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*
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208;
Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742; and
Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852
The cross-linking of the B cell Ag receptor (BCR) leads to the
initiation of a signal transduction cascade in which the earliest
events involve the phosphorylation of the immunoreceptor tyrosine-based
activation motifs of Ig
and Ig
by the Src family kinase Lyn and
association of the BCR with the actin cytoskeleton. However, the
mechanism by which BCR cross-linking initiates the cascade remains
obscure. In this study, using various A20-transfected cell lines,
biochemical and genetic evidence is provided that BCR cross-linking
leads to the translocation of the BCR into cholesterol- and
sphingolipid-rich lipid rafts in a process that is independent of the
initiation of BCR signaling and does not require the actin
cytoskeleton. Translocation of the BCR into lipid rafts did not require
the Ig/Ig signaling complex, was not dependent on engagement of
the FcR, and was not blocked by the Src family kinase inhibitor PP2 or
the actin-depolymerizing agents cytochalasin D or latrunculin. Thus,
cross-linking or oligomerization of the BCR induces the BCR
translocation into lipid rafts, defining an event in B cell activation
that precedes receptor phosphorylation and association with the actin
cytoskeleton.
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