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Department of Biochemistry and Molecular Biology, Immunology Research Group, Faculty of Medicine, University of Calgary, Calgary, Alberta, Canada
The B cell Ag receptor (BCR) and CD20, a putative calcium channel,
inducibly associate with cholesterol-dependent membrane microdomains
known as lipid rafts. A functional association between the BCR and CD20
is suggested by the effects of CD20-specific mAbs, which can modulate
cell cycle transitions elicited by BCR signaling. Using
immunofluorescence microscopy we show here that the BCR and CD20
colocalize after receptor ligation and then rapidly dissociate at the
cell surface before endocytosis of the BCR. After separation, surface
BCR and CD20 were detected in distinct lipid rafts isolated as low
density, detergent-resistant membrane fragments. Pretreatment with
methyl-
-cyclodextrin, which we have previously shown to enhance
receptor-mediated calcium mobilization, did not prevent colocalization
of the BCR and CD20, but slowed their dissociation. The data
demonstrate rapid dynamics of the BCR in relation to CD20 at the cell
surface. Activation-dependent dissociation of the BCR from CD20 occurs
before receptor endocytosis and appears to require in part the
integrity of lipid rafts.
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