Journal
FEBS LETTERS
Volume 584, Issue 8, Pages 1585-1590Publisher
WILEY
DOI: 10.1016/j.febslet.2010.03.018
Keywords
Ubiquitin; Proteasome; Ubiquitin binding domain; Stabilization signal; Paget's disease of bone; Sequestosome-1; Rad23
Funding
- Swedish Research Council (NPD)
- Swedish Cancer Society (NPD)
- Nordic Center of Excellence Neurodegeneration (NPD)
- European Community Network of Excellence RUBICON [LSHCCT-2005-018683]
- Wenner-Gren Foundation (CB)
- Foundation of Geriatric Diseases (CB)
- Biotechnology and Biological Sciences Research Council (JL)
- Engineering and Physical Sciences Research Council (TPG)
- School of Chemistry at Nottingham (TPG)
- National Association for the Relief of Paget's Disease and Arthritis Research Campaign (RL)
- MRC [G0300413] Funding Source: UKRI
- Medical Research Council [G0300413] Funding Source: researchfish
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We show that the ubiquitin-associated domain (UBA) of human p62/sequestosome-1 (SQSTM1) can delay degradation of proteasome substrates in yeast. Taking advantage of naturally occurring mutant UBA domains that are linked to Paget's disease of bone (PDB), we found that three of the four mutant UBA domains tested in this study were able to inhibit proteasomal degradation, albeit not to the same extent as the wild-type domain. Interestingly, the stability measured as the fraction of folded protein, and not the ubiquitin binding properties, of the PDB-associated UBA domains correlated with their protective effects. These data suggest that the protective effect of UBA domains depends on their structural integrity rather than ubiquitin binding capabilities. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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