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(Received for publication, October 4, 1996, and in revised form, November 14, 1996)
From the Cross-linking of the Fc receptor (FcR) to surface
immunoglobulin (sIg) on B cells inhibits the influx of extracellular
calcium and abrogates the proliferative signal. The mechanism by which this occurs is not well understood. In this report we show that co-cross-linking the FcR to the antigen receptor gives rise to very
selective modulation of signal transduction in B cells.
Co-cross-linking sIg and the FcR enhanced the phosphorylation of the
FcR, the adapter protein, Shc, and the inositol 5
Volume 272, Number 6,
Issue of February 7, 1997
pp. 3838-3844
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
REGULATION OF THE ASSOCIATION OF PHOSPHATIDYLINOSITOL 3-KINASE
AND INOSITOL 5
-PHOSPHATASE WITH THE ANTIGEN RECEPTOR COMPLEX
,
,
and
Department of Immunological Diseases,
Bristol-Myers Squibb Pharmaceutical Research Institute,
Seattle, Washington 98121 and ¶ Fred Hutchinson Cancer Research
Center, Seattle, Washington 98125
-phosphatase Ship.
Furthermore, phosphorylation of the FcR induced its association with
Ship. Cross-linking of the FcR and sIg decreased the tyrosine
phosphorylation of CD19, which led to a reduction in the association of
phosphatidylinositol 3-kinase. In addition, the phosphorylation of
several other proteins of 73, 39, and 34 kDa was reduced. Activation of
the cells with either F(ab)2 or intact anti-IgG induced
very similar changes in levels of tyrosine phosphorylation of most
other proteins, and no differences in the activation of several protein
kinases were observed. These results indicate that the inhibitory
signal that is transmitted through the FcR is not mediated by a global shutdown of tyrosine phosphorylation but is, rather, a selective mechanism involving localized changes in the interactions of adapter proteins and the enzymes Ship and phosphatidylinositol 3-kinase with
the antigen receptor complex.
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