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Prepublished online as a Blood First Edition Paper on May 17, 2002; DOI 10.1182/blood-2001-12-0340. This Article Full Text Full Text (PDF) All Versions of this Article: 2001-12-0340v1 100/6/2138    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 Sada, K. Articles by Yamamura, H. Search for Related Content PubMed PubMed Citation Articles by Sada, K. Articles by Yamamura, H. Related Collections Immunobiology Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 September 2002, Vol. 100, No. 6, pp. 2138-2144 IMMUNOBIOLOGY Regulation of FcRI-mediated degranulation by an adaptor protein 3BP2 in rat basophilic leukemia RBL-2H3 cells Kiyonao Sada, S. M. Shahjahan Miah, Koichiro Maeno, Shinkou Kyo, Xiujuan Qu, and Hirohei Yamamura From the Division of Proteomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Japan. Aggregation of high-affinity IgE receptor FcRI induces sequential activation of nonreceptor-type protein-tyrosine kinases and subsequent tyrosine phosphorylation of cellular proteins, leading to degranulation in mast cells. A hematopoietic cell-specific adaptor protein, 3BP2, that was originally identified as an Abl SH3-binding protein was rapidly tyrosine phosphorylated by the aggregation of FcRI on rat basophilic leukemia RBL-2H3 cells. Tyrosine phosphorylation of 3BP2 did not depend on calcium influx from external sources. To examine the role of 3BP2 in mast cells, we overexpressed the SH2 domain of 3BP2 in the RBL-2H3 cells. Overexpression of 3BP2-SH2 domain resulted in a suppression of antigen-induced degranulation as assessed by -hexosaminidase release. Even though overall tyrosine phosphorylation of cellular protein was not altered, antigen-mediated tyrosine phosphorylation of phospholipase C- (PLC-) and calcium mobilization were significantly suppressed in the cells overexpressing the 3BP2-SH2 domain. Furthermore, antigen stimulation induced the association of 3BP2-SH2 domain with LAT and other signaling molecule complexes in the RBL-2H3 cells. FcRI-mediated phosphorylation of JNK and ERK was not affected by the overexpression of 3BP2-SH2 domain. These data indicate that 3BP2 functions to positively regulate the FcRI-mediated tyrosine phosphorylation of PLC- and thereby the signals leading to degranulation. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: G. Chen, I. D. Dimitriou, J. La Rose, S. Ilangumaran, W.-C. Yeh, G. Doody, M. Turner, J. Gommerman, and R. Rottapel The 3BP2 Adapter Protein Is Required for Optimal B-Cell Activation and Thymus-Independent Type 2 Humoral Response Mol. Cell. Biol., April 15, 2007; 27(8): 3109 - 3122. [Abstract] [Full Text] [PDF] E. B. Cook, J. L. Stahl, A. M. Brooks, F. M. Graziano, and N. P. Barney Allergic tears promote upregulation of eosinophil adhesion to conjunctival epithelial cells in an ex vivo model: inhibition with olopatadine treatment. Invest. Ophthalmol. Vis. Sci., August 1, 2006; 47(8): 3423 - 3429. [Abstract] [Full Text] [PDF] M. A. de la Fuente, L. 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