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(Received for publication, December 4, 1995; and in revised form, February 14, 1996) Previously, we have demonstrated that the cytoplasmic tyrosine
kinase p72
Volume 271,
Number 18,
Issue of May 3, 1996 pp. 10775-10781
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
Noncovalently Associate with
the Low Affinity Fc
Receptor on Human Platelets through an
Immunoreceptor Tyrosine-based Activation Motif
RECONSTITUTION WITH SYNTHETIC PHOSPHOPEPTIDES
is coupled to the platelet Fc
receptor for IgG (Fc
RIIA) (Chacko, G. W., Duchemin, A. M.,
Coggeshall, K. M., Osborne, J. M., Brandt, J. T., and Anderson, C. L.
(1994) J. Biol. Chem. 269, 32435-32440). Further
analysis of the platelet activation by FcRIIA demonstrated that
FcRIIA is also inducibly coupled to the serine/threonine and lipid
kinase, phosphoinositide 3-kinase (PI 3-K). Activation of platelets
with anti-FcRIIA antibodies resulted in the noncovalent
association of PI 3-K with FcRIIA as well as an increase in
FcRIIA-associated PI 3-K activity. Binding of both p72 and PI 3-K to FcRIIA was reconstituted with synthetic
phosphopeptides corresponding to the sequence of the atypical
immunoreceptor tyrosine-based activation motif (ITAM) in the
cytoplasmic domain of FcRIIA. Our findings demonstrate that
coupling of both p72 and PI 3-K activities to
FcRIIA is regulated by tyrosine phosphorylation of the ITAM, and
we speculate that p72 might act as an adapter to
recruit PI 3-K to activated FcRIIA.
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