Fibroblast growth factor inhibits MRF4 activity independently of the phosphorylation status of a conserved threonine residue within the DNA-binding domain

• Published in: Molecular and Cellular Biology Vol. 13; no. 10; pp. 5943 - 5956
• Main Authors: Hardy, S, Kong, Y, Konieczny, S F
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for Microbiology 01.10.1993
• Subjects: Amino Acid Sequence; Animals; Binding Sites; Biological and medical sciences; Cell differentiation, maturation, development, hematopoiesis; Cell Line; Cell physiology; Cloning, Molecular; Conserved Sequence; Cyclic AMP-Dependent Protein Kinases - metabolism; DNA - metabolism; Fibroblast Growth Factors - metabolism; Fundamental and applied biological sciences. Psychology; Humans; Mice; Molecular and cellular biology; Molecular Sequence Data; Mutation; Myogenic Regulatory Factors - antagonists & inhibitors; Myogenic Regulatory Factors - metabolism; Myogenin; Peptide Mapping; Phosphorylation; Protein Kinase C - metabolism; Rats; Sequence Homology, Amino Acid; Substrate Specificity; Threonine - metabolism; Transcription Factors - metabolism; Transcription, Genetic; Reaction inhibitor; Transcription factor MRF4; Phosphorylation; Protein kinase C; Enzyme; Transferases; DNA binding protein; Basic fibroblast growth factor; Cell differentiation; Myogenesis; Protein kinase; Mechanism of action; Growth factor

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