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PDBsum entry 5e6o
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Protein binding/peptide
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PDB id
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5e6o
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References listed in PDB file
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Key reference
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Title
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Structural basis of the differential function of the two c. Elegans atg8 homologs, Lgg-1 and lgg-2, In autophagy.
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Authors
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F.Wu,
Y.Watanabe,
X.Y.Guo,
X.Qi,
P.Wang,
H.Y.Zhao,
Z.Wang,
Y.Fujioka,
H.Zhang,
J.Q.Ren,
T.C.Fang,
Y.X.Shen,
W.Feng,
J.J.Hu,
N.N.Noda,
H.Zhang.
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Ref.
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Mol Cell, 2015,
60,
914-929.
[DOI no: ]
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PubMed id
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Abstract
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Multicellular organisms have multiple homologs of the yeast ATG8 gene, but the
differential roles of these homologs in autophagy during development remain
largely unknown. Here we investigated structure/function relationships in the
two C. elegans Atg8 homologs, LGG-1 and LGG-2. lgg-1 is essential for
degradation of protein aggregates, while lgg-2 has cargo-specific and
developmental-stage-specific roles in aggregate degradation. Crystallography
revealed that the N-terminal tails of LGG-1 and LGG-2 adopt the closed and open
form, respectively. LGG-1 and LGG-2 interact differentially with autophagy
substrates and Atg proteins, many of which carry a LIR motif. LGG-1 and LGG-2
have structurally distinct substrate binding pockets that prefer different
residues in the interacting LIR motif, thus influencing binding specificity.
Lipidated LGG-1 and LGG-2 possess distinct membrane tethering and fusion
activities, which may result from the N-terminal differences. Our study reveals
the differential function of two ATG8 homologs in autophagy during C. elegans
development.
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