Article
Prevention of aberrant protein aggregation by anchoring the molecular chaperone αB-crystallin to the endoplasmic reticulum.
Biochemical and biophysical research communications - 12 Dec 2014
Yamamoto Shinichiro, Yamashita Arisa, Arakaki Naokatu, Nemoto Hisao, Yamazaki Tetsuo
Abstract excerpt
The chaperone αB-crystallin (αBC) is a member of the small heat shock protein family and its point or truncated mutants cause the muscular disorder α-crystallinopathy. The illness is histologically characterized by accumulation of protein aggregates in muscle cells. Expression of the myopathy-causing R120G mutant of αBC, harboring an arginine-to-glycine mutation at position 120, results in aggregate formation. We...
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