Back to Search Start Over

Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

Authors :
Tal Keren-Kaplan
Lee Zeev Peters
Olga Levin-Kravets
Ilan Attali
Oded Kleifeld
Noa Shohat
Shay Artzi
Ori Zucker
Inbar Pilzer
Noa Reis
Michael H. Glickman
Shay Ben-Aroya
Gali Prag
Source :
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Publication Year :
2016
Publisher :
Nature Portfolio, 2016.

Abstract

Ubiquitin (Ub) receptors are responsible for the recognition of ubiquitylated proteins. Here the authors describe the crystal structure of the ubiquitylated form of the Ub-receptor Rpn10, which suggest that ubiquitylation of Rpn10 promotes its dissociation from the proteasome.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
7
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.8431d5b994ec4a4ca5d12daa3a68d3a3
Document Type :
article
Full Text :
https://doi.org/10.1038/ncomms12960