A reversible phospho-switch mediated by ULK1 regulates the activity of autophagy protease ATG4B
Upon autophagy induction, LC3 is cleaved by the protease ATG4 and conjugated to the autophagosomal membrane; however, its removal is mediated by the same protease. Here the authors show that ULK1-mediated phosphorylation and PP2A-mediated dephosphorylation of ATG4 regulates its cellular activity to...
Main Authors: | N. Pengo, A. Agrotis, K. Prak, J. Jones, R. Ketteler |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2017-08-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-00303-2 |
Similar Items
-
The regulation of human autophagy by ATG4 proteases
by: Agrotis, Alexander George
Published: (2018) -
ULK1-ATG13 and their mitotic phospho-regulation by CDK1 connect autophagy to cell cycle.
by: Zhiyuan Li, et al.
Published: (2020-06-01) -
On ATG4B as Drug Target for Treatment of Solid Tumours—The Knowns and the Unknowns
by: Alexander Agrotis, et al.
Published: (2019-12-01) -
An ULK1-Independent Mechanism of ATG9A Regulation in Basal Autophagy
by: Kannangara, Ashari Rashmi
Published: (2020) -
Autophagy-Independent Lysosomal Targeting Regulated by ULK1/2-FIP200 and ATG9
by: Jonathan M. Goodwin, et al.
Published: (2017-09-01)