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KMID : 0390320070170020168
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Chungbuk Medical Journal
2007 Volume.17 No. 2 p.168 ~ p.175
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Identification Of Serine/Threonine Phosphorylation Sites Of Insulin Receptor Substrate-1 (IRS-1) By Mass Spectrometry
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Lee Yong-Hee
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Abstract
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Purpose: Multisite serine/threonine phosphorylation of insulin receptor substrate-1 (IRS-1) protein regulates insulin/IGF-1 signaling and is an important mechanism contributing to insulin resistance. We sought to identify multiple phosphorylation sites in IRS-1 using mass spectrometry.
Materials and Methods: HPLC Tandem mass spectrometry (LC-MS/MS) was employeded to identify new serine/threonine phosphorylation sites in IRS-1 protein that was immunoprecipitated from insulin-stimulated CHO cells overexpressing insulin receptor and IRS-1.
Results: We report the in vivo identification of more than 40 phosphoserine or phosphothreonine residues in IRS-1. The identified phosphoserine/phosphothreonine residues were located in consensus phosphorylation sites for various kinases, including AGC and proline-directed kinases.
Conclusion: Identification of serine/threonine phosphorylation sites in IRS-1 protein will substantively contribute to our understanding of the molecular basis of insulin resistance and associated heath disorders.
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KEYWORD
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Insulin resistance, IRS-1, Phosphorylation, Mass spectrometry
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