DnaJ homolog subfamily A member 1

Definition:

Co-chaperone for HSPA8/Hsc70. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV.

References:

[1]. K Terada, et al. Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. J Biol Chem. 2000 Aug 11;275(32):24728-34. [Content Brief]

[2]. M Kanazawa, et al. HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria. J Biochem. 1997 May;121(5):890-5. [Content Brief]

[3]. Jaime L Stark, et al. Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer. Biochemistry. 2014 Mar 4;53(8):1360-72. [Content Brief]

[4]. T Gotoh, et al. hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ. 2004 Apr;11(4):390-402. [Content Brief]

[5]. 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]

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