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PDBsum entry 5jm6
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References listed in PDB file
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Key reference
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Title
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Higher-Order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the cvt vesicle.
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Authors
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C.Bertipaglia,
S.Schneider,
A.J.Jakobi,
A.K.Tarafder,
Y.S.Bykov,
A.Picco,
W.Kukulski,
J.Kosinski,
W.J.Hagen,
A.C.Ravichandran,
M.Wilmanns,
M.Kaksonen,
J.A.Briggs,
C.Sachse.
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Ref.
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Embo Rep, 2016,
17,
1044-1060.
[DOI no: ]
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PubMed id
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Abstract
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Selective autophagy is the mechanism by which large cargos are specifically
sequestered for degradation. The structural details of cargo and receptor
assembly giving rise to autophagic vesicles remain to be elucidated. We utilize
the yeast cytoplasm-to-vacuole targeting (Cvt) pathway, a prototype of selective
autophagy, together with a multi-scale analysis approach to study the molecular
structure of Cvt vesicles. We report the oligomeric nature of the major Cvt
cargo Ape1 with a combined 2.8 Å X-ray and negative stain EM structure, as well
as the secondary cargo Ams1 with a 6.3 Å cryo-EM structure. We show that the
major dodecameric cargo prApe1 exhibits a tendency to form higher-order chain
structures that are broken upon interaction with the receptor Atg19 in vitro The
stoichiometry of these cargo-receptor complexes is key to maintaining the size
of the Cvt aggregate in vivo Using correlative light and electron microscopy, we
further visualize key stages of Cvt vesicle biogenesis. Our findings suggest
that Atg19 interaction limits Ape1 aggregate size while serving as a vehicle for
vacuolar delivery of tetrameric Ams1.
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