5YPC

p62/SQSTM1 ZZ domain with Phe-peptide

5YPC の概要

• エントリーDOI: 10.2210/pdb5ypc/pdb
• 分子名称: 78 kDa glucose-regulated protein,Sequestosome-1, ZINC ION (3 entities in total)
• 機能のキーワード: complex, p62/sqstm1, zz domain, autophagy, n-end rule, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 26536.45

構造登録者

Kwon, D.H.,Kim, L.,Song, H.K. (登録日: 2017-11-01, 公開日: 2018-08-29, 最終更新日: 2024-03-27)

主引用文献

Kwon, D.H.,Park, O.H.,Kim, L.,Jung, Y.O.,Park, Y.,Jeong, H.,Hyun, J.,Kim, Y.K.,Song, H.K.
Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter.
Nat Commun, 9:3291-3291, 2018

PubMed Abstract: p62/SQSTM1 is the key autophagy adapter protein and the hub of multi-cellular signaling. It was recently reported that autophagy and N-end rule pathways are linked via p62. However, the exact recognition mode of degrading substrates and regulation of p62 in the autophagic pathway remain unknown. Here, we present the complex structures between the ZZ-domain of p62 and various type-1 and type-2 N-degrons. The binding mode employed in the interaction of the ZZ-domain with N-degrons differs from that employed by classic N-recognins. It was also determined that oligomerization via the PB1 domain can control functional affinity to the R-BiP substrate. Unexpectedly, we found that self-oligomerization and disassembly of p62 are pH-dependent. These findings broaden our understanding of the functional repertoire of the N-end rule pathway and provide an insight into the regulation of p62 during the autophagic pathway.

PubMed: 30120248
DOI: 10.1038/s41467-018-05825-x

実験手法

X-RAY DIFFRACTION (1.962 Å)