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Gassen, Nils C; Niemeyer, Daniela; Muth, Doreen; Corman, Victor M; Martinelli, Silvia; Gassen, Alwine; Hafner, Kathrin; Papies, Jan; Mösbauer, Kirstin; Zellner, Andreas; Zannas, Anthony S; Herrmann, Alexander; Holsboer, Florian; Brack-Werner, Ruth; Boshart, Michael; Müller-Myhsok, Bertram; Drosten, Christian; Müller, Marcel A; Rein, Theo
Nature communications, 12/2019, Letnik: 10, Številka: 1Journal Article
Autophagy is an essential cellular process affecting virus infections and other diseases and Beclin1 (BECN1) is one of its key regulators. Here, we identified S-phase kinase-associated protein 2 (SKP2) as E3 ligase that executes lysine-48-linked poly-ubiquitination of BECN1, thus promoting its proteasomal degradation. SKP2 activity is regulated by phosphorylation in a hetero-complex involving FKBP51, PHLPP, AKT1, and BECN1. Genetic or pharmacological inhibition of SKP2 decreases BECN1 ubiquitination, decreases BECN1 degradation and enhances autophagic flux. Middle East respiratory syndrome coronavirus (MERS-CoV) multiplication results in reduced BECN1 levels and blocks the fusion of autophagosomes and lysosomes. Inhibitors of SKP2 not only enhance autophagy but also reduce the replication of MERS-CoV up to 28,000-fold. The SKP2-BECN1 link constitutes a promising target for host-directed antiviral drugs and possibly other autophagy-sensitive conditions.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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