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Src homology 2 domains of protein tyrosine phosphatase are associated in vitro with both the insulin receptor and insulin receptor substrate‐1 via different phosphotyrosine motifs
Author(s) -
Ugi Satoshi,
Maegawa Hiroshi,
Olefsky Jerrold M.,
Shigeta Yukio,
Kashiwagi Atsunori
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80141-x
Subject(s) - sh2 domain , insulin receptor , proto oncogene tyrosine protein kinase src , insulin receptor substrate , protein tyrosine phosphatase , irs1 , phosphotyrosine binding domain , grb10 , biochemistry , receptor , biology , insulin , chemistry , microbiology and biotechnology , insulin resistance , endocrinology
To clarify the role of protein tyrosine phosphatase containing Src homology 2 (SH2) regions on insulin signaling, we investigated the interactions among the insulin receptor, a pair of SH2 domains of SH‐PTP2 coupled to glutathione‐ S ‐transferase (GST) and insulin receptor substrate‐1 (IRS‐1)‐GST fusion proteins (amino‐portion, IRS‐1N; carboxyl portion, IRS‐1C). GST‐SH2 protein of SH‐PTP2 bound to the wild type insulin receptor, but not to that with a carboxyl‐terminal mutation (Y/F2). Furthermore, even though Y/F2 receptors were used, the SH2 protein was also co‐immunoprecipitated with IRS‐1C, but not with IRS‐1N. These results indicate that SH2 domains of SH‐PTP2 can directly associate with the Y 1322 TXM motif on the carboxyl terminus of insulin receptors and also may bind to the carboxyl portion of IRS‐1, possibly via the V 1172 IDL motif in vitro.