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A more recent version of this article appeared on February 1, 2003
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Submitted on May 21, 2002
Revised on September 20, 2002
Accepted on October 21, 2002
1 Department of Microbiology and Immunology, G.W. Hooper Foundation, University of California, San Francisco, CA 94143
* Corresponding author. E-mail address: defranco{at}cgl.ucsf.edu.
Recent biochemical evidence indicates that an early event in signal transduction by the B cell antigen receptor (BCR) is its translocation to specialized membrane subdomains known as lipid rafts. We have taken a microscopic approach to image lipid rafts and early events associated with BCR signal transduction. Lipid rafts were visualized on primary splenic B lymphocytes from wild type or anti-hen egg lysozyme (HEL) BCR transgenic mice, and on a mature mouse B cell line Bal 17 by using fluorescent conjugates of cholera toxin B subunit or a Lyn-based chimeric protein, which targets green fluorescent protein to the lipid raft compartment. Time-lapse imaging of B cells stimulated via the BCR with the antigen HEL, or surrogate for antigen anti-IgM demonstrated that lipid rafts are highly dynamic entities, which move laterally on the surface of these cells and coalesce into large regions. These regions of aggregated lipid rafts co-localized with the BCR and tyrosine phosphorylated proteins. Microscopic imaging of live B cells also revealed an inducible co-localization of lipid rafts with the tyrosine kinase Syk and the receptor tyrosine phosphatase CD45. These two proteins play indispensable roles in BCR-mediated signaling but are not detectable in biochemically purified lipid raft fractions. Strikingly, BCR stimulation also induced the formation of long, thread-like filopodial projections, similar to previously described structures called cytonemes. These B cell cytonemes are rich in lipid rafts and actin filaments suggesting that they might play a role in long-range communication and/or transportation of signaling molecules during an immune response. These results provide a window into the morphological and molecular organization of the B cell membrane during the early phase of BCR signaling.
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