Serine Phosphorylation of HIV-1 Vpu and Its Binding to Tetherin Regulates Interaction with Clathrin Adaptors.

Serine Phosphorylation of HIV-1 Vpu and Its Binding to Tetherin Regulates Interaction with Clathrin Adaptors.

HIV-1 Vpu prevents incorporation of tetherin (BST2/ CD317) into budding virions and targets it for ESCRT-dependent endosomal degradation via a clathrin-dependent process. This requires a variant acidic dileucine-sorting motif (ExxxLV) in Vpu. Structural studies demonstrate that recombinant Vpu/tethe...

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Bibliographic Details
Main Authors: Tonya Kueck, Toshana L Foster, Julia Weinelt, Jonathan C Sumner, Suzanne Pickering, Stuart J D Neil
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-08-01
Series:PLoS Pathogens
Online Access:http://europepmc.org/articles/PMC4552633?pdf=render

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http://europepmc.org/articles/PMC4552633?pdf=render

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