Transcriptional regulation by MAP kinases

  title={Transcriptional regulation by MAP kinases},
  author={Roger J. Davis},
  journal={Molecular Reproduction and Development},
  • R. Davis
  • Published 1 December 1995
  • Biology, Computer Science
  • Molecular Reproduction and Development
Tyrosine kinase growth factor receptors activate MAP kinase by a complex mechanism involving the SH2/3 protein Grb2, the exchange protein Sos, and Ras. The GTP‐bound Ras protein binds to the Raf kinase and initiates a protein kinase cascade that leads to MAP kinase activation. Three MAP kinase kinase kinases have been described‐c‐Raf, c‐Mos, and Mekk—that phosphorylate and activate Mek, the MAP kinase kinase. Activated Mek phosphorylates and activates MAP kinase. Subsequently, the activated MAP… 
The Regulation of MAP Kinase Pathways by MAP Kinase Phosphatases
Mitogen activated protein (MAP) kinase signal transduction pathways are evolutionary conserved protein modules that play a central role in conveying information from the extracellular environment
Activation and signal transduction via mitogen‐activated protein (MAP) kinases in T lymphocytes
This review examines how the activation of several MAP kinases is regulated, their role in signal transduction initiated by a variety of stimuli, and how this may lead to different cellular responses.
Mitogen-activated protein kinases and apoptosis in PIN
Overexpression of the three MAP kinases and MKP-1 mRNA was found in all cases of high-grade PIN compared with normal prostate, and this results are consistent with the previous demonstration of preferential inhibition of the apoptosis-related kinases by MKp-1 and further support the contention that MKPs, even in PIN, may shift the balance existing between cell proliferation and death.
MEKK-1, a Component of the Stress (Stress-activated Protein Kinase/c-Jun N-terminal Kinase) Pathway, Can Selectively Activate Smad2-mediated Transcriptional Activation in Endothelial Cells*
A novel mechanism for activation of Smad protein-mediated signaling in endothelial cells is demonstrated and it is suggested that Smad2 may act as an integrator of diverse stimuli in these cells.
MAP kinase signaling cascades and gene expression in osteoblasts.
This work discusses in detail the nature and activation of the mitogen-activated protein kinase pathways, how they induce c-fos expression and how these MAPK cascades can differentially regulate the activity of AP-1 and thereby osteoblast-specific gene expression.
The Ras-Raf-MEK-ERK Pathway in the Treatment of Cancer
This review addresses the rationale for targeting the MAP kinase pathway and the current status of various pharmacological approaches and a number of drugs inhibiting Ras, Raf or MEK are currently under clinical investigation.
Discordance between the Binding Affinity of Mitogen-activated Protein Kinase Subfamily Members for MAP Kinase Phosphatase-2 and Their Ability to Activate the Phosphatase Catalytically*
This report found that the catalytic activity of MKP-2 was enhanced dramatically by ERK and JNK but was affected only minimally by p38, and provided a mechanistic explanation for the substrate preference of MKp-2 and suggest that catalytic activation of MKF2 upon binding to its substrates is crucial for its function.
Role of mitogen-activated protein kinase in cardiac hypertrophy and heart failure.
The activation of ERK1/2 is involved in signal transduction pathways associated with cardiac hypertrophy; however, the exact status of MAPKs in heart failure remains to be clearly defined.
Big Mitogen-activated Kinase Regulates Multiple Members of the MEF2 Protein Family*
It is demonstrated that, upon growth factor induction, BMK1 directly phosphorylates and activates three members of theMEF2 family of transcription factors thereby inducing MEF2-dependent gene expression.
Uncoupling of Hepatic, Epidermal Growth Factor-mediated Mitogen-activated Protein Kinase Activation in the Fetal Rat*
In studies using primary cultures of E19 fetal rat hepatocytes, uncoupling of MAP kinase activation from MEK activation could be induced by incubation of fetal hepatocytes for 24 h with a potent fetal hepatocyte mitogen, transforming growth factor-α.


Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1
Several lines of evidence are presented indicating that PAC1 is a physiologically relevant MAP kinase phosphatase, and that Recombinant PAC1 in vitro is a dual-specific Thr/Tyr phosphat enzyme with stringent substrate specificity for MAP kinases.
Phosphorylation of c-jun mediated by MAP kinases
Evidence is presented that mitogen-activated protein-serine (MAP) kinases (pp54 and pp42/44) specifically phosphorylate these sites and that their phosphorylation positively regulates the transacting activity of c-jun.
Genomic loci of human mitogen-activated protein kinases.
Mitogen-activated protein (MAP) kinases [also known as Erks] have been established to function as important mediators of signal transduction by growth factor receptors. Several components of the MAP
Activation of cAMP and mitogen responsive genes relies on a common nuclear factor
It is reported here that micro-injection of an anti-CBP antiserum into fibroblasts can inhibit transcription from a cAMP responsive promoter, and proposed that CBP is recruited to the promoter through interaction with certain phosphorylated factors, and may thus play a critical role in the transmission of inductive signals from cell surface receptor to the transcriptional apparatus.
Signal transduction by tumor necrosis factor mediated by JNK protein kinases.
Data indicate a role for the JNK group of protein kinases in the signal transduction pathway initiated by proinflammatory cytokines and UV radiation.
SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins.
Observations suggest that SH2 and SH3 domains participate in the control of intracellular responses to growth factor stimulation.
Transcription factor ATF2 regulation by the JNK signal transduction pathway
A role for the JNK signal transduction pathway in transcriptional responses mediated by ATF2 is demonstrated and mutations in this pathway inhibited ATF2-stimulated gene expression mediated by the retinoblastoma tumor suppressor and the adenovirus early region 1A (E1A) oncoprotein.
Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73
Site-directed mutagenesis indicates that phosphorylation of these serines is essential for stimulation of c-Jun activity and for cooperation with Ha-ras in ocogenic transformation.