, California, United States of America, 2 Department of Anatomy and Cell Biology, University of ´ Kansas Medical Center, Kansas City, Kansas, United States of America, 3 Institut Cochin, Universite Paris Descartes, CNRS (UMR 8104), Paris, France, 4 Inserm, U567, Paris, France, 5 CellVir, Genopole, Evry, France, 6 San Diego Veterans Affairs Healthcare System, San Diego, California, United States of America Abstract The interferon-induced transmembrane protein BST-2/CD317 (tetherin) restricts the release of diverse enveloped viruses from infected cells. The HIV-1 accessory protein Vpu antagonizes this restriction by an unknown mechanism that likely involves the down-regulation of BST-2 from the cell surface. Here, we show that the optimal removal of BST-2 from the plasma membrane by Vpu requires the cellular protein b-TrCP, a substrate adaptor for a multi-subunit SCF E3 ubiquitin ligase complex and a known Vpu-interacting protein. b-TrCP is also required for the optimal enhancement of virion-release by Vpu. Mutations in the DSGxxS b-TrCP binding-mo