5JM9

Structure of S. cerevesiae mApe1 dodecamer

5JM9 の概要

• エントリーDOI: 10.2210/pdb5jm9/pdb
• EMDBエントリー: 8167
• 分子名称: Vacuolar aminopeptidase 1 (1 entity in total)
• 機能のキーワード: dodecamer, aminopeptidase, vacuole, cvt, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Vacuole : P14904
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57162.43

構造登録者

Sachse, C.,Bertipaglia, C. (登録日: 2016-04-28, 公開日: 2016-06-15, 最終更新日: 2024-05-15)

主引用文献

Bertipaglia, C.,Schneider, S.,Jakobi, A.J.,Tarafder, A.K.,Bykov, Y.S.,Picco, A.,Kukulski, W.,Kosinski, J.,Hagen, W.J.,Ravichandran, A.C.,Wilmanns, M.,Kaksonen, M.,Briggs, J.A.,Sachse, C.
Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle.
Embo Rep., 17:1044-1060, 2016

PubMed Abstract: 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.

PubMed: 27266708
DOI: 10.15252/embr.201541960

実験手法

ELECTRON MICROSCOPY (24 Å)