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Título

Rpn10 monoubiquitination orchestrates the association of the ubiquilin-Type DSK2 receptor with the proteasome

AutorZuin, Alice; Bichmann, Anne; Isasa, Marta; Puig-Sàrries, Pilar; Díaz, Luis Miguel; Crosas, Bernat
Palabras claveMonoubiquitination
Proteasome
Rpn10 (regulatory particle non-ATPase 10)
Ubiquitin
Dsk2 (dual-specificity protein kinase 2)
Fecha de publicación27-nov-2015
EditorPortland Press
CitaciónBiochemical Journal 472(3): 353-365 (2015)
ResumenDespite the progress made in understanding the roles of proteasome polyubiquitin receptors, such as the subunits Rpn10 (regulatory particle non-ATPase 10) and Rpn13, and the transient interactors Rad23 (radiation sensitivity abnormal 23) and Dsk2 (dual-specificity protein kinase 2), the mechanisms involved in their regulation are virtually unknown. Rpn10, which is found in the cell in proteasome-bound and-unbound pools, interacts with Dsk2, and this interaction has been proposed to regulate the amount of Dsk2 that gains access to the proteasome. Rpn10 monoubiquitination has emerged as a conserved mechanism with a strong effect on Rpn10 function. In the present study, we show that functional yeast proteasomes have the capacity to associate and dissociate with Rpn10 and that Rpn10 monoubiquitination decreases the Rpn10-proteasome and Rpn10-Dsk2 associations. Remarkably, this process facilitates the formation of Dsk2-proteasomes in vivo. Therefore, Rpn10 monoubiquitination acts as mechanism that serves to switch the proteasome from an 'Rpn10 high/Dsk2 low' state to an 'Rpn10 low/Dsk2 high' state. Interestingly, Rpn10-ubiquitin, with an inactivated ubiquitin-interacting motif (UIM), and Dsk2, with an inactive ubiquitin-like domain (UBL), show temperaturedependent phenotypes with multiple functional interactions.
Versión del editorhttp://dx.doi.org/10.1042/BJ20150609
URIhttp://hdl.handle.net/10261/133946
DOI10.1042/BJ20150609
Identificadoresdoi: 10.1042/BJ20150609
issn: 1470-8728
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