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The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
MAP kinase pathways.
- D. Morrison
- BiologyCold Spring Harbor perspectives in biology
- 1 November 2012
MAP kinases are activated within protein kinase cascades that regulate cell proliferation, differentiation, and death and are grouped into three families: ERKs, JNKs, and p38/SAPKs.
Regulation of Raf-1 by direct feedback phosphorylation.
Integrating signals from RTKs to ERK/MAPK
Signals received at the cell surface must be properly transmitted to critical targets within the cell to achieve the appropriate biological response. This process of signal transduction is often…
Protein Phosphatase 2A Positively Regulates Ras Signaling by Dephosphorylating KSR1 and Raf-1 on Critical 14-3-3 Binding Sites
Regulation of MAP kinase signaling modules by scaffold proteins in mammals.
The evidence that supports a physiologically relevant role of MAPK scaffold proteins in mammals is critically evaluated.
Comparative genomics of the eukaryotes.
The fly has orthologs to 177 of the 289 human disease genes examined and provides the foundation for rapid analysis of some of the basic processes involved in human disease.
Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
It is demonstrated that maturation of the tyrosine phosphorylation sites can dramatically alter the function of Raf-1 and this is the first report that a transforming Raf- 1 protein can be generated by a single amino acid substitution.
Phosphatidylinositol 3-kinase regulates Raf1 through Pak phosphorylation of serine 338
Unlocking the code of 14-3-3
Recent studies now indicate that the serine/threonine protein phosphatases PP1 and PP2A are important regulators of 14-3-3 binding interactions, and demonstrate a role for 14- 3-3 in controlling the translocation of certain proteins from the cytoplasmic and endoplasmic reticulum to the plasma membrane.