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J Biol Chem, Vol. 274, Issue 46, 32662-32666, November 12, 1999
§,§
From the We have recently demonstrated that the
D3-phosphoinositide phosphatidylinositol 3,4,5-trisphosphate
(PtdIns-3,4,5-P3) is critical for producing sustained
calcium signals through its role in promoting the function of TEC
family tyrosine kinases such as Bruton's tyrosine kinase. Although
PtdIns-3,4,5-P3 can potentially be synthesized by any of
several types of phosphoinositide 3-kinases (PI3Ks), B cell receptor
(BCR)-induced PtdIns-3,4,5-P3 production is thought to
occur primarily through the activation of the class Ia (p85/p110) PI3Ks. This process has been proposed to be mediated by an interaction between the Src family kinase LYN and the p85 subunit of PI3K and/or
through p85 membrane recruitment mediated by CBL and/or CD19. However,
calcium signaling and other PI3K-dependent signals are
relatively preserved in a LYN kinase-deficient B lymphocyte cell line,
suggesting that an alternative pathway for PI3K activation exists. As
SYK/ZAP70 kinases are upstream from many BCR-initiated signaling
events, we directly analyzed SYK-dependent accumulation of
both PtdIns-3,4,5-P3 and PtdIns-3,4-P2 in B
cell receptor signaling using both dominant negative and genetic
knockout approaches. Both methods indicate that SYK is upstream of, and
necessary for, a significant portion of BCR-induced
PtdIns-3,4,5-P3 production. Whereas CD19 does not appear to
be involved in this SYK-dependent pathway, the SYK
substrate CBL is likely involved as the dominant negative SYK markedly
attenuates CBL tyrosine phosphorylation and completely blocks the
BCR-dependent association of CBL with p85 PI3K.
Laboratory of Allergy and Immunology and the
¶ Division of Signal Transduction,
Cell Biology,
Harvard Medical School, Boston, Massachusetts 02215, and the
** Department of Molecular Genetics Kansai Medical
University, Moriguchi 570, Japan
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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