BAG family molecular chaperone regulator 3

Definition:

Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport.

References:

[1]. J H Lee, et al. Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death. Oncogene. 1999 Nov 4;18(46):6183-90. [Content Brief]

[2]. S Takayama, et al. An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators. J Biol Chem. 1999 Jan 8;274(2):781-6. [Content Brief]

[3]. Young-Hee Jin, et al. BAG3 affects the nucleocytoplasmic shuttling of HSF1 upon heat stress. Biochem Biophys Res Commun. 2015 Aug 21;464(2):561-7. [Content Brief]

[4]. Jennifer N Rauch, et al. Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J Biol Chem. 2014 Jan 17;289(3):1402-14. [Content Brief]

[5]. Jennifer N Rauch, et al. Non-canonical Interactions between Heat Shock Cognate Protein 70 (Hsc70) and Bcl2-associated Anthanogene (BAG) Co-Chaperones Are Important for Client Release. J Biol Chem. 2016 Sep 16;291(38):19848-57. [Content Brief]

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