Ca2+ control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation.

H. L. Yin, K. S. Zaner, T. P. Stossel

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Abstract

We elucidated the mechanism by which gelsolin, a Ca2+-dependent regulatory protein from lung macrophages, controls the network structure of actin filaments. In the presence of micromolar Ca2+, gelsolin bound Ca2+. The Ca2+-gelsolin complex reduced the apparent viscosity and flow birefringence of F-actin and the lengths of actin filaments viewed in the electron microscope. However, concentrations of gelsolin causing these alterations did not effect proportionate changes in the turbidity of actin filament solutions or in the quantity of nonsedimentable actin as determined by a radioassay. From these findings, we conclude that gelsolin shortens actin filaments without net depolymerization. Such an effect on the distribution of actin filament lengths led to the prediction that low concentrations of gelsolin would increase the critical concentration of actin-binding protein required for incipient gelation of actin filaments in the presence of Ca2+, providing an efficient mechanism for controlling actin network structure. We verified the prediction experimentally, and we estimated that the Ca2+-gelsolin complex effectively breaks the bond between actin monomers in filaments with a stoichiometry of 1:1. The effect of Ca2+-gelsolin complex on actin solation was rapid, independent of temperature between 0 degrees and 37 degrees C, and reversed by reducing the free Ca2+ concentration.

Original languageEnglish (US)
Pages (from-to)9494-9500
Number of pages7
JournalJournal of Biological Chemistry
Volume255
Issue number19
StatePublished - Oct 10 1980

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Gelsolin
Gelation
Actin Cytoskeleton
Actins
Birefringence
Microfilament Proteins
Viscosity
Depolymerization
Macrophages
Turbidity
Electrons
Stoichiometry
Lung
Temperature
Electron microscopes

ASJC Scopus subject areas

  • Biochemistry

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Ca2+ control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation. / Yin, H. L.; Zaner, K. S.; Stossel, T. P.

In: Journal of Biological Chemistry, Vol. 255, No. 19, 10.10.1980, p. 9494-9500.

Research output: Contribution to journalArticle

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AB - We elucidated the mechanism by which gelsolin, a Ca2+-dependent regulatory protein from lung macrophages, controls the network structure of actin filaments. In the presence of micromolar Ca2+, gelsolin bound Ca2+. The Ca2+-gelsolin complex reduced the apparent viscosity and flow birefringence of F-actin and the lengths of actin filaments viewed in the electron microscope. However, concentrations of gelsolin causing these alterations did not effect proportionate changes in the turbidity of actin filament solutions or in the quantity of nonsedimentable actin as determined by a radioassay. From these findings, we conclude that gelsolin shortens actin filaments without net depolymerization. Such an effect on the distribution of actin filament lengths led to the prediction that low concentrations of gelsolin would increase the critical concentration of actin-binding protein required for incipient gelation of actin filaments in the presence of Ca2+, providing an efficient mechanism for controlling actin network structure. We verified the prediction experimentally, and we estimated that the Ca2+-gelsolin complex effectively breaks the bond between actin monomers in filaments with a stoichiometry of 1:1. The effect of Ca2+-gelsolin complex on actin solation was rapid, independent of temperature between 0 degrees and 37 degrees C, and reversed by reducing the free Ca2+ concentration.

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