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CUTTING EDGE |
,§,§
*
Department of Molecular Genetics, Institute for Liver Research, Kansai Medical University, Moriguchi, Japan;
Laboratory of Molecular Genetics and Immunology, Rockefeller University, New York, NY 10021;
Department of Pharmacology, Faculty of Medicine, University of Tokyo, Tokyo Japan;
§
Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Tokyo, Japan; and
¶
Department of Biomolecular Sciences, Fukushima Medical College, Fukushima, Japan
Src
homology-2 domain-containing inositol polyphosphate
5'-phosphatase (SHIP) is a recently identified protein that has been
implicated as an important signaling molecule. Although SHIP has
been shown to participate in the Fc
RIIB-mediated inhibitory signal,
the functional role of SHIP in activation responses by immunoreceptor
tyrosine-based activation motif-bearing receptors such as B cell
receptor (BCR) remains unclear. Indeed, it has been proposed that SHIP
serves as a linking molecule for the regulation of the extracellular
signal-regulated kinase pathway in BCR signaling, because SHIP
associates with Shc. We now report that SHIP-deficient DT40 B cells
display enhanced Ca2+ mobilization in response to BCR
ligation, whereas extracellular signal-regulated kinase
activation is unaffected. This Ca2+ enhancement is due to a
sustained intracellular Ca2+ increase or to long-lasting
Ca2+ oscillations by loss of SHIP, as revealed by
single-cell Ca2+ imaging analysis. These results
demonstrate the importance of SHIP in B cell activation by the
modulation of Ca2+
mobilization.
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