English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/179070
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Early cysteine-dependent inactivation of 26S proteasomes does not involve particle disassembly

AuthorsHugo, Martín; Korovila, Ioanna; Köhler, Markus; García-García, Carlos ; Cabrera-García, J. Daniel; Marina, Anabel ; Martínez-Ruiz, Antonio ; Grune, Tilman
Issue Date22-Feb-2018
PublisherElsevier
CitationRedox Biology 16: 123- 128 (2018)
AbstractUnder oxidative stress 26S proteasomes suffer reversible disassembly into its 20S and 19S subunits, a process mediated by HSP70. This inhibits the degradation of polyubiquitinated proteins by the 26S proteasome and allows the degradation of oxidized proteins by a free 20S proteasome. Low fluxes of antimycin A-stimulated ROS production caused dimerization of mitochondrial peroxiredoxin 3 and cytosolic peroxiredoxin 2, but not peroxiredoxin overoxidation and overall oxidation of cellular protein thiols. This moderate redox imbalance was sufficient to inhibit the ATP stimulation of 26S proteasome activity. This process was dependent on reversible cysteine oxidation. Moreover, our results show that this early inhibition of ATP stimulation occurs previous to particle disassembly, indicating an intermediate step during the redox regulation of the 26S proteasome with special relevance under redox signaling rather than oxidative stress conditions.
URIhttp://hdl.handle.net/10261/179070
Identifiersdoi: 10.1016/j.redox.2018.02.016
issn: 2213-2317
Appears in Collections:(CBM) Artículos
Files in This Item:
File Description SizeFormat 
MarinaA_EarlyCysteine-Dependent.pdf588,84 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.