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Trivalent RING Assembly on Retroviral Capsids Activates TRIM5 Ubiquitination and Innate Immune Signaling.

Cell Host Microbe. 2018; 
FletcherAdam J,VaysburdMarina,MaslenSarah,ZengJingwei,SkehelJ Mark,TowersGreg J,JamesL
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Biochemicals G (VSV-G envelope) GenScript N/A CMV-Ampho This group N/A pONY3....G (GenScript) or CMV-Ampho, and 1. Get A Quote

摘要

TRIM5 is a RING domain E3 ubiquitin ligase with potent antiretroviral function. TRIM5 assembles into a hexagonal lattice on retroviral capsids, causing envelopment of the infectious core. Concomitantly, TRIM5 initiates innate immune signaling and orchestrates disassembly of the viral particle, yet how these antiviral responses are regulated by capsid recognition is unclear. We show that hexagonal assembly triggers N-terminal polyubiquitination of TRIM5 that collectively drives antiviral responses. In uninfected cells, N-terminal monoubiquitination triggers non-productive TRIM5 turnover. Upon TRIM5 assembly on virus, a trivalent RING arrangement allows elongation of N-terminally anchored K63-linked ubi... More

关键词

HIV-1,K63-linked Ub,TRIM5,UFD pathway,Ube2N/Ube2V2,Ube2W,innate immunity,restriction factor,reverse transcrip