ArticlePLoS computational biology2014
Compact modeling of allosteric multisite proteins: application to a cell size checkpoint.
Article in PLoS computational biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Effect of magnitude and variability of energy of activation in multisite ultrasensitive biochemical processes.PLoS computational biology · 2020Article
- A conserved signaling network monitors delivery of sphingolipids to the plasma membrane in budding yeast.Molecular biology of the cell · 2017Article
- The effect of site-to-site variability in ultrasensitive dose responses.Journal of mathematical biology · 2017Article
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Authors and funding
3 authors.
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Abstract
We explore a framework to model the dose response of allosteric multisite phosphorylation proteins using a single auxiliary variable. This reduction can closely replicate the steady state behavior of detailed multisite systems such as the Monod-Wyman-Changeux allosteric model or rule-based models. Optimal ultrasensitivity is obtained when the activation of an allosteric protein by its individual sites is concerted and redundant. The reduction makes this framework useful for modeling and analyzing biochemical systems in practical applications, where several multisite proteins may interact simultaneously. As an application we analyze a newly discovered checkpoint signaling pathway in budding yeast, which has been proposed to measure cell growth by monitoring signals generated at sites of plasma membrane growth. We show that the known components of this pathway can form a robust hysteretic switch. In particular, this system incorporates a signal proportional to bud growth or size, a mechanism to read the signal, and an all-or-none response triggered only when the signal reaches a threshold indicating that sufficient growth has occurred.
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