| First Author | Dennissen FJ | Year | 2011 |
| Journal | FEBS Lett | Volume | 585 |
| Issue | 16 | Pages | 2568-74 |
| PubMed ID | 21762696 | Mgi Jnum | J:175529 |
| Mgi Id | MGI:5285991 | Doi | 10.1016/j.febslet.2011.06.037 |
| Citation | Dennissen FJ, et al. (2011) Mutant ubiquitin (UBB+1) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3). FEBS Lett 585(16):2568-74 |
| abstractText | Mutant ubiquitin (UBB(+1)) accumulates in the hallmarks of tauopathies and polyglutamine diseases. We show that the deubiquitinating enzyme YUH1 of Saccharomyces cerevisiae and its mouse and human ortholog UCH-L3 are able to hydrolyze the C-terminal extension of UBB(+1). This yields another dysfunctional ubiquitin molecule (UB(G76Y)) with biochemical properties similar to full length UBB(+1). UBB(+1) may be detected in post-mortem tissue due to impaired C-terminal truncation of UBB(+1). Although the level of UCH-L3 protein in several neurodegenerative diseases is unchanged, we show that in vitro oxidation of recombinant UCH-L3 impairs its deubiquitinating activity. We postulate that impaired UCH-L3 function may contribute to the accumulation of full length UBB(+1) in various pathologies. |
