Affinity of alpha-actinin for actin determines the structure and mechanical properties of actin filament gels.

Abstract:

:Proteins that cross-link actin filaments can either form bundles of parallel filaments or isotropic networks of individual filaments. We have found that mixtures of actin filaments with alpha-actinin purified from either Acanthamoeba castellanii or chicken smooth muscle can form bundles or isotropic networks depending on their concentration. Low concentrations of alpha-actinin and actin filaments form networks indistinguishable in electron micrographs from gels of actin alone. Higher concentrations of alpha-actinin and actin filaments form bundles. The threshold for bundling depends on the affinity of the alpha-actinin for actin. The complex of Acanthamoeba alpha-actinin with actin filaments has a Kd of 4.7 microM and a bundling threshold of 0.1 microM; chicken smooth muscle has a Kd of 0.6 microM and a bundling threshold of 1 microM. The physical properties of isotropic networks of cross-linked actin filaments are very different from a gel of bundles: the network behaves like a solid because each actin filament is part of a single structure that encompasses all the filaments. Bundles of filaments behave more like a very viscous fluid because each bundle, while very long and stiff, can slip past other bundles. We have developed a computer model that predicts the bundling threshold based on four variables: the length of the actin filaments, the affinity of the alpha-actinin for actin, and the concentrations of actin and alpha-actinin.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Wachsstock DH,Schwartz WH,Pollard TD

doi

10.1016/S0006-3495(93)81059-2

subject

Has Abstract

pub_date

1993-07-01 00:00:00

pages

205-14

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(93)81059-2

journal_volume

65

pub_type

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