6TGN

Cryo-EM structure of AtNBR1-PB1 filament (L-type)

6TGN の概要

• エントリーDOI: 10.2210/pdb6tgn/pdb
• EMDBエントリー: 10499
• 分子名称: Protein NBR1 homolog (1 entity in total)
• 機能のキーワード: autophagy, helical filament, signaling protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10198.56

構造登録者

Jakobi, A.J.,Sachse, C. (登録日: 2019-11-17, 公開日: 2020-02-12, 最終更新日: 2024-05-22)

主引用文献

Jakobi, A.J.,Huber, S.T.,Mortensen, S.A.,Schultz, S.W.,Palara, A.,Kuhm, T.,Shrestha, B.K.,Lamark, T.,Hagen, W.J.H.,Wilmanns, M.,Johansen, T.,Brech, A.,Sachse, C.
Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake.
Nat Commun, 11:440-440, 2020

PubMed Abstract: p62/SQSTM1 is an autophagy receptor and signaling adaptor with an N-terminal PB1 domain that forms the scaffold of phase-separated p62 bodies in the cell. The molecular determinants that govern PB1 domain filament formation in vitro remain to be determined and the role of p62 filaments inside the cell is currently unclear. We here determine four high-resolution cryo-EM structures of different human and Arabidopsis PB1 domain assemblies and observed a filamentous ultrastructure of p62/SQSTM1 bodies using correlative cellular EM. We show that oligomerization or polymerization, driven by a double arginine finger in the PB1 domain, is a general requirement for lysosomal targeting of p62. Furthermore, the filamentous assembly state of p62 is required for autophagosomal processing of the p62-specific cargo KEAP1. Our results show that using such mechanisms, p62 filaments can be critical for cargo uptake in autophagy and are an integral part of phase-separated p62 bodies.

PubMed: 31974402
DOI: 10.1038/s41467-020-14343-8

実験手法

ELECTRON MICROSCOPY (3.9 Å)