Rpn10 monoubiquitination orchestrates the association of the ubiquilin-type DSK2 receptor with the proteasome (original) (raw)
Research Article| November 27 2015
*Institut de Biologia Molecular de Barcelona, CSIC, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain
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*Institut de Biologia Molecular de Barcelona, CSIC, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain
†Department of Biochemistry and Molecular Biology, Faculty of Biosciences, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain
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*Institut de Biologia Molecular de Barcelona, CSIC, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain
‡Department of Cell Biology, Harvard Medical School, Longwood, Boston, MA 02115, U.S.A.
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*Institut de Biologia Molecular de Barcelona, CSIC, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain
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*Institut de Biologia Molecular de Barcelona, CSIC, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain
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*Institut de Biologia Molecular de Barcelona, CSIC, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain
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Publisher: Portland Press Ltd
Received: May 26 2015
Revision Received: August 10 2015
Accepted: October 07 2015
Accepted Manuscript online: October 08 2015
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2015 Authors; published by Portland Press Limited
2015
Biochem J (2015) 472 (3): 353–365.
Revision Received:
August 10 2015
Accepted:
October 07 2015
Accepted Manuscript online:
October 08 2015
Despite 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 Dsk2I45S, with an inactive ubiquitin-like domain (UBL), show temperature-dependent phenotypes with multiple functional interactions.
© 2015 Authors; published by Portland Press Limited
2015
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