7BRT

Crystal structure of Sec62 LIR fused to GABARAP

7BRT の概要

• エントリーDOI: 10.2210/pdb7brt/pdb
• 関連するPDBエントリー: 7BRN 7BRQ
• 分子名称: Translocation protein SEC62,Gamma-aminobutyric acid receptor-associated protein (2 entities in total)
• 機能のキーワード: autophagy, endoplasmic reticulum, membrane protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31783.97

構造登録者

Yamasaki, A.,Noda, N.N. (登録日: 2020-03-30, 公開日: 2020-07-08, 最終更新日: 2023-11-29)

主引用文献

Mochida, K.,Yamasaki, A.,Matoba, K.,Kirisako, H.,Noda, N.N.,Nakatogawa, H.
Super-assembly of ER-phagy receptor Atg40 induces local ER remodeling at contacts with forming autophagosomal membranes.
Nat Commun, 11:3306-3306, 2020

PubMed Abstract: The endoplasmic reticulum (ER) is selectively degraded by autophagy (ER-phagy) through proteins called ER-phagy receptors. In Saccharomyces cerevisiae, Atg40 acts as an ER-phagy receptor to sequester ER fragments into autophagosomes by binding Atg8 on forming autophagosomal membranes. During ER-phagy, parts of the ER are morphologically rearranged, fragmented, and loaded into autophagosomes, but the mechanism remains poorly understood. Here we find that Atg40 molecules assemble in the ER membrane concurrently with autophagosome formation via multivalent interaction with Atg8. Atg8-mediated super-assembly of Atg40 generates highly-curved ER regions, depending on its reticulon-like domain, and supports packing of these regions into autophagosomes. Moreover, tight binding of Atg40 to Atg8 is achieved by a short helix C-terminal to the Atg8-family interacting motif, and this feature is also observed for mammalian ER-phagy receptors. Thus, this study significantly advances our understanding of the mechanisms of ER-phagy and also provides insights into organelle fragmentation in selective autophagy of other organelles.

PubMed: 32620754
DOI: 10.1038/s41467-020-17163-y

実験手法

X-RAY DIFFRACTION (1.999 Å)