DnaJ homolog subfamily B member 12

Definition:

Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear.; (Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection.

References:

[1]. Kai Li, et al. Tetrameric Assembly of K+ Channels Requires ER-Located Chaperone Proteins. Mol Cell. 2017 Jan 5;65(1):52-65. [Content Brief]

[2]. Yo-hei Yamamoto, et al. A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR. Cell Struct Funct. 2010;35(2):107-16. [Content Brief]

[3]. Edward C Goodwin, et al. BiP and multiple DNAJ molecular chaperones in the endoplasmic reticulum are required for efficient simian virus 40 infection. mBio. 2011 Jun 14;2(3):e00101-11. [Content Brief]

[4]. Edward C Goodwin, et al. Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure. PLoS One. 2014 Apr 14;9(4):e94322. [Content Brief]

[5]. Diane E Grove, et al. The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508. Mol Biol Cell. 2011 Feb 1;22(3):301-14. [Content Brief]

[6]. Christopher Paul Walczak, et al. A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum. PLoS Pathog. 2014 Mar 27;10(3):e1004007. [Content Brief]

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