Phosphorylation inhibits the DNA-binding activity of MyoD homodimers but not MyoD-E12 heterodimers.
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منابع مشابه
Phosphorylation inhibits the DNA-binding activity of MyoD homodimers but not MyoD-E12 heterodimers.
MyoD is a member of the basic helix-loop-helix (bHLH) family of muscle gene regulatory proteins that includes myogenin, myf-5, and MRF4. These proteins have been shown to heterodimerize with E2A bHLH proteins, E12/E47, and to bind to a consensus sequence known as an E-box, CANNTG, the target for transcriptional activation by these myogenic regulators. MyoD is also a phosphorylated nuclear prote...
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MyoD is a nuclear phosphoprotein that belongs to the family of myogenic regulatory factors and acts in the transcriptional activation of muscle-specific genes. We have investigated the role of cAMP-dependent protein kinase (A-kinase) in modulating the nuclear locale of MyoD. Purified MyoD protein microinjected into the cytoplasm of rat embryo fibroblasts is rapidly translocated into the nucleus...
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The members of the MyoD family of basic helix-loop-helix (bHLH) transcription factors are critical regulators of skeletal muscle differentiation that function as heterodimers with ubiquitously expressed E-protein bHLH transcription factors. These heterodimers must compete successfully with homodimers of E12 and other E-proteins to enable myogenesis. Here, we show that E12 mutants resistant to C...
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Smooth muscle cells (SMCs) have evolved to subserve a variety of diverse functions in higher vertebrates, including modulation of arterial tone, regulation of airway resistance, and control of gastrointestinal motility. The diverse functional capacities of SMCs are ultimately determined by the expression of genes encoding SMC-restricted contractile and cytoskeletal proteins, intracellular enzym...
متن کاملAnalysis of the inhibition of MyoD activity by ITF-2B and full-length E12/E47.
MyoD heterodimerizes with E type factors (E12/E47 and ITF-2A/ITF-2B) and binds E box sequences within promoters of muscle-specific genes. In transient transfection assays, MyoD activates transcription in the presence of ITF-2A but not ITF-2B, which contains a 182-amino acid N-terminal extension. The first 83 amino acids of the inhibitory N terminus of ITF-2B show high sequence homology to the N...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)80541-9