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PDBsum entry 4p1w
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Protein transport
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PDB id
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4p1w
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Contents |
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72 a.a.
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135 a.a.
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399 a.a.
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66 a.a.
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126 a.a.
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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 starvation-Induced assembly of the autophagy initiation complex.
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Authors
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Y.Fujioka,
S.W.Suzuki,
H.Yamamoto,
C.Kondo-Kakuta,
Y.Kimura,
H.Hirano,
R.Akada,
F.Inagaki,
Y.Ohsumi,
N.N.Noda.
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Ref.
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Nat Struct Biol, 2014,
21,
513-521.
[DOI no: ]
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PubMed id
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Abstract
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Assembly of the preautophagosomal structure (PAS) is essential for autophagy
initiation in yeast. Starvation-induced dephosphorylation of Atg13 is required
for the formation of the Atg1-Atg13-Atg17-Atg29-Atg31 complex (Atg1 complex), a
prerequisite for PAS assembly. However, molecular details underlying these
events have not been established. Here we studied the interactions of yeast
Atg13 with Atg1 and Atg17 by X-ray crystallography. Atg13 binds tandem
microtubule interacting and transport domains in Atg1, using an elongated
helix-loop-helix region. Atg13 also binds Atg17, using a short region, thereby
bridging Atg1 and Atg17 and leading to Atg1-complex formation. Dephosphorylation
of specific serines in Atg13 enhanced its interaction with not only Atg1 but
also Atg17. These observations update the autophagy-initiation model as follows:
upon starvation, dephosphorylated Atg13 binds both Atg1 and Atg17, and this
promotes PAS assembly and autophagy progression.
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