Tyrosine phosphorylation-dependent and -independent role of Shc in the regulation of IGF-1-induced mitogenesis and glycogen synthesis

Endocrinology

Volumn 142, Issue 12, 2001, Pages 5226-5235

  Sasaoka, Toshiyasu ^a   Ishiki, Manabu ^a   Wada, Tsutomu ^a   Hori, Hiroyuki ^a   Hirai, Hiroki ^a   Haruta, Tetsuro ^a   Ishihara, Hajime ^a   Kobayashi, Masashi ^a  

^a UNIVERSITY OF TOYAMA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN RECEPTOR SUBSTRATE 1; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN SHC; SOMATOMEDIN C; THYMIDINE; TYROSINE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DNA TRANSFECTION; ENZYME ACTIVATION; GLYCOGEN SYNTHESIS; MITOGENESIS; MYOBLAST; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN PHOSPHORYLATION; RAT;

EID: 0035213291     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.142.12.8543     Document Type: Article

References (40)

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8. Comparison of the insulin and insulin-like growth factor 1 mitogenic intracellular signaling pathways
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15. Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein
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34. Non-SH2 domains with insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor 1 receptor
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38. The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions
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