Disease relevance of DNAJB11

• Although overexpression of ERdj3 by gene transfection could not strengthen ER stress tolerance of neuroblastoma cells, reduction of ERdj3 expression by small interfering ribonucleic acid decreased the tolerance of cells, indicating that ERdj3 might have just a marginal role in the ER stress resistance of neuroblastoma cells [1].

High impact information on DNAJB11

• ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates [2].
• BiP remained bound to unfolded light chains longer than ERdj3, which interacted with unfolded light chains initially, but quickly disassociated before protein folding was completed [2].
• Down-regulation of ABBP-2 expression in cultured cells inhibits endogenous apobec-1-mediated apoB mRNA editing [3].
• It is a ubiquitously expressed protein, and, by transfection analysis of GFP-ABBP-2, we found that the protein is located in both the nucleus and cytosol of transfected cells, with predominance in the nucleus [3].
• Overexpression of GRP78 partially suppressed the apoptosis and induction of CHOP in the presence of celecoxib and this suppression was stimulated by coexpression of either ERdj3 or ERdj4 [4].

Biological context of DNAJB11

• In contrast, overexpression of ERdj3 notably suppressed vero toxin-induced cell death [1].

Anatomical context of DNAJB11

• Localization and function in endoplasmic reticulum stress tolerance of ERdj3, a new member of Hsp40 family protein [1].
• A burful of dentin was removed from the EDJ of one of the section faces and these samples were processed to establish the level of dentin infection [5].
• Among the samples studied, cercopithecoid primates have a unique dentine shape, and it is suggested that the development of bilophodont molars may be related to the distinctive EDJ configuration in cercopithecoids [6].

Associations of DNAJB11 with chemical compounds

• Biochemical analysis of the canine protein characterized ERj3p as a soluble glycoprotein of the pancreatic endoplasmic reticulum [7].

Physical interactions of DNAJB11

• Furthermore, we found that ERj3p interacts with SDF2L1 protein that may be involved in protein O-glycosylation [7].

Analytical, diagnostic and therapeutic context of DNAJB11

• Epitope-tagged HEDJ was demonstrated by confocal microscopy to be localized to the endoplasmic reticulum [8].
• Here we verified the predicted protein sequence of human ERj3p by sequence analysis of the corresponding cDNA [7].

References