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10.1038/s41467-019-13659-4

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suck abstract from ncbi


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pmid31852899      Nat+Commun 2019 ; 10 (1): 5770
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  • SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection #MMPMID31852899
  • Gassen NC; Niemeyer D; Muth D; Corman VM; Martinelli S; Gassen A; Hafner K; Papies J; Mosbauer K; Zellner A; Zannas AS; Herrmann A; Holsboer F; Brack-Werner R; Boshart M; Muller-Myhsok B; Drosten C; Muller MA; Rein T
  • Nat Commun 2019[Dec]; 10 (1): 5770 PMID31852899show ga
  • 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.
  • |Animals[MESH]
  • |Autophagy/drug effects/*immunology[MESH]
  • |Beclin-1/*metabolism[MESH]
  • |Chlorocebus aethiops[MESH]
  • |Coronavirus Infections/*immunology/virology[MESH]
  • |Gene Knockdown Techniques[MESH]
  • |HEK293 Cells[MESH]
  • |Humans[MESH]
  • |Middle East Respiratory Syndrome Coronavirus/*immunology/pathogenicity[MESH]
  • |Proteolysis/drug effects[MESH]
  • |S-Phase Kinase-Associated Proteins/antagonists & inhibitors/genetics/*metabolism[MESH]
  • |Ubiquitination/drug effects/immunology[MESH]


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