TY - JOUR
T1 - Rescue of enzymatic function for disease-associated RPE65 proteins containing various missense mutations in non-active sites
AU - Li, Songhua
AU - Izumi, Tadahide
AU - Hu, Jane
AU - Jin, Heather H.
AU - Siddiqui, Ahmed Abdul A.
AU - Jacobson, Samuel G.
AU - Bok, Dean
AU - Jin, Minghao
PY - 2014/7/4
Y1 - 2014/7/4
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/84903828418
UR - https://www.scopus.com/pages/publications/84903828418#tab=citedBy
U2 - 10.1074/jbc.M114.552117
DO - 10.1074/jbc.M114.552117
M3 - Article
C2 - 24849605
AN - SCOPUS:84903828418
SN - 0021-9258
VL - 289
SP - 18943
EP - 18956
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 27
ER -