Coupling of the RAS-MAPK Pathway to Gene Activation by RSK2, a Growth Factor-Regulated CREB Kinase
@article{Xing1996CouplingOT, title={Coupling of the RAS-MAPK Pathway to Gene Activation by RSK2, a Growth Factor-Regulated CREB Kinase}, author={Jun Xing and David D. Ginty and Michael Eldon Greenberg}, journal={Science}, year={1996}, volume={273}, pages={959 - 963} }
A signaling pathway has been elucidated whereby growth factors activate the transcription factor cyclic adenosine monophosphate response element-binding protein (CREB), a critical regulator of immediate early gene transcription. Growth factor-stimulated CREB phosphorylation at serine-133 is mediated by the RAS-mitogen-activated protein kinase (MAPK) pathway. MAPK activates CREB kinase, which in turn phosphorylates and activates CREB. Purification, sequencing, and biochemical characterization of…
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References
SHOWING 1-10 OF 38 REFERENCES
Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB
- BiologyCell
- 1994
Nuclear localization and regulation of erk- and rsk-encoded protein kinases.
- BiologyMolecular and cellular biology
- 1992
In vitro studies raise the possibility that the MAP kinase/RSK signal transduction pathway represents a protein-Tyr/Ser/Thr phosphorylation cascade with the spatial distribution and temporal regulation that can account for the rapid transmission of growth-regulating information from the membrane, through the cytoplasm, and to the nucleus.
A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity
- Biology, ChemistryMolecular and cellular biology
- 1993
A model in which the growth factor-induced phosphorylation of SRF contributes to the activation of c-fos transcription by facilitating the formation of an active transcription complex at the serum response element is suggested.
Serine 133-Phosphorylated CREB Induces Transcription via a Cooperative Mechanism That May Confer Specificity to Neurotrophin Signals
- BiologyMolecular and Cellular Neuroscience
- 1995
Results indicate that CREB is a versatile transcription factor that activates transcription via distinct mechanisms in a stimulus-specific manner and that by selectively activating delayed response genes, CREB may confer specificity to neurotrophin signals that promote the survival and differentiation of neurons.
Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1993
Evidence is provided that two growth-regulated, nucleus- and cytoplasm-localized protein kinases, 90-kDa ribosomal S6 kinase (RSK and MAP kinase), contribute to the serum-induced phosphorylation of c-Fos.
Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter
- BiologyNature
- 1992
It is shown that p62TCF is phosphorylated by MAP kinase in vitro and that phosphorylation results in enhanced ternary complex formation, linking the expression of the human c-fos proto-oncogene to signal transduction pathways known to be activated before its own induction.
The MAPK signaling cascade
- BiologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
- 1995
This review highlights primarily the first MAPK cascade to be discovered that uses the MEK and ERK isoforms and describes their involvement in different cellular processes, and it is now known that signaling pathways initiated by phorbol esters, iono‐phors, heat shock, and liganda for seven transmembrane receptors use distinct MAPK cascades with little or no cross‐reactivity between them.
Activation of ternary complex factor Elk‐1 by MAP kinases.
- BiologyThe EMBO journal
- 1993
It is demonstrated that recombinant Elk‐1 is hyperphosphorylated in vivo upon joint overexpression ofMAPKs and constitutively activated Raf‐1 kinase, the latter serving as an indirect in vivo activator of MAPKs.
The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain
- BiologyCell
- 1993
Calcium activates serum response factor-dependent transcription by a Ras- and Elk-1-independent mechanism that involves a Ca2+/calmodulin-dependent kinase
- BiologyMolecular and cellular biology
- 1995
Findings indicate that SRF is a versatile transcription factor that, when bound to the SRE, can function by distinct mechanisms and can mediate transcriptional responses to both CaMK- and Ras-dependent signaling pathways.