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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 (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 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. Social Bookmarking                   What's this? Submitted December 27, 2001 Accepted April 16, 2002 Regulation of FcRI-Mediated Degranulation by an Adaptor Protein 3BP2 in the Rat Basophilic Leukemia RBL-2H3 Cells Kiyonao Sada*, Shahjahan S Miah, Koichiro Maeno, Shinkou Kyo, Xiujuan Qu, and Hirohei Yamamura Div. Proteomics, Dept. of Genome Sciences, Kobe University, Kobe, Japan * Corresponding author; email: ksada{at}med.kobe-u.ac.jp. Aggregation of high affinity IgE receptor (FcRI) induces sequential activation of non-receptor type of 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 the 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, the SH2 domain of 3BP2 was overexpressed in the RBL-2H3 cells. Overexpression of 3BP2-SH2 domain resulted in a suppression of antigen-induced degranulation as assessed by ß-hexosaminidase release. Even overall tyrosine phosphorylation of cellular protein was not altered, antigen-mediated tyrosine phosphorylation of PLC- and calcium mobilization were significantly suppressed in the cells overexpressing 3BP2-SH2 domain. Furthermore, antigen-stimulation induced the association of 3BP2-SH2 domain with LAT and other signaling molecule complex 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. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? 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