SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection
Here, Gassen et al. show that S-phase kinase-associated protein 2 (SKP2) is responsible for lysine-48-linked poly-ubiquitination of beclin 1, resulting in its proteasomal degradation, and that inhibition of SKP2 enhances autophagy and reduces replication of MERS coronavirus.
Guardado en:
Autores principales: | Nils C. Gassen, Daniela Niemeyer, Doreen Muth, Victor M. Corman, Silvia Martinelli, Alwine Gassen, Kathrin Hafner, Jan Papies, Kirstin Mösbauer, Andreas Zellner, Anthony S. Zannas, Alexander Herrmann, Florian Holsboer, Ruth Brack-Werner, Michael Boshart, Bertram Müller-Myhsok, Christian Drosten, Marcel A. Müller, Theo Rein |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/173953915c6a47688637a8c938baf515 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Functional comparison of MERS-coronavirus lineages reveals increased replicative fitness of the recombinant lineage 5
por: Simon Schroeder, et al.
Publicado: (2021) -
Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.
por: Zhi-Xin Lyu, et al.
Publicado: (2012) -
6mer seed toxicity in tumor suppressive microRNAs
por: Quan Q. Gao, et al.
Publicado: (2018) -
14-3-3Tau regulates Beclin 1 and is required for autophagy.
por: Bing Wang, et al.
Publicado: (2010) -
The NUCKS1-SKP2-p21/p27 axis controls S phase entry
por: Samuel Hume, et al.
Publicado: (2021)