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Journal of Cancer Prevention

Review

Cancer prevention research 2006; 11(1): 1-8

Published online March 30, 2006

© Korean Society of Cancer Prevention

Protein Phosphorylation as a Regulatory Mechanism of Various Cellular Function

Jae Yeon Ahn, Eung-Ryoung Lee, Jang-Yong Kim and Ssang-Goo Cho

Abstract

Lots of oncogenics factors including signaling molecules, reactive oxygen species, and receptor proteins are closely involved in protein phosphorylation. Protein phosphorylation is probably one of the most studied post-translational modification mechanism which is very important for regulating the activities of important regulatory proteins in cellular signaling pathways. Here, we shortly presented recent advances in the protein phosphorylation research. Despite of the many studies, more extensive and specific research tools are needed for more comprehensive understanding of the exact molecular targets and functions of the cellular kinases. Recently, several proteomics tools are developed to analyze the phosphoproteomes or kinomes and this highthroughput study on the protein phosphorylation would be very helpful for understanding the mechanisms of many cellular functions such as cell cycle, aging, cancer or neurodegeneration. For the proteomics study, more works are needed to be done with phosphopeptides, but phosphopeptides are difficult to analyse due to the poor ionising capacity under standard MALDI conditions. Several methods have been developed to deal with the low sensitivity and specificity of the phosphopeptide analysis. The optimisation of the approach is described for a standard model peptide and protein. (Cancer Prev Res 11, 1-8, 2006)

Keywords: Phosphorylation, MAPK, Proteomics, ROS, PI3K, CDK

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