We have studied in cultured rat astroglial cells MAP kinases, known for their role in intracellular signal transduction. The MAP kinase activity was stimulated by growth factors (FGFb, FGFa, EGF, PDGF, and IGFl), by a phorbol ester (TPA) activating-protein kinase C (PKC), by a neuropeptide (endothel
Selectivity in Overlapping MAP Kinase Cascades
β Scribed by OSCAR J.G. SOMSEN; MARCO SIDERIUS; FLORIAN F. BAUER; JACKY L. SNOEP; HanS V. WESTERHOFF
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- English
- Weight
- 239 KB
- Volume
- 218
- Category
- Article
- ISSN
- 0022-5193
No coin nor oath required. For personal study only.
β¦ Synopsis
Some protein kinases operate in more than one mitogen-activated protein-kinase (MAPK) cascade. We here address the question whether specificity of the cascades necessitates physical sequestration of these "promiscuous" kinases (e.g. by binding to scaffolds). A model is constructed, in which two MAPK cascades depend on a single MAP-kinase kinase that is not sequestered in two subpopulations. We show that in this model selective signal transduction is possible provided that there is an additional interaction at the MAP-kinase level, there is no simultaneous activation of more than one response by either signal. We discuss a number of additional interactions that can generate the selectivity, as well as some kinetic features by which this mechanism may be recognized experimentally.
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