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PDBsum entry 3vu4
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Protein transport
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PDB id
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3vu4
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References listed in PDB file
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Key reference
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Title
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Structure-Based analyses reveal distinct binding sites for atg2 and phosphoinositides in atg18.
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Authors
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Y.Watanabe,
T.Kobayashi,
H.Yamamoto,
H.Hoshida,
R.Akada,
F.Inagaki,
Y.Ohsumi,
N.N.Noda.
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Ref.
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J Biol Chem, 2012,
287,
31681-31690.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Autophagy is an intracellular degradation system by which cytoplasmic materials
are enclosed by an autophagosome and delivered to a lysosome/vacuole. Atg18
plays a critical role in autophagosome formation as a complex with Atg2 and
phosphatidylinositol 3-phosphate (PtdIns(3)P). However, little is known about
the structure of Atg18 and its recognition mode of Atg2 or PtdIns(3)P. Here, we
report the crystal structure of Kluyveromyces marxianus Hsv2, an Atg18 paralog,
at 2.6 Å resolution. The structure reveals a seven-bladed β-propeller without
circular permutation. Mutational analyses of Atg18 based on the K. marxianus
Hsv2 structure suggested that Atg18 has two phosphoinositide-binding sites at
blades 5 and 6, whereas the Atg2-binding region is located at blade 2. Point
mutations in the loops of blade 2 specifically abrogated autophagy without
affecting another Atg18 function, the regulation of vacuolar morphology at the
vacuolar membrane. This architecture enables Atg18 to form a complex with Atg2
and PtdIns(3)P in parallel, thereby functioning in the formation of
autophagosomes at autophagic membranes.
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