Selectivity in overlapping MAP kinase cascades.
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.
Somsen
Oscar J G
OJ
Department of Molecular Cell Physiology, Free University Amsterdam, De Boelelaan 1087, NL-1081 HV, Amsterdam, The Netherlands.
Siderius
Marco
M
Bauer
Florian F
FF
Snoep
Jacky L
JL
Westerhoff
Hans V
HV
D000222:Adaptation, Physiological; D000818:Animals; D004789:Enzyme Activation; D020935:MAP Kinase Signaling System / Q000502:physiology*; D020929:Mitogen-Activated Protein Kinase Kinases / Q000502:physiology; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D008956:Models, Chemical
D020928:Mitogen-Activated Protein Kinases; D020929:Mitogen-Activated Protein Kinase Kinases