Regular ArticleAnalysis of Apoptosis Induced by HIV-1 Vpr and Examination of the Possible Role of the hHR23A Protein
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HIV-1 Vpr hijacks EDD-DYRK2-DDB1<sup>DCAF1</sup> to disrupt centrosome homeostasis
2018, Journal of Biological ChemistryCitation Excerpt :Coincidentally, CP110 has been documented to undergo ubiquitination by SCFcyclin F and EDD-DYRK2-DDB1DCAF1 (37, 52), and subsequently proteasomal degradation, in G2/M. Thus, we sought to address whether down-regulation of CP110 induced by Vpr is due to prolonged G2/M arrest. For this purpose, we utilized a well-characterized Vpr mutant, Vpr(R80A), which, in contrast to Vpr(Q65R), can bind to DCAF1 but is unable to provoke G2/M arrest (Ref. 54, 55 and Fig. 6A). Similar to WT Vpr, Vpr(R80A) was detected at the centrosome in ∼20–25% of the transfected cells (Fig. 6, B and C).
HHR23A is required to control the basal turnover of Chk1
2015, Cellular SignallingCitation Excerpt :Studies in yeast have revealed that they are likely to modulate cell cycle progression by promoting the proteasome-mediated degradation of regulatory proteins [31–33]. Human HR23A proteins have been shown to help control the stability and transcriptional activity of p53 [26,34,35], and functional studies of the Vpr protein in HIV have indicated that Vpr expression mimics DNA damage and causes cells to arrest at the G2/M phase via a direct interaction with hHR23A [36,37]. In the present study, we provide a novel mechanism by which HR23A controls the stability of Chk1.
HIV-1 Vpr: Mechanisms of G<inf>2</inf> arrest and apoptosis
2008, Experimental and Molecular PathologyInteractions of HIV-1 proteins as targets for developing anti-HIV-1 peptides
2015, Future Medicinal Chemistry
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