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(Received for publication, July 11, 1996, and in revised form, October 11, 1996)
From the Interactions between SHP-2 phosphotyrosine
phosphatase and JAK tyrosine kinases have recently been implicated in
cytokine signal transduction. However, the molecular basis of these
interactions is not well understood. In this study, we demonstrate that
SHP-2 is tyrosine-phosphorylated by and associated with JAK1 and JAK2 but not JAK3 in COS-1 cell cotransfection experiments. SHP-2
phosphatase activity appears not to be required for JAK and SHP-2
interactions because SHP-2 with a mutation at amino acid 463 from Cys
to Ser, which renders SHP-2 inactive, can still bind JAKs. We further demonstrate that SHP-2 SH2 domains (amino acids 1-209) are not essential for the association of JAKs with SHP-2, and the region between amino acids 232 and 272 in SHP-2 is important for the interactions. Furthermore, tyrosine residues 304 and 327 in SHP-2 are
phosphorylated by JAKs, and phosphorylated SHP-2 can associate with the
downstream adapter protein Grb2. Finally, deletion of the N terminus
but not the kinase-like domain of JAK2 abolishes the association of
JAK2 with SHP-2. Taken together, these studies identified novel
sequences for SHP-2 and JAK interactions that suggest unique signaling
mechanisms mediated by these two molecules.
Volume 272, Number 2,
Issue of January 10, 1997
pp. 1032-1037
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,¶
,¶
and§¶
Walther Oncology Center and
§ Departments of Medicine (Hematology/Oncology) and
¶ Biochemistry and Molecular Biology, Indiana University School of
Medicine, Indianapolis, Indiana 46202
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