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Blood, 15 December 2006, Vol. 108, No. 13, pp. 4086-4093. Prepublished online as a Blood First Edition Paper on August 24, 2006; DOI 10.1182/blood-2006-05-025338. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2006-05-025338v1 108/13/4086    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Drake, L. Articles by Drake, J. R. Search for Related Content PubMed PubMed Citation Articles by Drake, L. Articles by Drake, J. R. Related Collections Immunobiology Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  IMMUNOBIOLOGY BCR ubiquitination controls BCR-mediated antigen processing and presentation Lisa Drake, Erica M. McGovern-Brindisi, and James R. Drake From the Albany Medical College, Center for Immunology and Microbial Disease, Albany, NY. BCR-mediated antigen processing occurs at immunologically relevant antigen concentrations and hinges on the trafficking of antigen-BCR (Ag-BCR) complexes to class II–containing multivesicular bodies (MVBs) termed MIICs. However, the molecular mechanism underlying the trafficking of Ag-BCR complexes to and within MIICs is not well understood. In contrast, the trafficking of the epidermal growth factor receptor (EGFR) to and within MVBs occurs via a well-characterized ubiquitin-dependent mechanism, which is blocked by acute inhibition of proteasome activity. Using a highly characterized antigen-specific model system, it was determined that the immunoglobulin heavy chain subunit of the IgM BCR of normal (ie, nontransformed) B cells is ubiquitinated. Moreover, acute inhibition of proteasome activity delays the formation of ubiquitinated ligand–BCR complexes, alters the intracellular trafficking of internalized Ag-BCR complexes, and selectively blocks the BCR-mediated processing and presentation of cognate antigen, without inhibiting the endocytosis, processing, and presentation of non–cognate antigen internalized by fluidphase endocytosis. These results demonstrate that the trafficking of Ag-BCR complexes to and within MVB-like antigen processing compartments occurs via a molecular mechanism with similarities to that used by the EGFR, and establishes the EGFR as a paradigm for the further analysis of Ag-BCR trafficking to and within MIICs. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: B. R. Schram, L. E. Tze, L. B. Ramsey, J. Liu, L. Najera, A. L. Vegoe, R. R. Hardy, K. L. Hippen, M. A. Farrar, and T. W. Behrens B Cell Receptor Basal Signaling Regulates Antigen-Induced Ig Light Chain Rearrangements J. Immunol., April 1, 2008; 180(7): 4728 - 4741. [Abstract] [Full Text] [PDF] M. Zhang, M. Veselits, S. O'Neill, P. Hou, A. L. Reddi, I. Berlin, M. Ikeda, P. D. Nash, R. Longnecker, H. Band, et al. Ubiquitinylation of Igbeta Dictates the Endocytic Fate of the B Cell Antigen Receptor J. Immunol., October 1, 2007; 179(7): 4435 - 4443. [Abstract] [Full Text] [PDF] F. Vascotto, D. Lankar, G. Faure-Andre, P. Vargas, J. Diaz, D. Le Roux, M.-I. Yuseff, J.-B. Sibarita, M. Boes, G. Raposo, et al. The actin-based motor protein myosin II regulates MHC class II trafficking and BCR-driven antigen presentation J. Cell Biol., March 26, 2007; 176(7): 1007 - 1019. [Abstract] [Full Text] [PDF]

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