Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/123774
COMPARTIR / EXPORTAR:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Título

An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination

AutorPuig-Sàrries, Pilar CSIC; Bijlmakers, Marie-José CSIC; Zuin, Alice CSIC ORCID ; Bichmann, Anne CSIC; Pons, Miquel CSIC; Crosas, Bernat CSIC ORCID
Palabras claveE3 ubiquitin ligase
Fold-back model
Intrinsically disordered protein
Monoubiquitination
Polyubiquitin chain
Proteasome
Rpn10
Rsp5
Ubiquitin
Fecha de publicación1-ago-2015
EditorPortland Press
Biochemical Society
CitaciónBiochemical Journal 469(3): 455-467 (2015)
Resumen© 2015 Authors; published by Portland Press Limited. Despite being a common mechanism in eukaryotes, the process by which protein monoubiquitination is produced and regulated in vivo is not completely understood. We present here the analysis of the process of monoubiquitination of the proteasomal subunit Rpn10 (regulatory particle non-ATPase 10), involved in the recruitment of polyubiquitinated substrates. Rpn10 is monoubiquitinated in vivo by the Nedd4 (neural precursor cell expressed developmentally down-regulated 4) enzyme Rsp5 (reverses SPT-phenotype protein 5) and this modification impairs the interaction of Rpn10 with substrates, having a regulatory effect on proteasome function. Remarkably, a disordered region near the ubiquitin-interacting motif of Rpn10 plays a role in the restriction of the polyubiquitin extension activity of Rsp5. Mutations in this disordered region promote ubiquitin chain extension of Rpn10. Thus, our work sheds light on the molecular basis and the functional relevance of a type of monoubiquitination that is driven by the substrate. Moreover, we uncover a putative role for disordered regions in modulating ubiquitin-protein ligation.
Versión del editorhttp://dx.doi.org/10.1042/BJ20141571
URIhttp://hdl.handle.net/10261/123774
DOI10.1042/BJ20141571
Identificadoresdoi: 10.1042/BJ20141571
issn: 1470-8728
Aparece en las colecciones: (IBMB) Artículos




Ficheros en este ítem:
Fichero Descripción Tamaño Formato
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo

CORE Recommender

SCOPUSTM   
Citations

3
checked on 10-mar-2024

WEB OF SCIENCETM
Citations

3
checked on 25-feb-2024

Page view(s)

313
checked on 17-mar-2024

Download(s)

113
checked on 17-mar-2024

Google ScholarTM

Check

Altmetric

Altmetric


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.