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International Immunology Advance Access originally published online on November 1, 2007
International Immunology 2007 19(12):1403-1412; doi:10.1093/intimm/dxm110
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© The Japanese Society for Immunology. 2007. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

The transmembrane tyrosine of µ-heavy chain is required for BCR destabilization and entry of antigen into clathrin-coated vesicles

Jin Hyang Kim, Jennifer A. Rutan and Barbara J. Vilen

Department of Microbiology and Immunology and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA

Correspondence to: B. Vilen; E-mail: barb_vilen{at}med.unc.edu

The B cell antigen receptor (BCR) delivers antigen to the endocytic compartment and transduces signals that regulate the stability of the receptor complex. Previous studies showed that BCR-mediated signal transduction dissociates µ-heavy chain (µm) from Ig-{alpha}/Ig-ß, facilitating the delivery of antigen to clathrin-coated vesicles (CCVs). Herein, we demonstrate that the dissociation of Ig-{alpha}/Ig-ß from µm requires tyrosine-587 of the µm transmembrane domain. Receptors expressing a mutation at tyrosine-587 (Y587F) transduced signals that were comparable to wild type, yet they failed to dissociate µm from Ig-{alpha}/Ig-ß. Further, receptors harboring the Y587F mutation failed to associate with CCVs, resulting in diminished antigen in the lysosome-associated membrane protein-1 (LAMP-1+) compartment and severely impaired antigen presentation, indicating that endocytosis through CCVs is required for antigen presentation. Thus, the transmembrane tyrosine of µm mediates destabilization of the BCR complex, facilitating antigen processing by promoting the association of antigen with CCVs.

Keywords: antigen processing/presentation, B cell, cell activation, signal transduction

Transmitting editor: T. F. Tedder

Received 9 January 2007, accepted 1 October 2007.


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