Lentivirus Vpr and Vpx accessory proteins usurp the cullin4-DDB1 (DCAF1) E3 ubiquitin ligase.

@article{Romani2012LentivirusVA,
  title={Lentivirus Vpr and Vpx accessory proteins usurp the cullin4-DDB1 (DCAF1) E3 ubiquitin ligase.},
  author={Bizhan Romani and {\'E}ric A Cohen},
  journal={Current opinion in virology},
  year={2012},
  volume={2 6},
  pages={755-63}
}
Myeloid cells display a differential permissivity to primate lentivirus infection that is related to their ability to encode the Vpx and to a lesser extent the Vpr accessory proteins. Vpr is encoded by all primate lentiviruses, including HIV-1 and HIV-2, while its paralog, Vpx, is unique to HIV-2 and a subset of simian lentiviruses. Both proteins usurp the CRL4A (DCAF1) E3 ligase to fulfil their functions. Vpx induces the degradation of SAMHD1, a nucleotide triphosphohydrolase that blocks… CONTINUE READING

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Lentiviral Vpr usurps CUL 4 – DDB 1 [ VprBP ] E 3 ubiquitin ligase to Current Opinion in

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