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Prepublished online as a Blood First Edition Paper on May 17, 2002; DOI 10.1182/blood-2001-12-0340.
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Blood, 15 September 2002, Vol. 100, No. 6, pp. 2138-2144
IMMUNOBIOLOGY
Regulation of Fc RI-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 Fc RI 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.
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