Article
Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper.
The EMBO journal - 1 Mar 2001
Thress K, Song J, Morimoto R I, Kornbluth S
Abstract excerpt
Protein folding mediated by the Hsp70 family of molecular chaperones requires both ATP and the co-chaperone Hdj-1. BAG-1 was recently identified as a bcl-2-interacting, anti-apoptotic protein that binds to the ATPase domain of Hsp70 and prevents the release of the substrate. While this suggested that cells had the potential to modulate Hsp70-mediated protein folding, physiological regulators of BAG-1 have yet to...
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