Rescue of enzymatic function for disease-associated RPE65 proteins containing various missense mutations in non-active sites

Songhua Li, Tadahide Izumi, Jane Hu, Heather H. Jin, Ahmed Abdul A. Siddiqui, Samuel G. Jacobson, Dean Bok, Minghao Jin

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)18943-18956
Number of pages14
JournalJournal of Biological Chemistry
Volume289
Issue number27
DOIs
StatePublished - Jul 4 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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