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Wright WE, Li C, Zheng CX, et al. FOXP1 Interacts with MyoD to Repress its Transcription and Myoblast Conversion. J Cell Signal. 2021;2(1):9-26
Wright, W. E., Li, C., Zheng, C. X., & Tucker, H. O. (2021). FOXP1 Interacts with MyoD to Repress its Transcription and Myoblast Conversion. Journal of cellular signaling, 2(1), 9-26.
Wright, Woodring E, et al. "FOXP1 Interacts with MyoD to Repress its Transcription and Myoblast Conversion." Journal of cellular signaling vol. 2,1 (2021): 9-26.
Wright WE, Li C, Zheng CX, Tucker HO. FOXP1 Interacts with MyoD to Repress its Transcription and Myoblast Conversion. J Cell Signal. 2021;2(1):9-26. PMID: 33554216; PMCID: PMC7861563.
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J Cell Signal. 2021;2(1):9-26.

FOXP1 Interacts with MyoD to Repress its Transcription and Myoblast Conversion.

Journal of cellular signaling

Woodring E Wright, Chuan Li, Chang-Xue Zheng, Haley O Tucker

Affiliations

  1. Department of Cell Biology, UT Southwestern Medical School, Dallas TX 75235, USA.
  2. Department of Microbiology, University of Texas Southwestern Medical Center, Dallas TX 75235, USA.
  3. Department of Molecular Biosciences, the University of Texas at Austin, Austin TX 78712, USA.

PMID: 33554216 PMCID: PMC7861563

Abstract

Forkhead transcription factors (TFs) often dimerize outside their extensive family, whereas bHLH transcription factors typically dimerize with E12/E47. Based on structural similarities, we predicted that a member of the former, Forkhead Box P1 (FOXP1), might heterodimerize with a member of the latter, MYOD1 (MyoD). Data shown here support this hypothesis and further demonstrate the specificity of this forkhead/myogenic interaction among other myogenic regulatory factors. We found that FOXP1-MyoD heterodimerization compromises the ability of MyoD to bind to E-boxes and to transactivate E box- containing promoters. We observed that FOXP1 is required for the full ability of MyoD to convert fibroblasts into myotubules. We provide a model in which FOXP1 displaces ID and E12/E47 to repress MyoD during the proliferative phase of myoblast differentiation. These data identify FOXP1 as a hitherto unsuspected transcriptional repressor of MyoD. We suggest that isolation of paired E-box and forkhead sites within 1 turn helical spacings provides potential for cooperative interactions among heretofore distinct classes of transcription factors.

Keywords: Forkhead box P1; Myoblast differentiation; Myogenic regulatory factors; Transcriptional regulation

Conflict of interest statement

Competing Financial Interests The authors declare no competing financial interests.

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