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Vol. 16, Issue 5, 2275-2284, May 2005

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Actin Depolymerization Transduces the Strength of B-Cell Receptor Stimulation

Immunology Research Laboratories, Department of Veterinary Science, and Integrated Bioscience Graduate Program of the Huck Institute for Life Sciences, Cell and Developmental Biology Graduate Option, The Pennsylvania State University, University Park, PA 16802

Submitted October 8, 2004; Revised January 3, 2005; Accepted February 13, 2005
Monitoring Editor: Anne Ridley

Polymerization of the actin cytoskeleton has been found to be essential for B-cell activation. We show here, however, that stimulation of BCR induces a rapid global actin depolymerization in a BCR signal strength-dependent manner, followed by polarized actin repolymerization. Depolymerization of actin enhances and blocking actin depolymerization inhibits BCR signaling, leading to altered BCR and lipid raft clustering, ERK activation, and transcription factor activation. Furthermore actin depolymerization by itself induces altered lipid raft clustering and ERK activation, suggesting that F-actin may play a role in separating lipid rafts and in setting the threshold for cellular activation.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

^* Present address: Division of Biology, California Institute of Technology, 1200 E. California Boulevard, MC 147-75, Pasadena, CA 91125.

Address correspondence to: Avery August (axa45{at}psu.edu).

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