Identification of the insulin-responsive tyrosine phosphorylation sites on IRSp53.

European Journal of Cell Biology
Man-Yeung HeungLaura M Machesky

Abstract

The 53-kDa insulin receptor substrate protein (IRSp53) is part of a regulatory network that organises the actin cytoskeleton in response to stimulation by small GTPases, promoting formation of actin-rich cell protrusions such as filopodia and lamellipodia. It had been established earlier that IRSp53 is tyrosine phosphorylated in response to stimulation of the insulin and insulin-related growth factor receptors, but the consequences of tyrosine phosphorylation for IRSp53 function are unknown. Here, we have used a variety of IRSp53 truncation and point mutants to identify insulin-responsive tyrosine phosphorylation sites on IRSp53. We have found that the C-terminal half of IRSp53 (residues 251-521) undergoes tyrosine phosphorylation in response to insulin stimulation of the insulin beta receptor or epidermal growth factor stimulation via the epidermal growth factor receptor, and that the key residue for insulin receptor-mediated phosphorylation is tyrosine 310, located in a region between the N-terminal IRSp53/MIM homology domain (IMD, residue 1-250) and the central SH3 domain (residues 374-438) that is predicted to be natively unstructured. Mutation of tyrosine 310 to phenylalanine or glutamic acid abrogates the phosphorylation ...Continue Reading

Citations

Mar 17, 2010·Neural Development·Shu-Ling Chiu, Hollis T Cline
Aug 16, 2011·FEBS Letters·Gang ChenXin Zhang
Nov 28, 2016·Journal of Neurochemistry·Matthias Gralle
Dec 7, 2018·The Journal of Cell Biology·Wilton T SneadJeanne C Stachowiak
Mar 21, 2019·Molecular Biology of the Cell·David J Kast, Roberto Dominguez
Jun 20, 2019·International Journal of Molecular Sciences·Chongchao WuZeguang Han

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