Abstract:
:Mutations in retinol dehydrogenase 12 (RDH12) cause severe retinal degeneration. However, some of the disease-associated RDH12 mutants retain significant catalytic activity, indicating the existence of additional pathophysiological mechanisms. This study demonstrates that the catalytically active T49M and I51N mutants undergo accelerated degradation, which results in their reduced cellular levels. Inhibition of proteasome leads to significant accumulation of ubiquitylated T49M and I51N. Furthermore, the degree of ubiquitylation strongly correlates with the half-lives of the proteins. These results suggest that the accelerated degradation of RDH12 mutants by the ubiquitin-proteasome system contributes to the pathophysiology and phenotypic variability associated with mutations in the RDH12 gene.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lee SA,Belyaeva OV,Kedishvili NYdoi
10.1016/j.febslet.2009.12.009subject
Has Abstractpub_date
2010-02-05 00:00:00pages
507-10issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(09)01055-2journal_volume
584pub_type
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