The insulin-like growth factor I receptor-induced interaction of insulin receptor substrate-4 and Crk-II

Endocrinology
M KarasD Leroith

Abstract

Stimulation of the insulin or insulin-like growth factor (IGF)-I receptor results in activation of several signaling pathways. Proteins of the insulin receptor substrate (IRS) family play important roles in mediating these signaling cascades. To date, four members of the IRS family of docking proteins have been characterized. Recently, we have reported that stimulation of the IGF-I receptor in 293 HEK cells regulates interaction of the newly discovered IRS-4 molecule with the Crk family of proteins. In the present study, we characterize the molecular basis of these interactions. C- and N termini truncation analysis of IRS-4 demonstrated that the region between amino acids 678 and 800 of the IRS-4 molecule is involved in this interaction. This region contains a cluster of four tyrosines (Y(700), Y(717), Y(743), and Y(779)). We hypothesize that one or more of these tyrosines are involved in the interaction between the SH2 domain of the Crk-II molecule when IRS-4 is phosphorylated upon IGF-I receptor activation. Additional mutational analyses confirmed this hypothesis. Interestingly, none of these four tyrosines was individually critical for the interaction between Crk-II and IRS-4, but when all four tyrosines were simultaneously ...Continue Reading

References

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Citations

Jun 19, 2009·Cell Communication and Signaling : CCS·Katerina MardilovichLeslie M Shaw
Apr 29, 2005·Molecular Pain·Jeremy J Van BurenLouis S Premkumar
Jun 5, 2013·Cell Biochemistry and Biophysics·Chiranjib ChakrabortyS A Syed Haneef
May 5, 2005·Oncogene·Haoqun QiuW Todd Miller
Dec 13, 2006·Microbiology and Molecular Biology Reviews : MMBR·Marie A Bogoyevitch, Bostjan Kobe
Jul 16, 2021·The Journal of Biological Chemistry·Matthea R SandersonRachel Wevrick

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