Functional antagonism between c-Jun and MyoD proteins: a direct physical association
E Bengal, L Ransone, R Scharfmann, VJ Dwarki… - Cell, 1992 - cell.com
Cell, 1992•cell.com
The product of the proto-oncogene Jun inhibits myogenesis. Constitutive expression of Jun
in myoblasts interferes with the expression and the function of MyoD protein. In transient
transfection assays Jun inhibits transactivation of the MyoD promoter, the muscle creatine
kinase enhancer, and a reporter gene linked to MyoD DNA-binding sites. Conversely, MyoD
suppresses the transactivation by Jun of genes linked to an AP-1 site. We demonstrate that
both in vivo and in vitro MyoD and Jun proteins physically interact. Mutational analysis …
in myoblasts interferes with the expression and the function of MyoD protein. In transient
transfection assays Jun inhibits transactivation of the MyoD promoter, the muscle creatine
kinase enhancer, and a reporter gene linked to MyoD DNA-binding sites. Conversely, MyoD
suppresses the transactivation by Jun of genes linked to an AP-1 site. We demonstrate that
both in vivo and in vitro MyoD and Jun proteins physically interact. Mutational analysis …
Summary
The product of the proto-oncogene Jun inhibits myogenesis. Constitutive expression of Jun in myoblasts interferes with the expression and the function of MyoD protein. In transient transfection assays Jun inhibits transactivation of the MyoD promoter, the muscle creatine kinase enhancer, and a reporter gene linked to MyoD DNA-binding sites. Conversely, MyoD suppresses the transactivation by Jun of genes linked to an AP-1 site. We demonstrate that both in vivo and in vitro MyoD and Jun proteins physically interact. Mutational analysis suggests that this interaction occurs via the leucine zipper domain of Jun and the helix-loop-helix region of MyoD.
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