Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation.

ABSTRACT: The ULK complex initiates the autophagosome formation, and has recently been implicated in selective autophagy by interacting with autophagy receptors through its FIP200 subunit. However, the structural mechanism underlying the interactions of autophagy receptors with FIP200 and the relevant regulatory mechanism remain elusive. Here, we discover that the interactions of FIP200 Claw domain with autophagy receptors CCPG1 and Optineurin can be regulated by the phosphorylation in their respective FIP200-binding regions. We determine the crystal structures of FIP200 Claw in complex with the phosphorylated CCPG1 and Optineurin, and elucidate the detailed molecular mechanism governing the interactions of FIP200 Claw with CCPG1 and Optineurin as well as their potential regulations by kinase-mediat

SUBMITTER: Zhou Z 

PROVIDER: S-EPMC7946963 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature