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Schott, Kerstin; Fuchs, Nina V.; Derua, Rita; Mahboubi, Bijan; Schnellbächer, Esther; Seifried, Janna; Tondera, Christiane; Schmitz, Heike; Shepard, Caitlin; Brandariz-Nuñez, Alberto; Diaz-Griffero, Felipe; Reuter, Andreas; Kim, Baek; Janssens, Veerle; König, Renate

Dephosphorylation of the HIV-1 restriction factor SAMHD1 is mediated by PP2A-B55α holoenzymes during mitotic exit

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  • Medientyp: E-Artikel
  • Titel: Dephosphorylation of the HIV-1 restriction factor SAMHD1 is mediated by PP2A-B55α holoenzymes during mitotic exit
  • Beteiligte: Schott, Kerstin; Fuchs, Nina V.; Derua, Rita; Mahboubi, Bijan; Schnellbächer, Esther; Seifried, Janna; Tondera, Christiane; Schmitz, Heike; Shepard, Caitlin; Brandariz-Nuñez, Alberto; Diaz-Griffero, Felipe; Reuter, Andreas; Kim, Baek; Janssens, Veerle; König, Renate
  • Erschienen: Springer Science and Business Media LLC, 2018
  • Erschienen in: Nature Communications
  • Sprache: Englisch
  • DOI: 10.1038/s41467-018-04671-1
  • ISSN: 2041-1723
  • Schlagwörter: General Physics and Astronomy ; General Biochemistry, Genetics and Molecular Biology ; General Chemistry ; Multidisciplinary
  • Entstehung:
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  • Beschreibung: <jats:title>Abstract</jats:title><jats:p>SAMHD1 is a critical restriction factor for HIV-1 in non-cycling cells and its antiviral activity is regulated by T592 phosphorylation. Here, we show that SAMHD1 dephosphorylation at T592 is controlled during the cell cycle, occurring during M/G<jats:sub>1</jats:sub> transition in proliferating cells. Using several complementary proteomics and biochemical approaches, we identify the phosphatase PP2A-B55α responsible for rendering SAMHD1 antivirally active. SAMHD1 is specifically targeted by PP2A-B55α holoenzymes during mitotic exit, in line with observations that PP2A-B55α is a key mitotic exit phosphatase in mammalian cells. Strikingly, as HeLa or activated primary CD4<jats:sup>+</jats:sup> T cells enter the G<jats:sub>1</jats:sub> phase, pronounced reduction of RT products is observed upon HIV-1 infection dependent on the presence of dephosphorylated SAMHD1. Moreover, PP2A controls SAMHD1 pT592 level in non-cycling monocyte-derived macrophages (MDMs). Thus, the PP2A-B55α holoenzyme is a key regulator to switch on the antiviral activity of SAMHD1.</jats:p>
  • Zugangsstatus: Freier Zugang