This framework reveals distinct regulatory mechanisms of actin dynamics in vivo, indicating insights into protein interactions.
The length of actin filaments is regulated by the combined action of hundreds of actin-binding proteins. While the roles of individual proteins are well understood, how they combine to regulate actin dynamics in vivo remains unclear. Recent advances in microscopy have enabled precise, high-throughput measurements of filament lengths over time. However, the absence of a unified theoretical framework has hindered a mechanistic understanding of the multicomponent regulation of actin dynamics. To address this, we propose a general kinetic model that incorporates the combined effects of an arbitrary number of regulatory proteins on actin dynamics. We derive exact closed-form expressions for the moments of (1) the distribution of filament lengths over time and (2) the long-time distribution of changes in filament lengths within a fixed time window. We show that these moments allow us to distinguish between different regulatory mechanisms of multicomponent regulation of actin dynamics. Our theoretical framework provides a powerful tool for interpreting existing data and guiding future experiments.
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Nandi et al. (2025) studied this question.
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