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Independent Trafficking of Ig-/Ig- and µ-Heavy Chain Is Facilitated by Dissociation of the B Cell Antigen Receptor Complex ¹

Jin-Hyang Kim, Lorraine Cramer, Heather Mueller, Bridget Wilson^* and Barbara J. Vilen^2,

^* Department of Pathology and the Cancer Research and Treatment Center, University of New Mexico Health Sciences Center, Albuquerque, NM 87131; and Department of Microbiology/Immunology and Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599

The BCR relays extracellular signals and internalizes Ag for processing and presentation. We have previously demonstrated that ligation of the BCR destabilizes Ig-/Ig- (Ig-) from µ-H chain (µm). In this study we report that receptor destabilization represents a physical separation of µm from Ig-. Sucrose gradient fractionation localized Ig- to G_M1-containing lipid microdomains in the absence of µm. Confocal and electron microscopy studies revealed the colocalization of unsheathed µm with clathrin-coated vesicles. Furthermore, µm failed to associate with clathrin-coated vesicles when receptor destabilization was inhibited, suggesting that unsheathing of µm is required for clathrin-mediated endocytosis. In summary, we found that Ag stimulation physically separates Ig- from µm, facilitating concomitant signal transduction and Ag delivery to the endocytic compartment.

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The JI 2005 175: 1-2. [Full Text]  

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