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Structural insights into Cullin4-RING ubiquitin ligase remodelling by Vpr from simian immunodeficiency viruses

ABSTRACT: crosslinking mass spectrometry results for sulfo-SDA crosslinking of human CUL4-NEDD8/ROC1/DDB1/DCAF1-CtD in complex with SAMHD1 and Vpr protein from simian immunodeficiency virus infecting Cercopithecus cephus (SIVmus Vpr)

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Andrea Graziadei

LAB HEAD: Juri Rappsilber

PROVIDER: PXD020453 | Pride | 2021-07-20

REPOSITORIES: Pride

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Structural insights into Cullin4-RING ubiquitin ligase remodelling by Vpr from simian immunodeficiency viruses.

Banchenko Sofia S Krupp Ferdinand F Gotthold Christine C Bürger Jörg J Graziadei Andrea A O'Reilly Francis J FJ Sinn Ludwig L Ruda Olga O Rappsilber Juri J Spahn Christian M T CMT Mielke Thorsten T Taylor Ian A IA Schwefel David D

PLoS pathogens 20210802 8

Viruses have evolved means to manipulate the host's ubiquitin-proteasome system, in order to down-regulate antiviral host factors. The Vpx/Vpr family of lentiviral accessory proteins usurp the substrate receptor DCAF1 of host Cullin4-RING ligases (CRL4), a family of modular ubiquitin ligases involved in DNA replication, DNA repair and cell cycle regulation. CRL4DCAF1 specificity modulation by Vpx and Vpr from certain simian immunodeficiency viruses (SIV) leads to recruitment, poly-ubiquitylation ...[more]

PMID: 34339457

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