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Jun dimerization protein 2, known as JDP2, a member of the AP-1 family, is an inhibitor of such acetylation and contributes to the maintenance of chromatin structure. Furthermore, JDP2 is a novel member of the basic leucine zipper family of transcription factors. Some reports show that JDP2 binds DNA as a homodimer and heterodimer with ATF2 and Jun proteins but not with c-Fos proteins. JDP2 was the first time isolated on the basis of its ability to interact specifically with the AP-1 transcription factor c-Jun. In fact, JDP2 is a relatively small (163 amino acids), ubiquitously expressed bZIP protein that can form stable heterodimers with c-Jun, JunB, or JunD, and it functions as a repressor of c-Jun and the c-Jun/c-Fos heterodimer. JDP2 also interacts with ATF-2 both in vitro and in vivo via its bZIP domain and binds to the cyclic AMP response element to repress the cyclic AMP response element-dependent transcription that is mediated by ATF-2. Some reports show that JDP2 is an inhibitory subunit of the DRF complex.
The overexpression of JDP2 inhibits the transactivation of the c-jun gene by ATF-2 and p300 by recruitment of the histone deacetylase 3 (HDAC3) complex, thereby inhibiting the RA-induced transcription of the c-jun gene and inhibiting the RA-mediated differentiation of F9 cells. Moreover, JDP2 is a bona fide substrate for the c-Jun N-terminal kinase. JDP2 is a direct substrate of JNK. Overexpression of JDP2 leads to increased cell viability following ER stress and counteracts CHOP10 proapoptotic activity. Some studies indicate that JDP2 expression may determine the threshold for cell sensitivity to ER stress. JDP2 may function as an oncogene. JDP2 is ubiquitously expressed and its level remains unaltered following various stimuli.
JDP2 plays a key role as aninhibitor of adipocyte differentiation by regulating the expression of the gene for C/EBPd via inhibition of histone acetylation. JDP2 is associated with all such processes as an AP-1 repressor and, indeed, an inhibitory role for JDP2 in the regulation of UV-induced apoptosis via suppression of the expression of p53 was reported recently. JDP2 specifically repressed the DRE-dependent transcription of the reporter construct that was mediated by ATF-2 and p300. JDP2 suppresses the RA-dependent transcription of the cjun gene. JDP2 functions in an HDAC-dependent manner. Some reports show that the C/EBPd gene might be a target of JDP2. JDP2 is physically and functionally associated with HDAC3. JDP2 inhibits the RA-induced differentiation of F9 cells. The leucine zipper domain of CHOP10 is necessary for its association with JDP2, and the basic region of CHOP10 plays a role in mediating the binding of the complex to the TRE DNA sequences. JDP2 counteracts the pro-apoptotic activity of CHOP10 and thus provides increased cell resistance to endoplasmic reticulum (ER) stress. Ectopic expression of JDP2 in rhabdomyosarcoma cells induces myogenesis and the formation of incomplete myotubes. JDP2 might play multiple roles in the initial steps in the differentiation of cells. Some studies indicate that JDP2 has histone-chaperone activity and participates in nucleosome assembly in vitro. JDP2 can act directly to inhibit the histone acetyltransferase (HAT) activity induced by p300 in undifferentiated F9 cells and that it induces chromatin assembly.