The ubiquitin specific protease-4 (USP4) interacts with the S9/Rpn6 subunit of the proteasome

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...

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Autores:
Tipo de recurso:
Fecha de publicación:
2012
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/23511
Acceso en línea:
https://doi.org/10.1016/j.bbrc.2012.09.075
https://repository.urosario.edu.co/handle/10336/23511
Palabra clave:
Lysine
Proteasome
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
Ubiquitin thiolesterase
Proteasome
S9/psmd11/rpn6
Ubiquitin specific protease 4 (usp4)
Ubiquitin-like domain
tertiary
Protein structure
Rights
License
Abierto (Texto Completo)
Description
Summary: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.