Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 1140120060110010001
Cancer Prevention Research
2006 Volume.11 No. 1 p.1 ~ p.8
Protein Phosphorylation as a Regulatory Mechanism of Various Cellular Function
Ahn Jae-Yeon

Lee Eung-Ryoung
Kim Jang-Yong
Cho Ssang-Goo
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.
KEYWORD
Phosphorylation, MAPK, Proteomics, ROS, PI3K, CDK
FullTexts / Linksout information
 
Listed journal information
ÇмúÁøÈïÀç´Ü(KCI) ´ëÇÑÀÇÇÐȸ ȸ¿ø