The Ras-MAPK signal transduction pathway, cancer and chromatin remodeling

2005 ◽  
Vol 83 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Katherine L Dunn ◽  
Paula S Espino ◽  
Bojan Drobic ◽  
Shihua He ◽  
James R Davie
Keyword(s):  
Breast Cancer ◽  
Signal Transduction ◽  
Chromatin Remodeling ◽  
Mapk Pathway ◽  
Histone H3 ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Transduction Pathway ◽  
H3 Phosphorylation ◽  
Mitogen Activated Protein

Stimulation of the Ras-mitogen-activated protein kinase (MAPK) signal transduction pathway results in a multitude of events including expression of the immediate-early genes, c-fos and c-myc. Downstream targets of this stimulated pathway are the mitogen- and stress-activated protein kinases (MSK) 1 and 2, which are histone H3 kinases. In chromatin immunoprecipitation assays, it has been shown that the mitogen-induced phosphorylated H3 is associated with the immediate-early genes and that MSK1/2 activity and H3 phosphorylation have roles in chromatin remodeling and transcription of these genes. In oncogene-transformed fibroblasts in which the Ras-MAPK pathway is constitutively active, histone H1 and H3 phosphorylation is increased and the chromatin of these cells has a more relaxed structure than the parental cells. In this review we explore the deregulation of the Ras-MAPK pathway in cancer, with an emphasis on breast cancer. We discuss the features of MSK1 and 2 and the impact of a constitutively activated Ras-MAPK pathway on chromatin remodeling and gene expression.Key words: Ras, mitogen-activated protein kinase signal transduction pathway, histone H3 phosphorylation, MSK1, breast cancer.

Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes

1993 ◽  
Vol 13 (9) ◽  
pp. 5659-5669 ◽  
Author(s):  
M Tyers ◽  
B Futcher
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
G1 Phase ◽  
Transduction Pathway ◽  
Yeast Saccharomyces Cerevisiae ◽  
Alpha Factor ◽  
Mitogen Activated Protein

In the yeast Saccharomyces cerevisiae, the Cdc28 protein kinase controls commitment to cell division at Start, but no biologically relevant G1-phase substrates have been identified. We have studied the kinase complexes formed between Cdc28 and each of the G1 cyclins Cln1, Cln2, and Cln3. Each complex has a specific array of coprecipitated in vitro substrates. We identify one of these as Far1, a protein required for pheromone-induced arrest at Start. Treatment with alpha-factor induces a preferential association and/or phosphorylation of Far1 by the Cln1, Cln2, and Cln3 kinase complexes. This induced interaction depends upon the Fus3 protein kinase, a mitogen-activated protein kinase homolog that functions near the bottom of the alpha-factor signal transduction pathway. Thus, we trace a path through which a mitogen-activated protein kinase regulates a Cdc2 kinase.

scholarly journals Enteropathogenic Escherichia coli Infection Induces Expression of the Early Growth Response Factor by Activating Mitogen-Activated Protein Kinase Cascades in Epithelial Cells

2001 ◽  
Vol 69 (10) ◽  
pp. 6217-6224 ◽  
Author(s):  
Myriam de Grado ◽  
Carrie M. Rosenberger ◽  
Annick Gauthier ◽  
Bruce A. Vallance ◽  
B. Brett Finlay
Keyword(s):  
Signal Transduction ◽  
Type Iii Secretion ◽  
Growth Response ◽  
Signal Transduction Pathway ◽  
Early Growth ◽  
Secretion System ◽  
Mitogen Activated Protein Kinase ◽  
Transduction Pathway ◽  
Early Growth Response ◽  
Mitogen Activated Protein

ABSTRACT Enteropathogenic Escherichia coli (EPEC) is an extracellular bacterial pathogen that infects the human intestinal epithelium and is a major cause of infantile diarrhea in developing countries. EPEC belongs to the group of attaching and effacing (A/E) pathogens. It uses a type III secretion system to deliver proteins into the host cell that mediate signal transduction events in host cells. We used gene array technology to study epithelial cell responses to EPEC infection at the level of gene expression. We found that EPEC induces the expression of several genes in infected HeLa cells by a lipopolysaccharide (LPS)-independent mechanism, including cytokines and early growth response factor 1 (Egr-1). The transcription factor Egr-1 is an immediate-early-induced gene that is activated in most cell types in response to stress. EPEC-induced upregulation ofegr-1 is mediated by the activation of the MEK/extracellular signal-regulated kinase signal transduction pathway and is dependent on the type III secretion system. egr-1 is also induced during infection of mice by the A/E pathogenCitrobacter rodentium, suggesting that both Egr-1 and the activation of this mitogen-activated protein kinase signal transduction pathway may play a role in disease.

Clozapine and the mitogen-activated protein kinase signal transduction pathway: Implications for antipsychotic actions

2005 ◽  
Vol 57 (6) ◽  
pp. 617-623 ◽  
Author(s):  
Jeff L. Browning ◽  
Tushar Patel ◽  
Paul C. Brandt ◽  
Keith A. Young ◽  
Leigh A. Holcomb ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Transduction Pathway ◽  
Mitogen Activated Protein
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