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MBC in Press, published online ahead of print February 23, 2005
Mol. Biol. Cell 10.1091/mbc.E04-10-0881

A more recent version of this article appeared on May 1, 2005
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Submitted on October 8, 2004
Revised on January 3, 2005
Accepted on February 13, 2005

Actin Depolymerization Transduces the Strength of B Cell Receptor Stimulation

Shengli Hao* and Avery August

Immunology Research Laboratories and 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

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.


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

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




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