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(Received for publication, December 18, 1996, and in revised form, February 11, 1997)
From the The Terry Fox Laboratory, British Columbia Cancer Agency,
University of British Columbia, Vancouver,
British Columbia V5Z 1L3, Canada
We recently purified and cloned a 145-kDa protein
that becomes tyrosine phosphorylated and associated with Shc in
response to multiple cytokines. Based on its predicated amino acid
sequence and its enzymatic activity, we have called this protein SHIP, for rc omology 2-containing
nositol hosphatase. To gain further insight
into the intracellular pathways that this putative signal transduction
intermediate might regulate we have investigated whether SHIP binds to
intracellular proteins other than Shc. The results presented herein
demonstrate that following interleukin-3 stimulation, SHIP binds to the
tyrosine phosphatase, SHP2 (also called Syp, PTP1D, SHPTP2, and PTP2C)
and that Shc is not present in these SHIP-SHP2 complexes. Time course
studies reveal that SHIP's association with SHP2 is transient and is
maximal at 10 min of stimulation with interleukin-3. We further show
that the association of SHIP with SHP2 occurs through the direct
interaction of the SH2 domain of SHIP with a pYXN(I/V)
sequence within SHP2.
Volume 272, Number 17,
Issue of April 25, 1997
pp. 10998-11001
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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