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(Received for publication, May 6, 1996, and in revised form, August 16, 1996)
From the Immunoreceptors such as the high affinity IgE
receptor, Fc
Volume 271, Number 46,
Issue of November 15, 1996
pp. 29271-29278
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-Phosphatase SHIP Binds to Immunoreceptor
Signaling Motifs and Responds to High Affinity IgE Receptor
Aggregation
,
,
,
,
,
and
Department of Metabolic Diseases,
Hoffmann-La Roche, Inc., Nutley, New Jersey 07110, the
¶ Division of Hematology, Washington University School
of Medicine, St. Louis, Missouri 63110, the 
Division of Signal
Transduction, Department of Medicine, Beth Israel Hospital, and the
Department of Cell Biology, Harvard Medical School,
Boston, Massachusetts 02115
RI, and T-cell receptor-associated proteins share a
common motif, the immunoreceptor tyrosine-based activation motif
(ITAM). We used the yeast tribrid system to identify downstream
effectors of the phosphorylated FcRI ITAM-containing subunits 
and 
. One novel cDNA was isolated that encodes a protein that is
phosphorylated on tyrosine, contains a Src-homology 2 (
)
domain, 
nositolpoly
hosphate 5-phosphatase
activity, three NXXY motifs, several proline-rich regions,
and is called SHIP. Mutation of the conserved tyrosine or leucine
residues within the FcRI or ITAMs eliminates SHIP binding
and indicates that the SHIP-ITAM interaction is specific. SHIP also
binds to ITAMs from the CD3 complex and T cell receptor 
chain
in vitro. SHIP protein possesses both
phosphatidylinositol-3,4,5-trisphosphate 5
-phosphatase and
inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity.
Phosphorylation of SHIP by a protein-tyrosine kinase, Lck, results in a
reduction in enzyme activity. FcRI activation induces the
association of several tyrosine phosphoproteins with SHIP. SHIP is
constitutively tyrosine-phosphorylated and associated with Shc and
Grb2. These data suggest that SHIP may serve as a multifunctional
linker protein in receptor activation.
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O. Malbec, D. C. Fong, M. Turner, V. L. J. Tybulewicz, J. C. Cambier, W. H. Fridman, and M. Daeron Fc{epsilon} Receptor I-Associated lyn-Dependent Phosphorylation of Fc{gamma} Receptor IIB During Negative Regulation of Mast Cell Activation J. Immunol., February 15, 1998; 160(4): 1647 - 1658. [Abstract] [Full Text] [PDF]
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X. Zhang, P. A. Hartz, E. Philip, L. C. Racusen, and P. W. Majerus Cell Lines from Kidney Proximal Tubules of a Patient with Lowe Syndrome Lack OCRL Inositol Polyphosphate 5-Phosphatase and Accumulate Phosphatidylinositol 4,5-Bisphosphate J. Biol. Chem., January 16, 1998; 273(3): 1574 - 1582. [Abstract] [Full Text] [PDF]
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