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Published online on January 25, 2005, 10.1073/pnas.0409062102
PNAS | February 8, 2005 | vol. 102 | no. 6 | 1921-1926


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CELL BIOLOGY
Gelsolin mediates calcium-dependent disassembly of Listeria actin tails

Laura Larson *, Serge Arnaudeau {dagger}, Bruce Gibson *, Wei Li *, Ryoko Krause {ddagger}, Binghua Hao *, James R. Bamburg §, Daniel P. Lew {ddagger}, Nicolas Demaurex {dagger}, and Frederick Southwick *, ¶

*Department of Medicine, Division of Infectious Diseases, University of Florida College of Medicine, Gainesville, FL 32610; {dagger}Departments of Physiology and {ddagger}Medicine/Infectious Diseases, University of Geneva, 1211 Geneva, Switzerland; and §Departments of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523

Edited by Thomas P. Stossel, Harvard Medical School, Boston, MA, and approved December 28, 2004 (received for review December 6, 2004)

The role of intracellular Ca2+ in the regulation of actin filament assembly and disassembly has not been clearly defined. We show that reduction of intracellular free Ca2+ concentration ([Ca2+]i) to <40 nM in Listeria monocytogenes-infected, EGFP–actin-transfected Madin–Darby canine kidney cells results in a 3-fold lengthening of actin filament tails. This increase in tail length is the consequence of marked slowing of the actin filament disassembly rate, without a significant change in assembly rate. The Ca2+-sensitive actin-severing protein gelsolin concentrates in the Listeria rocket tails at normal resting [Ca2+]i and disassociates from the tails when [Ca2+]i is lowered. Reduction in [Ca2+]i also blocks the severing activity of gelsolin, but not actin-depolymerizing factor (ADF)/cofilin microinjected into Listeria-infected cells. In Xenopus extracts, Listeria tail lengths are also calcium-sensitive, markedly shortening on addition of calcium. Immunodepletion of gelsolin, but not Xenopus ADF/cofilin, eliminates calcium-sensitive actin-filament shortening. Listeria tail length is also calcium-insensitive in gelsolin-null mouse embryo fibroblasts. We conclude that gelsolin is the primary Ca2+-sensitive actin filament recycling protein in the cell and is capable of enhancing Listeria actin tail disassembly at normal resting [Ca2+]i (145 nM). These experiments illustrate the unique and complementary functions of gelsolin and ADF/cofilin in the recycling of actin filaments.

actin-based motility | actin-depolymerizing factor/cofilin

Author contributions: L.L., S.A., B.G., J.R.B., D.P.L., N.D., and F.S. designed research; L.L., S.A., B.G., W.L., R.K., B.H., and F.S. performed research; L.L., B.G., W.L., R.K., B.H., J.R.B., D.P.L., N.D., and F.S. analyzed data; J.R.B. and N.D. contributed new reagents/analytic tools; and L.L., J.R.B., N.D., and F.S. wrote the paper

This paper was submitted directly (Track II) to the PNAS office.

Abbreviations: ADF, actin-depolymerizing factor; XAC, Xenopus ADF/cofilin; [Ca2+]i, intracellular free Ca2+ concentration; MDCK, Madin–Darby canine kidney; BAPTA-AM, 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetate-acetoxymethyl ester; Fura-2-AM, Fura 2-acetoxymethyl ester.

To whom correspondence should be addressed. E-mail: southfs{at}medmac.ufl.edu.

© 2005 by The National Academy of Sciences of the USA


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