Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

Autor: 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
Jazyk: angličtina
Rok vydání: 2016
Předmět:
Zdroj: Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/ncomms12960
Popis: 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.
Databáze: Directory of Open Access Journals