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

被引:35
作者
UGI, S
MAEGAWA, H
OLEFSKY, JM
SHIGETA, Y
KASHIWAGI, A
机构
[1] SHIGA UNIV MED SCI, DEPT MED 3, OTSU, SHIGA 52021, JAPAN
[2] UNIV CALIF SAN DIEGO, DEPT MED, LA JOLLA, CA 92093 USA
关键词
INSULIN RECEPTOR; PROTEIN TYROSINE PHOSPHATASE; INSULIN RECEPTOR SUBSTRATE-1; SRC HOMOLOGY 2; PHOSPHOTYROSINE MOTIF;
D O I
10.1016/0014-5793(94)80141-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Y(1172)IDL motif in vitro.
引用
收藏
页码:216 / 220
页数:5
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