Abstract
A mechanism by which the nerve growth factor (NGF) signal is transduced to the nucleus to induce gene expression has been characterized. An NGF-inducible, Ras-dependent protein kinase has been identified that catalyzes the phosphorylation of the cyclic AMP response element-binding protein (CREB) at Ser-133. Phosphorylation of Ser-133 stimulates the ability of CREB to activate transcription in NGF-treated cells. These findings suggest that CREB has a more widespread function than previously believed and functions in the nucleus as a general mediator of growth factor responses.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Cell Line
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Cyclic AMP Response Element-Binding Protein / metabolism*
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Enzyme Activation / drug effects
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GTPase-Activating Proteins
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Genes, fos* / drug effects
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Mice
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Nerve Growth Factors / pharmacology*
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Phosphorylation
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Protein Kinases / metabolism*
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Proteins / metabolism
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Rats
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Signal Transduction / drug effects
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Transcription, Genetic / drug effects
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ras GTPase-Activating Proteins
Substances
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Cyclic AMP Response Element-Binding Protein
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GTPase-Activating Proteins
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Nerve Growth Factors
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Proteins
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ras GTPase-Activating Proteins
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Protein Kinases