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- W3105758061 abstract "Abstract HIV-1 encodes four ‘accessory proteins’ (Vif, Vpr, Vpu and Nef), dispensable for viral replication in vitro, but essential for viral pathogenesis in vivo. Well characterised cellular targets have been associated with Vif, Vpu and Nef, which counteract host restriction and promote viral replication. Conversely, whilst several substrates of Vpr have been described, their biological significance remains unclear. Here, we use complementary, unbiased mass spectrometry-based approaches to demonstrate that Vpr is both necessary and sufficient for DCAF1/DDB1/CUL4 E3 ubiquitin ligase-mediated degradation of at least 38 cellular proteins, causing systems-level changes to the cellular proteome. We therefore propose that promiscuous targeting of multiple host factors underpins complex Vpr-dependent cellular phenotypes, and validate this in the case of G2/M cell cycle arrest. Our model explains how Vpr modulates so many cell biological processes, and why the functional consequences of previously described Vpr targets, identified and studied in isolation, have proved elusive." @default.
- W3105758061 created "2020-11-23" @default.
- W3105758061 creator A5001166242 @default.
- W3105758061 creator A5010792984 @default.
- W3105758061 creator A5056182587 @default.
- W3105758061 creator A5073204352 @default.
- W3105758061 creator A5075336505 @default.
- W3105758061 creator A5078092601 @default.
- W3105758061 date "2018-07-23" @default.
- W3105758061 modified "2023-10-18" @default.
- W3105758061 title "Promiscuous targeting of cellular proteins by Vpr drives massive proteomic remodelling in HIV-1 infection" @default.
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