Mos Activates Myogenic Differentiation by Promoting Heterodimerization of MyoD and E12 Proteins

Lenormand, Jean-Luc; Benayoun, Béatrice; Guillier, Martine; Vandromme, Marie; Leibovitch, Marie-Pierre; Leibovitch, Serge A.

doi:10.1128/mcb.17.2.584

Cited by 32 publications

(41 citation statements)

References 57 publications

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“…First, activated Mos stimulates dimerization of MyoD and E12 and second, MyoD directly interacts with Mos, inhibiting downstream Mos-mediated activation of the MEK/MAPK pathway (205,206). These results suggest that alterations in the dimerization status of the MRFs are important levels of myogenic regulation.…”

Section: Functional Protein-protein Interactionsmentioning

confidence: 67%

Molecular mechanisms regulating myogenic determination and differentiation

Robert¹

2000

Front Biosci

293

236

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Section: Functional Protein-protein Interactionsmentioning

confidence: 67%

Molecular mechanisms regulating myogenic determination and differentiation

Robert¹

2000

Front Biosci

293

236

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“…Thus, MafA phosphorylation is likely to control the transactivating capacity of MafA per se. It could either modulate MafA's ability to interact with the basal transcription machinery or affect its capacity to interact with critical partners, as was demonstrated in the case of the MyoD transcription factor (37). Likewise, phosphorylation of JunB, on threonine 102 and threonine 104, by JNK was suggested to favor interaction with c-Maf dimers and to consequently elicit synergistic activation of the interleukin-4 promoter by both transcription factors (38).…”

Section: Discussionmentioning

confidence: 99%

“…Among these, Microphthalmia (19) and the Drosophila Yan and pointed P2 proteins of the Ets family (5) are phosphorylated by ERKs, c-Jun (21) and ATF2 (16) are phosphorylated by JNKs, and CHOP (63), Pax6 (41), and MEF2C (17) are phosphorylated by p38. Various functional consequences of phosphorylation on transcription factors have been observed, such as alteration of protein stability (43), cellular localization (8), DNA binding (64), interaction with partners (37), and transactivation capacity (3). Thus, phosphorylation cascades, elicited at the cellular membrane, have the potential to turn extracellular signals into specific and finely tuned nuclear responses.…”

mentioning

confidence: 99%

Phosphorylation of MafA Is Essential for Its Transcriptional and Biological Properties

Benkhelifa

Provot

Nabais

et al. 2001

Molecular and Cellular Biology

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We previously described the identification of quail MafA, a novel transcription factor of the Maf bZIP (basic region leucine zipper) family, expressed in the differentiating neuroretina (NR). In the present study, we provide the first evidence that MafA is phosphorylated and that its biological properties strongly rely upon phosphorylation of serines 14 and 65, two residues located in the transcriptional activating domain within a consensus for phosphorylation by mitogen-activated protein kinases and which are conserved among Maf proteins. These residues are phosphorylated by ERK2 but not by p38, JNK, and ERK5 in vitro. However, the contribution of the MEK/ERK pathway to MafA phosphorylation in vivo appears to be moderate, implicating another kinase. The integrity of serine 14 and serine 65 residues is required for transcriptional activity, since their mutation into alanine severely impairs MafA capacity to activate transcription. Furthermore, we show that the MafA S14A/S65A mutant displays reduced capacity to induce expression of QR1, an NR-specific target of Maf proteins. Likewise, the integrity of serines 14 and 65 is essential for the MafA ability to stimulate expression of crystallin genes in NR cells and to induce NR-to-lens transdifferentiation. Thus, the MafA capacity to induce differentiation programs is dependent on its phosphorylation.

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“…Immunoprecipitation was performed as previously described (Lenormand et al, 1997). Before immunoprecipitation, aliquots from each sample were loaded onto a 10% SDS ± PAGE and analysed by immunoblotting to test the expression of HA-tagged proteins (10 mg) and Flag-tagged proteins (30 mg) respectively.…”

Section: Immunoprecipitation and Immunoblottingmentioning

confidence: 99%

“…, cyclin D1, Cdk4 or cyclin D1-Cdk4 complexes were prepared by coupled in vitro transcriptiontranslation using the TnT coupled rabbit reticulocyte lysate system (Promega). GST pull-down assays were performed as described previously (Lenormand et al, 1997 proteins were removed by three wash cycles of binding buer. Then increasing amounts of labeled cyclin D1, Cdk4 or cotranslated cyclin D1-Cdk4 complexes were added to the binding reactions and the resulting mixtures were subjected to a GST pull-down assay.…”

Section: Kip2mentioning

confidence: 99%