NDLI: Proteasome regulation by ADP-ribosylation

Content Provider	PubMed Central
Author	Cho-park, Park F. Steller, Hermann
Copyright Year	2013
Abstract	Protein degradation by the ubiquitin-proteasome system is central to cell homeostasis and survival. Defects in this process are associated with diseases such as cancer and neurodegenerative disorders. The 26S proteasome is a large protease complex that degrades ubiquitinated proteins. Here we show that ADP-ribosylation promotes 26S proteasome activity in both Drosophila and human cells. We identify the ADP-ribosyl transferase Tankyrase (TNKS) and the 19S assembly chaperones dp27 and dS5b as direct binding partners of the proteasome regulator PI31. TNKS-mediated ADP-ribosylation of PI31 drastically reduces its affinity for 20S proteasome α-subunits to relieve 20S repression by PI31. Additionally, PI31 modification increases binding to and sequestration of dp27 and dS5b from 19S regulatory particles, promoting 26S assembly. Inhibition of TNKS by either RNAi or a small-molecule inhibitor, XAV939, blocks this process to reduce 26S assembly. These results unravel a mechanism of proteasome regulation that can be targeted with existing small-molecule inhibitors.
Related Links	http://dx.doi.org/10.1016/j.cell.2013.03.040
Ending Page	627
Page Count	14
Starting Page	614
File Format	PDF
ISSN	00928674
e-ISSN	10974172
Journal	Cell
Issue Number	3
Volume Number	153
Language	English
Publisher Date	2013-04-01
Access Restriction	Open
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology

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