Structural instability in an autophosphorylating kinase switch.
We analyse a simple kinase model that exhibits bistability when there is no protein turnover, and show analytically that the property of being bistable is not necessarily conserved when degradation and synthesis of the kinase are taken into account.
Grinfeld
Michael
M
Department of Mathematics, University of Strathclyde, 26 Richmond Street, Glasgow G1 1XH, UK. michael@maths.strath.ac.uk
Webb
Steven D
SD
D000465:Algorithms; D064007:Ataxia Telangiectasia Mutated Proteins; D055162:Biocatalysis; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2 / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D004795:Enzyme Stability; D007700:Kinetics; D008954:Models, Biological; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D025521:Tumor Suppressor Proteins / Q000378:metabolism
D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D025521:Tumor Suppressor Proteins; D011494:Protein Kinases; D064007:Ataxia Telangiectasia Mutated Proteins; D017346:Protein Serine-Threonine Kinases; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D010749:Phosphoprotein Phosphatases