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Structure paper

TitleHigher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle.
Journal, issue, pagesEMBO Rep, Vol. 17, Issue 7, Page 1044-1060, Year 2016
Publish dateJun 6, 2016
AuthorsChiara Bertipaglia / Sarah Schneider / Arjen J Jakobi / Abul K Tarafder / Yury S Bykov / Andrea Picco / Wanda Kukulski / Jan Kosinski / Wim Jh Hagen / Arvind C Ravichandran / Matthias Wilmanns / Marko Kaksonen / John Ag Briggs / Carsten Sachse /
PubMed AbstractSelective 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 ...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.
External linksEMBO Rep / PubMed:27266708 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.758 - 24.0 Å
Structure data

8166

5jm0

EMDB-8166, PDB-5jm0:
Structure of the S. cerevisiae alpha-mannosidase 1
Method: EM (single particle) / Resolution: 6.3 Å

8167

5jm9

EMDB-8167, PDB-5jm9:
Structure of S. cerevesiae mApe1 dodecamer
Method: EM (single particle) / Resolution: 24.0 Å

PDB-5jm6:
Structure of Chaetomium thermophilum mApe1
Method: X-RAY DIFFRACTION / Resolution: 2.758 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae s288c (yeast)
  • chaetomium thermophilum (fungus)
KeywordsHYDROLASE / tetramer / cvt cargo / mannosidase / selective autophagy / aminopeptidase / dodecamer / cvt pathway / vacuole / cvt

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