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Structure And Dynamic States of Actin Filaments

Submitted:

21 April 2026

Posted:

29 April 2026

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Abstract
Actin, a highly conserved and ubiquitous eukaryotic protein, underlies essential cellular processes including motility, shape maintenance and muscle contraction. Its dynamic transition between monomeric and filamentous states is powered by ATP hydrolysis, which undergoes structural rearrangements that accelerate turnover in filaments and serve as a measure of filament aging. A wide range of actin binding proteins (ABPs) regulate polymerization, depolymerization, and network organization. Recent high resolution cryo-EM and cryo-ET studies have revealed detailed structures of actin, its isoforms, and ABP complexes, including their organization in cells, deepening our understanding of actin function in health and disease.
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Copyright: This open access article is published under a Creative Commons CC BY 4.0 license, which permit the free download, distribution, and reuse, provided that the author and preprint are cited in any reuse.
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