Ítem
Solo Metadatos
The ubiquitin specific protease-4 (USP4) interacts with the S9/Rpn6 subunit of the proteasome
Título de la revista
Autores
Zhao, Bin
Velasco, Kelly
Sompallae, Ramakrishna
Pfirrmann, Thorsten
Masucci, Maria G.
Lindsten, Kristina
Resumen
Abstract
The proteasome is the major non-lysosomal proteolytic machine in cells that, through degradation of ubiquitylated substrates, regulates virtually all cellular functions. Numerous accessory proteins influence the activity of the proteasome by recruiting or deubiquitylating proteasomal substrates, or by maintaining the integrity of the complex. Here we show that the ubiquitin specific protease (USP)-4, a deubiquitylating enzyme with specificity for both Lys48 and Lys63 ubiquitin chains, interacts with the S9/Rpn6 subunit of the proteasome via an internal ubiquitin-like (UBL) domain. S9/Rpn6 acts as a molecular clamp that holds together the proteasomal core and regulatory sub-complexes. Thus, the interaction with USP4 may regulate the structure and function of the proteasome or the turnover of specific proteasomal substrates. © 2012 Elsevier Inc.
Palabras clave
Keywords
Lysine , tertiary , Proteinase , Ubiquitin , Ubiquitin specific protease 4 , Unclassified drug , Article , Controlled study , Embryo , Enzyme binding , Enzyme specificity , Enzyme structure , Enzyme substrate , Enzyme substrate complex , Female , Human , Human cell , In vitro study , Priority journal , Protein domain , Protein function , Protein protein interaction , Protein subunit , Ubiquitination , Hek293 cells , Hela cells , Humans , Proteasome endopeptidase complex , Protein structure , Ubiquitin thiolesterase , Proteasome , S9/psmd11/rpn6 , Ubiquitin specific protease 4 (usp4) , Ubiquitin-like domain
