[HTML][HTML] HspB8 chaperone activity toward poly (Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy
S Carra, SJ Seguin, H Lambert, J Landry - Journal of Biological Chemistry, 2008 - ASBMB
Mutations in HspB8, a member of the B group of heat shock proteins (Hsp), have been
associated with human neuromuscular disorders. However, the exact function of HspB8 is
not yet clear. We previously demonstrated that overexpression of HspB8 in cultured cells
prevents the accumulation of aggregation-prone proteins such as the polyglutamine protein
Htt43Q. Here we report that HspB8 forms a stable complex with Bag3 in cells and that the
formation of this complex is essential for the activity of HspB8. Bag3 overexpression resulted …
associated with human neuromuscular disorders. However, the exact function of HspB8 is
not yet clear. We previously demonstrated that overexpression of HspB8 in cultured cells
prevents the accumulation of aggregation-prone proteins such as the polyglutamine protein
Htt43Q. Here we report that HspB8 forms a stable complex with Bag3 in cells and that the
formation of this complex is essential for the activity of HspB8. Bag3 overexpression resulted …