BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.
Function
chaperone binding;
Synonyms
BAG3; BCL2-associated athanogene 3; BAG family molecular chaperone regulator 3; docking protein CAIR-1; BCL2-binding athanogene 3; bcl-2-binding protein Bis; bcl-2-associated athanogene 3; BAG-family molecular chaperone regulator-3; BIS; BAG-3; CAIR-1; MGC104307;
Citations
Publication ()
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