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PDBsum entry 4tq1
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Protein binding
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PDB id
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4tq1
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References listed in PDB file
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Key reference
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Title
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Insights into autophagosome maturation revealed by the structures of atg5 with its interacting partners.
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Authors
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J.H.Kim,
S.B.Hong,
J.K.Lee,
S.Han,
K.H.Roh,
K.E.Lee,
Y.K.Kim,
E.J.Choi,
H.K.Song.
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Ref.
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Autophagy, 2015,
11,
75-87.
[DOI no: ]
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PubMed id
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Abstract
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Autophagy is a bulky catabolic process that responds to nutrient homeostasis and
extracellular stress signals and is a conserved mechanism in all eukaryotes.
When autophagy is induced, cellular components are sequestered within an
autophagosome and finally degraded by subsequent fusion with a lysosome. During
this process, the ATG12-ATG5 conjugate requires 2 different binding partners,
ATG16L1 for autophagosome elongation and TECPR1 for lysosomal fusion. In our
current study, we describe the crystal structures of human ATG5 in complex with
an N-terminal domain of ATG16L1 as well as an internal AIR domain of TECPR1.
Both binding partners exhibit a similar α-helical structure containing a
conserved binding motif termed AFIM. Furthermore, we characterize the critical
role of the C-terminal unstructured region of the AIR domain of TECPR1. These
findings are further confirmed by biochemical and cell biological analyses.
These results provide new insights into the molecular details of the
autophagosome maturation process, from its elongation to its fusion with a
lysosome.
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