Mutant p62/SQSTM1 UBA domains linked to Paget's disease of bone differ in their abilities to function as stabilization signals.
FEBS Lett
; 584(8): 1585-90, 2010 Apr 16.
Article
em En
| MEDLINE
| ID: mdl-20230821
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Osteíte Deformante
/
Ubiquitina
/
Proteínas Adaptadoras de Transdução de Sinal
/
Mutação
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article