title: Regulation of actin by ion-linked equilibria.
abstract: Actin assembly, filament mechanical properties, and interactions with regulatory proteins depend on the types and concentrations of salts in solution. Salts modulate actin through both nonspecific electrostatic effects and specific binding to discrete sites. Multiple cation-binding site classes spanning a broad range of affinities (nanomolar to millimolar) have been identified on actin monomers and filaments. This review focuses on discrete, low-affinity cation-binding interactions that drive polymerization, regulate filament-bending mechanics, and modulate interactions with regulatory proteins. Cation binding may be perturbed by actin post-translational modifications and linked equilibria. Partial cation occupancy under physiological and commonly used in vitro solution conditions likely contribute to filament mechanical heterogeneity and structural polymorphism. Site-specific cation-binding residues are conserved in Arp2 and Arp3, and may play a role in Arp2/3 complex activation and actin-filament branching activity. Actin-salt interactions demonstrate the relevance of ion-linked equilibria in the operation and regulation of complex biological systems.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut.
authors.forename: Hyeran
authors.initials: H
authors.lastname: Kang
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Bradley
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut.
authors.forename: W Austin
authors.initials: WA
authors.lastname: Elam
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut. Electronic address: enrique.delacruz@yale.edu.
authors.forename: Enrique M
authors.initials: EM
authors.lastname: De La Cruz
mesh_terms: D051376:Actin-Related Protein 2-3 Complex / Q000378:metabolism; D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002413:Cations, Divalent / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D055503:Protein Multimerization
chemical_list: D051376:Actin-Related Protein 2-3 Complex; D000199:Actins; D002413:Cations, Divalent