DnaJ homolog subfamily B member 2

Definition:

Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family. In parallel, also contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins. Thereby, may regulate the aggregation and promote the functional recovery of misfolded proteins like HTT, MC4R, PRKN, RHO and SOD1 and be crucial for many biological processes. Isoform 1 which is localized to the endoplasmic reticulum membranes may specifically function in ER-associated protein degradation of misfolded proteins.

References:

[1]. Xue-Chao Gao, et al. Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3. PLoS One. 2011;6(5):e19763. [Content Brief]

[2]. Johanna M Rose, et al. Molecular chaperone-mediated rescue of mitophagy by a Parkin RING1 domain mutant. Hum Mol Genet. 2011 Jan 1;20(1):16-27. [Content Brief]

[3]. Britta Westhoff, et al. HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr Biol. 2005 Jun 7;15(11):1058-64. [Content Brief]

[4]. John Labbadia, et al. Suppression of protein aggregation by chaperone modification of high molecular weight complexes. Brain. 2012 Apr;135(Pt 4):1180-96. [Content Brief]

[5]. Xue-Chao Gao, et al. The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation. J Biol Chem. 2012 Feb 17;287(8):6044-52. [Content Brief]

[6]. Sergey S Novoselov, et al. Molecular chaperone mediated late-stage neuroprotection in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis. PLoS One. 2013 Aug 30;8(8):e73944. [Content Brief]

[7]. M E Cheetham, et al. Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b. Eur J Biochem. 1994 Nov 15;226(1):99-107. [Content Brief]

[8]. Eirini Meimaridou, et al. The cytosolic chaperone Hsc70 promotes traffic to the cell surface of intracellular retained melanocortin-4 receptor mutants. Mol Endocrinol. 2011 Sep;25(9):1650-60. [Content Brief]

[9]. J Paul Chapple, et al. The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. J Biol Chem. 2003 May 23;278(21):19087-94. [Content Brief]

Biomedical Dictionary

The Biomedical Dictionary is a comprehensive and professional collection of biological academic terms and subject datas. All explanations are supported by authoritative books or high impact factor literatures, and you can acquire accurate explanations of the biomedical terms you want to know.

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z #

Name
Email *

	Sorry, but the email address you supplied was invalid.