Journal
PLOS COMPUTATIONAL BIOLOGY
Volume 8, Issue 6, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pcbi.1002551
Keywords
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Funding
- National Science Foundation [DMS-1122478, UBM-112908, DMS-0917492]
- National Institutes of Health [R01GM75309, R01GM67247, P50GM76516]
- [R01GM84332]
- [R01GM86883]
- Direct For Mathematical & Physical Scien [0917492] Funding Source: National Science Foundation
- Division Of Mathematical Sciences [0917492] Funding Source: National Science Foundation
- Division Of Mathematical Sciences
- Direct For Mathematical & Physical Scien [1122478, 1019544] Funding Source: National Science Foundation
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The phosphorylation of a substrate at multiple sites is a common protein modification that can give rise to important structural and electrostatic changes. Scaffold proteins can enhance protein phosphorylation by facilitating an interaction between a protein kinase enzyme and its target substrate. In this work we consider a simple mathematical model of a scaffold protein and show that under specific conditions, the presence of the scaffold can substantially raise the likelihood that the resulting system will exhibit bistable behavior. This phenomenon is especially pronounced when the enzymatic reactions have sufficiently large K-M, compared to the concentration of the target substrate. We also find for a closely related model that bistable systems tend to have a specific kinetic conformation. Using deficiency theory and other methods, we provide a number of necessary conditions for bistability, such as the presence of multiple phosphorylation sites and the dependence of the scaffold binding/unbinding rates on the number of phosphorylated sites.
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