Functional Importance of Shc Tyrosine 317 on Insulin Signaling in Rat1 Fibroblasts Expressing Insulin Receptors

Shc is phosphorylated on Tyr-317, which serves as a docking site for Grb2. To investigate the specific role of Shc phosphorylation and ShcÂ·Grb2 coupling on insulin signaling, we generated expression vectors for wild-type (WT-Shc) and a mutant Shc with a Tyr-317 â Phe substitution (317Y/F-Shc) and...

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Veröffentlicht in:	The Journal of biological chemistry 1997-04, Vol.272 (14), p.9581-9586
Hauptverfasser:	Ishihara, H, Sasaoka, T, Ishiki, M, Takata, Y, Imamura, T, Usui, I, Langlois, W J, Sawa, T, Kobayashi, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Adaptor Proteins, Signal Transducing Adaptor Proteins, Vesicular Transport Animals Calcium-Calmodulin-Dependent Protein Kinases - metabolism Enzyme Activation Fibroblasts - metabolism GRB2 Adaptor Protein Humans Insulin - metabolism Insulin Receptor Substrate Proteins Mitosis Oligonucleotides, Antisense - pharmacology Phosphoproteins - chemistry Phosphoproteins - metabolism Phosphorylation Point Mutation Proteins - chemistry Proteins - metabolism Rats Receptor, Insulin - chemistry Receptor, Insulin - metabolism RNA, Messenger - metabolism Shc Signaling Adaptor Proteins Src Homology 2 Domain-Containing, Transforming Protein 1 src Homology Domains Structure-Activity Relationship Tyrosine
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