Large-scale profiling of protein kinases for cellular signaling studies by mass spectrometry and other techniques.
Protein phosphorylation mediated by protein kinases plays key roles in cellular signal transduction in both eukaryotic and prokaryotic organisms. Many researches have been conducted to investigate their functions and regulatory mechanisms, but these were mostly focused on particular kinases related to well-known signaling pathways, drug targets, diseases, and so on. Therefore our overall understanding of the whole set of kinases (the kinome), including their structural basis for substrate recognition, is still limited. In this review, we describe technologies for determination of sequence preference and physiological substrates of individual target kinases and for kinome-scale profiling, focusing on peptide array technology or proteomic approaches based on liquid chromatography-mass spectrometry (LC-MS).
Graduate School of Pharmaceutical Sciences, Kyoto University, 46-29 Yoshida-shimoadachi-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Naoyuki
N
Sugiyama
Graduate School of Pharmaceutical Sciences, Kyoto University, 46-29 Yoshida-shimoadachi-cho, Sakyo-ku, Kyoto 606-8501, Japan. Electronic address: yishiham@pharm.kyoto-u.ac.jp.
Yasushi
Y
Ishihama
D000818:Animals; D002458:Cell Fractionation / Q000379:methods*; D002853:Chromatography, Liquid / Q000379:methods; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D010766:Phosphorylation / Q000502:physiology; D011494:Protein Kinases / Q000032:analysis* / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction / Q000502:physiology; D053719:Tandem Mass Spectrometry / Q000379:methods*
D011494:Protein Kinases
Mass spectrometry; Protein kinase; Proteomics; Signal transduction