Increase in p202 Expression during Skeletal Muscle Differentiation: Inhibition of MyoD Protein Expression and Activity by p202

Datta, Bansidhar; Wang, Min; Burma, Sandeep; Lengyel, Péter

doi:10.1128/mcb.18.2.1074

Cited by 87 publications

(109 citation statements)

References 73 publications

(102 reference statements)

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“…Binding of p202 to these proteins results in a loss of their transcriptional regulatory activities and inhibits the binding of E2F and AP-1 to speci®c DNA elements (Min et al, 1996;Choubey et al, 1996;Choubey and Gutterman, 1997). Expression of p202 correlated with a decrease in endogenous levels of MyoD RNA and with a loss of transcriptional activity mediated by transfected MyoD (Datta et al, 1998). The manner by which p202 regulates transactivation mediated by NF-kB, p53 and transfected MyoD has not yet been determined.…”

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confidence: 99%

“…Some members of the family have been demonstrated to modulate transcription and the best studied protein to date is p202 which can bind to a number of transcription factors including NF-kB (Min et al, 1996), AP-1 (c-Jun/c-Fos) (Min et al, 1996), MyoD (Datta et al, 1998), p53 (via its interaction with p53-binding protein 1 (p53bp)) and E2F (E2F-1/DP-1, E2F-4/DP-1) Choubey and Gutterman, 1997). Binding of p202 to these proteins results in a loss of their transcriptional regulatory activities and inhibits the binding of E2F and AP-1 to speci®c DNA elements (Min et al, 1996;Choubey et al, 1996;Choubey and Gutterman, 1997).…”

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Functional interaction between p53 and the interferon-inducible nucleoprotein IFI 16

et al. 2000

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Functional interaction between p53 and the interferon-inducible nucleoprotein IFI 16

et al. 2000

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“…Lowering the concentration of serum in the medium results in the increase in the level of p202a in fibroblasts (21). p202a is also induced during skeletal muscle differentiation in consequence of transactivation of the Ifi202a gene by the muscle-specific MyoD transcription factor (16,22). p202a can modulate during this process the activity of the muscle-specific transcription factors MyoD and myogenin, and it also inhibits apoptosis (16,17).…”

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confidence: 99%

“…This inhibitory effect can be correlated with the binding and inhibition of the activity of several transcription factors by p202a. These include c-Fos, c-Jun, AP2, E2F1, E2F4, MyoD, myogenin, cMyc, and NF-B (13)(14)(15)(16)(17). p202a also binds pRb (12) and inhibits the activity of p53 (18).…”

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The Interferon-inducible p202a Protein Modulates NF-κB Activity by Inhibiting the Binding to DNA of p50/p65 Heterodimers and p65 Homodimers While Enhancing the Binding of p50 Homodimers

Wang

Ding

et al. 2003

Journal of Biological Chemistry

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p202a is a member of the interferon-inducible murine p200 family of proteins. These proteins share 1 or 2 partially conserved 200 amino acid segments of the a or the b type. The known biological activities of p202a include among others the regulation of muscle differentiation, cell proliferation, and apoptosis. These biological activities of p202a can be correlated with the inhibition of the activity of several transcription factors. Thus, the binding of p202a results in the inhibition of the sequence-specific binding to DNA of the c-Fos, c-Jun, E2F1, E2F4, MyoD, myogenin, and c-Myc transcription factors. This study concerns the mechanisms by which p202a inhibits the activity of NF-B, a transcription factor involved among others in host defense, inflammation, immunity, and the apoptotic response. NF-B consists of p50 and p65 subunits. We demonstrate that p202a can inhibit in vitro and in vivo the binding to DNA of p65 homodimers and p50/65 heterodimers, whereas it increases the binding of p50 homodimers. Thus p202a can impair NF-B activity both by inhibiting the binding to DNA of the transcriptionally active p65 homodimers and p50/p65 heterodimers and by boosting the binding of the repressive p50 homodimers. p202a can bind p50 and p65 in vitro and in vivo, and p202a can be part of the p50 homodimer complex bound to DNA. p50 binds in p202a to the a type segment, whereas p65 binds to the b type segment. Transfected ectopic p202a increases the apoptotic effect of tumor necrosis factor (at least in part) by inhibiting NF-B and its antiapoptotic activity.

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“…In addition to E2F (E2F-1 and E2F-4), p202 also modulates the transcriptional activity of c-Myc (Wang et al, 2000), AP-1 (c-Fos and c-Jun; Min et al, 1996), NF-kB (p50 and p65; Min et al, 1996), p53 , MyoD, and myogenin (Datta et al, 1998). Therefore, it is likely that the binding of E1A to p202 also a ects p202's ability to modulate the activities of these factors.…”

Section: Discussionmentioning

confidence: 99%

p202, an interferon-inducible negative regulator of cell growth, is a target of the adenovirus E1A protein

et al. 2001

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Studies have revealed that human adenovirus-encoded E1A protein promotes cell proliferation through the targeted interaction with cellular proteins that act as key negative regulators of cell growth. The targets of E1A protein include the retinoblastoma tumor suppressor protein (pRb). Because p202, an interferon (IFN)-inducible murine protein (52-kDa), negatively regulates cell growth in part through the pRb/E2F pathway, we tested whether the p202 is a target of the adenovirusencoded E1A protein for functional inactivation. Here we report that the expression of E1A protein overcame p202-mediated inhibition of cell growth and this correlated with an alleviation of p202-mediated inhibition of the transcriptional activity of E2F. Furthermore, E1A protein relieved p202-mediated inhibition of the speci®c DNA-binding activity of E2F complexes, including those containing the pocket proteins. Additionally, the E1A protein bound to p202 both in vitro and in vivo and a deletion of four amino acids in the conserved region 2 (CR2) of E1A protein signi®cantly reduced the binding of E1A to p202. Interestingly, ectopic expression of p202 under reduced serum conditions signi®cantly reduced E1A-mediated apoptosis. Taken together, our observations provide support to the idea that the p202 and adenovirus E1A protein functionally counteract each other and E1A protein targets p202 to promote cell proliferation. Oncogene (2001) 20, 6828 ± 6839.

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Increase in p202 Expression during Skeletal Muscle Differentiation: Inhibition of MyoD Protein Expression and Activity by p202

Cited by 87 publications

References 73 publications

Functional interaction between p53 and the interferon-inducible nucleoprotein IFI 16

Functional interaction between p53 and the interferon-inducible nucleoprotein IFI 16

The Interferon-inducible p202a Protein Modulates NF-κB Activity by Inhibiting the Binding to DNA of p50/p65 Heterodimers and p65 Homodimers While Enhancing the Binding of p50 Homodimers

p202, an interferon-inducible negative regulator of cell growth, is a target of the adenovirus E1A protein

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