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PDBsum entry 7d0e
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Signaling protein/protein binding
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PDB id
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7d0e
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References listed in PDB file
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Key reference
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Title
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Phosphorylation regulates the binding of autophagy receptors to fip200 claw domain for selective autophagy initiation.
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Authors
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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.
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Ref.
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Nat Commun, 2021,
12,
1570.
[DOI no: ]
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PubMed id
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Abstract
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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.
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