PDBsum entry 7d0e

Signaling protein/protein binding

PDB id: 7d0e

Contents

Protein chains

96 a.a.

11 a.a.

Ligands

GO9

PEG

Waters ×95

PDB id:

7d0e

Name:

Signaling protein/protein binding

Title:

Crystal structure of fip200 claw/p-ccpg1 fir2

Structure:

Rb1-inducible coiled-coil protein 1. Chain: a. Synonym: fak family kinase-interacting protein of 200 kda,fip200. Engineered: yes. Cell cycle progression protein 1 fir2. Chain: b. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: rb1cc1, kiaa0203, rbicc. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ccpg1. Expression_system_taxid: 562

Resolution:

1.40Å R-factor: 0.187 R-free: 0.207

Authors:

Z.X.Zhou,L.F.Pan

Key ref:

Z.Zhou et al. (2021). Phosphorylation regulates the binding of autophagy receptors to FIP200 Claw domain for selective autophagy initiation. Nat Commun, 12, 1570. PubMed id: 33692357 DOI: 10.1038/s41467-021-21874-1

Date:

09-Sep-20 Release date: 31-Mar-21

Protein chain

Q8TDY2  (RBCC1_HUMAN) -  RB1-inducible coiled-coil protein 1 from Homo sapiens

Seq: 1594 a.a.

Struc: 96 a.a.

Protein chain

Q9ULG6  (CCPG1_HUMAN) -  Cell cycle progression protein 1 from Homo sapiens

Seq: 757 a.a.

Struc: 11 a.a.

DOI no: 10.1038/s41467-021-21874-1

Nat Commun 12:1570 (2021)

PubMed id: 33692357

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

Z.Zhou, J.Liu, T.Fu, P.Wu, C.Peng, X.Gong, Y.Wang, M.Zhang, Y.Li, Y.Wang, X.Xu, M.Li, L.Pan.

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-mediated phosphorylation. In addition, we define the consensus FIP200 Claw-binding motif, and find other autophagy receptors that contain this motif within their conventional LC3-interacting regions. In all, our findings uncover a general and phosphoregulatable binding mode shared by many autophagy receptors to interact with FIP200 Claw for autophagosome biogenesis, and are valuable for further understanding the molecular mechanism of selective autophagy.