DDIT3 Research Reagents

DNA damage-inducible transcript 3 protein is a protein in humans that is encoded by DDIT3 gene. Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription

The following DDIT3 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

DDIT3 Antibodies

DDIT3 Antibodies for Homo sapiens (Human)

DDIT3 Proteins

DDIT3 Proteins for Homo sapiens (Human)

DDIT3 Proteins for Mus musculus (Mouse)

DDIT3 Proteins for Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

DDIT3 Proteins for Bos taurus (Bovine)

DDIT3 Proteins for Rattus norvegicus (Rat)

DDIT3 Background

DNA damage-inducible transcript 3 (DDIT3), also called C/EBP homologous protein (CHOP), is an endoplasmic reticulum (ER) stress-inducible protein that belongs to a member of the CCAAT/enhancer-binding protein (C/EBP) family of DNA-binding transcription factors [1][2]. DDIT3/CHOP functions as a multifunctional transcription factor that contributes to cellular functions, including apoptosis, autophagy, inflammation, cell differentiation, and proliferation. DDIT3/CHOP possesses N-terminal transcriptional activation/repression domains necessary for its proteasomal degradation and a C-terminal basic-leucine zipper (bZIP) domain, including a basic region for DNA binding and a leucine zipper motif for dimerization [3]. A serine/threonine-rich motif in the transactivation domain of DDIT3/CHOP can be recognized by speckle-type POZ protein (SPOP), which triggers DDIT3/CHOP degradation via the ubiquitin-proteasome pathway [4]. TRB3 antagonized p300 binding to CHOP via its N-terminal domain [5]. Degradation of CHOP protein through the N-terminal domain was inhibited by treatment with trichostatin A (TSA) [5]. During ER stress, CHOP is mainly induced via activation of the PERK (ER-localized kinase double-stranded RNA-activated protein kinase (PKR)-like ER kinase) through the downstream phosphorylation of a translation initiation factor, eukaryotic initiation factor 2α (eIF2α), and induction of a transcription factor, activation transcription factor 4 (ATF4) [6]. Apoptosis ensues by ATF4-CHOP-mediated induction of several pro-apoptotic genes and suppression of the synthesis of anti-apoptotic Bcl-2 proteins [7]. Also, Oyadomari, S. and Mori, M. demonstrated that CHOP-mediated apoptosis during ER stress is involved in diseases with ER stress-dependent cell death, such as neurodegenerative disease and/or type I diabetes [8]. During amino acid limitation and ER stress, CHOP binds to the promoters of a set of autophagy genes [9]. WafaB'chir and his colleagues showed that during the first 6 h of starvation, CHOP upregulates numerous autophagy genes but is not involved in the first steps of the autophagic process. When the amino acid starvation is prolonged (16–48 h), CHOP exhibits a dual role in both inducing apoptosis and limiting autophagy through the transcriptional control of specific genes [10]. CHOP is also implicated in adipogenesis and erythropoiesis.

[1] Fornace, A. J., Nebert, D. et al. Mammalian genes coordinately regulated by growth arrest signals and DNA-damaging agents [J]. Mol. Cell. Biol. 1989, 9, 4196–4203.
[2] Lekstrom-Himes J. and Xanthopoulos K. G. Biological role of the CCAAT/enhancer-binding protein family of transcription factors [J]. J. Biol. Chem. 1998, 273, 28545–28548.
[3] Ubeda M, Wang XZ, et al. Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element [J]. Molecular and Cellular Biology. 1996, 16 (4): 1479–89.
[4] Zhang P, Gao K, et al. Destruction of DDIT3/CHOP protein by wild-type SPOP but not prostate cancer-associated mutants [J]. Hum Mutat (2014) 35(9):1142–51.
[5] Nobumichi Ohoka, Takayuki Hattori, et al. Critical and Functional Regulation of CHOP (C/EBP Homologous Protein) through the N-terminal Portion [J]. The Journal of Biological Chemistry 2007, 282, 35687-35694.
[6] Harding, H. P., Novoa, I., et al. Regulated translation initiation controls stress-induced gene expression in mammalian ce[J]. Mol. Cell 200o, 6, 1099–1108.
[7] W Rozpedek, D Pytel, et al. The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress [J]. Curr Mol Med, 2016, 16 (6), 533-44.
[8] Oyadomari, S., and Mori, M. Roles of CHOP/GADD153 in endoplasmic reticulum stress[J]. Cell Death Differ. 2004, 11, 381–389.
[9] B’Chir W, Maurin AC, et al. The eIF2alpha/ATF4 pathway is essential for stress-induced autophagy gene expression [J]. Nucleic Acids Res (2013) 41(16):7683–99.
[10] WafaB'chir, Cédric Chaveroux, et al. Dual role for CHOP in the crosstalk between autophagy and apoptosis to determine cell fate in response to amino acid deprivation [J]. Volume 26, Issue 7, July 2014, Pages 1385-1391.

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