Background: Disease-causing mutations reduce RPE65 protein levels with unknown mechanisms. Results: Interaction of 26 S proteasome non-ATPase regulatory subunit 13 with mutant RPE65s mediates degradation of misfolded RPE65s via the ubiquitin-proteasome pathway. Conclusion: Many mutant RPE65s with non-active site mutations are catalytically active and can be rescued. Significance: Low temperature and chaperones that rescue enzymatic function of mutant RPE65s are therapeutic candidates.
|Number of pages||14|
|Journal||Journal of Biological Chemistry|
|State||Published - Jul 4 2014|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology