[HTML][HTML] HspB8 participates in protein quality control by a non-chaperone-like mechanism that requires eIF2α phosphorylation
S Carra, JF Brunsting, H Lambert, J Landry… - Journal of biological …, 2009 - ASBMB
Aggregation of mutated proteins is a hallmark of many neurodegenerative disorders,
including Huntington disease. We previously reported that overexpression of the HspB8·
Bag3 chaperone complex suppresses mutated huntingtin aggregation via autophagy.
Classically, HspB proteins are thought to act as ATP-independent molecular chaperones
that can bind unfolded proteins and facilitate their processing via the help of ATP-dependent
chaperones such as the Hsp70 machine, in which Bag3 may act as a molecular link …
including Huntington disease. We previously reported that overexpression of the HspB8·
Bag3 chaperone complex suppresses mutated huntingtin aggregation via autophagy.
Classically, HspB proteins are thought to act as ATP-independent molecular chaperones
that can bind unfolded proteins and facilitate their processing via the help of ATP-dependent
chaperones such as the Hsp70 machine, in which Bag3 may act as a molecular link …