Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness.

Abstract:

:The assembly of actin monomers into filaments and networks plays vital roles throughout eukaryotic biology, including intracellular transport, cell motility, cell division, determining cellular shape, and providing cells with mechanical strength. The regulation of actin assembly and modulation of filament mechanical properties are critical for proper actin function. It is well established that physiological salt concentrations promote actin assembly and alter the overall bending mechanics of assembled filaments and networks. However, the molecular origins of these salt-dependent effects, particularly if they involve nonspecific ionic strength effects or specific ion-binding interactions, are unknown. Here, we demonstrate that specific cation binding at two discrete sites situated between adjacent subunits along the long-pitch helix drive actin polymerization and determine the filament bending rigidity. We classify the two sites as "polymerization" and "stiffness" sites based on the effects that mutations at the sites have on salt-dependent filament assembly and bending mechanics, respectively. These results establish the existence and location of the cation-binding sites that confer salt dependence to the assembly and mechanics of actin filaments.

authors

Kang H,Bradley MJ,McCullough BR,Pierre A,Grintsevich EE,Reisler E,De La Cruz EM

doi

10.1073/pnas.1211078109

subject

Has Abstract

pub_date

2012-10-16 00:00:00

pages

16923-7

issue

42

eissn

0027-8424

issn

1091-6490

pii

1211078109

journal_volume

109

pub_type

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