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Title 

The deubiquitinating enzyme USP20 stabilizes ULK1 and promotes autophagy initiation

Authors 

J H KimD SeoS J KimD W ChoiJ S ParkJ HaJ ChoiJ H LeeS M JungK W SeoEun Woo LeeY S LeeH CheongC Y ChoiS H Park

Publisher 

EMBO Press

Issue Date 

2018

Citation 

EMBO Reports

Keywords 

autophagydeubiquitinaselysosomal degradationULK1USP20

Abstract 

Autophagy begins with the formation of autophagosomes, a process that depends on the activity of the serine/threonine kinase ULK1 (hATG1). Although earlier studies indicated that ULK1 activity is regulated by dynamic polyubiquitination, the deubiquitinase involved in the regulation of ULK1 remained unknown. In this study, we demonstrate that ubiquitin-specific protease 20 (USP20) acts as a positive regulator of autophagy initiation through stabilizing ULK1. At basal state, USP20 binds to and stabilizes ULK1 by removing the ubiquitin moiety, thereby interfering with the lysosomal degradation of ULK1. The stabilization of basal ULK1 protein levels is required for the initiation of starvation-induced autophagy, since the depletion of USP20 by RNA interference inhibits LC3 puncta formation, a marker of autophagic flux. At later stages of autophagy, USP20 dissociates from ULK1, resulting in enhanced ULK1 degradation and apoptosis. Taken together, our findings provide the first evidence that USP20 plays a crucial role in autophagy initiation by maintaining the basal expression level of ULK1

ISSN 

1469-221X

Link 

http://dx.doi.org/10.15252/embr.201744378

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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