Ask about this productRelated genes to: DNAJB12 Blocking Peptide
- Gene:
- DNAJB12 NIH gene
- Name:
- DnaJ heat shock protein family (Hsp40) member B12
- Previous symbol:
- -
- Synonyms:
- DJ10, FLJ20027
- Chromosome:
- 10q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-09
- Date modifiied:
- 2016-10-05
Related products to: DNAJB12 Blocking Peptide
Related articles to: DNAJB12 Blocking Peptide
- Interorganellar protein redistribution is an emerging but underexplored aspect of proteostasis and cellular adaptation. Beyond canonical transcriptional and translational regulation, cells dynamically reprogram the spatial distribution of proteins to rapidly respond to environmental stress. This spatial plasticity enables single gene products to acquire novel, context-dependent functions on the basis of subcellular localization. Such relocalization is particularly pronounced in pathological conditions, such as cancer and viral infections, where proteome remodeling enhances cellular survival and adaptability. We previously defined endoplasmic reticulum (ER)-to-cytosol signaling (ERCYS) as a stress-responsive mechanism that alleviates ER burden by redistributing proteins into the cytosol. Despite growing interest, the molecular mechanisms driving ERCYS and related forms of spatial proteome remodeling remain poorly defined. - Source: PubMed
Publication date: 2026/02/14
Biadsy SumaGilad AyeletMadegam Laila AbuIgbaria Aeid - During chronic HBV infection, the massive secretion of HBV envelope proteins (HBsAg) as non-infectious subviral particles (SVPs) remains a significant challenge in achieving a functional cure. Despite this, the HBsAg folding process, essential for HBV and HDV particle morphogenesis, remains poorly understood. DNAJB12 and DNAJB14 are two recently identified co-chaperones implicated in transmembrane protein folding. Utilizing the nucleic acid polymer REP 2139 as a bait, we identified DNAJB12 as a REP 2139 interactor, and its knockdown impedes the morphogenesis and secretion of SVP and HBV virions. Conversely, DNAJB14, which did not interact with REP 2139, selectively impaired the morphogenesis of virions. Additionally, knockdowns of DNAJB12 and DNAJB14 hindered the production of infectious HDV. As DNAJB12 knockdown recapitulated REP 2139 antiviral effects observed in clinical trials, our findings highlight DNAJB12 as the potential primary target of REP 2139 and uncover functional roles for DNAJB12 and DNAJB14 in HBV and HDV life cycles. - Source: PubMed
Publication date: 2025/10/30
Angelo LénaBoulon RichardLabonté Patrick - Dilated cardiomyopathy (DCM) is a severe form of cardiomyopathy. The study aims to investigate the impact of metabolic and lifestyle factors on DCM and to identify new potential therapeutic targets. - Source: PubMed
Publication date: 2025/12/30
Wang HuiWang YihuiHuang DezhiJiang XiaoLi CaiyunXia XutingLiu GuichunShi JianchenLi Xinhui - Numerous cellular pathways are known to cause resistance in cancer cells. The unfolded protein response (UPR), a signaling pathway activated during proteostasis stress in the endoplasmic reticulum (ER), is an adaptive process to increase cancer cell fitness. However, the molecular mechanism between ER stress, UPR activation, and chemoresistance is insufficiently understood. Here, we report that ER stress induction and UPR activation are necessary for chemoresistance to cisplatin and doxorubicin. Mild ER stress is a sufficient precondition for cancer cells to evade cisplatin- and doxorubicin-associated cell death. Mechanistically, ER stress induction results in the redistribution of PDIA4 from the ER to the cytosol, facilitated by the c-tail-anchored proteins DNAJB12 and DNAJB14 and the cytosolic HSC70-cochaperone SGTA. In the cytosol, PDIA4 forms an inhibitory interaction with caspase-3 and wt-p53, leading to their attenuation and increased cancer cell proliferation. Furthermore, we show that PDIA4 must originate from the ER to inhibit caspase-3 and wt-p53 in the cytosol. Silencing PDIA4, DNAJB12/14, or SGTA rescues wt-p53 and caspase-3 activity. Finally, we found that in tumors isolated from colorectal cancer patients, PDIA4 and DNAJB12 are highly expressed compared to their healthy tissues; this expression is associated with the induction of the UPR. Our data show a novel non-genetic mechanism to inhibit apoptosis and suggest PDIA4, DNAJB12/14, and SGTA as novel therapeutic targets to rescue apoptosis and inhibit proliferation in cancer cells. - Source: PubMed
Publication date: 2025/10/21
Twito GalAbu Abayed Faiza AmteratGilad AyeletBiadsy SumaGavriel NoaSheikh Suliman SuadMizrahi YardenMegged HilaTenenboim MorAbu-Freha NaimIgbaria Aeid - The human (Homo sapiens; Hs) methyltransferase (MTase) METTL9 is the first enzyme shown to generate 1-methylhistidine (π-methylhistidine) in proteins. METTL9 preferentially methylates an alternating histidine (HxH) motif, where "x" is a small, uncharged amino acid, and multiple substrates have been identified. Putative METTL9 orthologues are found in most eukaryotes, and we have here investigated the activity of such enzymes from several species, representing all five eukaryotic supergroups. The majority of the tested enzymes demonstrated in vitro MTase activity on the prototype HsMETTL9 substrates ARMC6 and DNAJB12. We also detected protein methylation activity of the Caenorhabditis elegans METTL9 which had previously been suggested to be a DNA MTase. However, METTL9 from the fruit fly (Drosophila melanogaster; Dm) and the picoplankton Ostreococcus tauri (Ot) displayed distinct substrate specificities, differing from each other and from that of HsMETTL9. These differences were observed when recombinant proteins and short peptides were used as METTL9 substrates. To further analyze substrate specificity, we used peptide arrays to systematically replace the "x" residue and the residues flanking the HxH motif in a substrate peptide. This revealed varying degrees of tolerance among the METTL9 orthologues (Hs > Dm > Ot) for substitutions at these positions. Our results show that the METTL9 orthologues, although requiring an HxH target site, have evolved different substrate specificities, likely due to differing biologically relevant substrates in the respective organisms. Furthermore, we solved the X-ray structure of OtMETTL9, revealing several differences from the previously published HsMETTL9 structures that may explain its distinct substrate specificity. - Source: PubMed
Publication date: 2025/05/30
Schroer LisaWeirich SaraHammerstad MartaHersleth Hans-PetterGrønsberg Ida AndriettaHagen LarsSlupphaug GeirMalecki Jedrzej MieczyslawJeltsch AlbertFalnes Pål ØDavydova Erna