Citation: Zhi Li Li. Direct observation of the autophosphorylation of insulin receptor kinase by mass spectrometry[J]. Chinese Chemical Letters, ;2009, 20(2): 204-206. doi: 10.1016/j.cclet.2008.10.043 shu

Direct observation of the autophosphorylation of insulin receptor kinase by mass spectrometry

Zhi Li Li

Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and School of Basic Medicine, Peking Union Medical College, Beijing 100005, China

Received Date: 17 July 2008

Fund Project: This work was supported by National Natural Sciences Foundation of China (No. 20675088) and the National High Technology Research and Development Program (No. 2006AA02Z154).

The catalytic and signaling activities of insulin receptor kinase (IRK) are regulated by the autophosphorylation of three tyrosine residues in a cytoplasmic protein-tyrosine kinase domain at Tyro 1158, Tyro 1162 and Tyro 1163. In this study, time-course of the auphosphorylation of the core kinase (residues 978-1283) from IRK was directly investigated by online electrospray ionization mass spectrometry. It is found that two tyrosine residues were phosphorylated in reaction time range of 30 min. This study implies that mass spectrometric technique must be a powerful tool to directly monitor the biological macromolecular modification and will also provide the information of the order and the mechanism of autophosphorylation at the tyrosine sites coupled with tandem mass spectrometric technique.
- Phosphorylation,
- Insulin receptor kinase,
- Mass spectrometry,
- Time course
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