1. Developing novel methods to search for substrates of protein kinases such as Rho-kinase.
- Author
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Nishioka T, Shohag MH, Amano M, and Kaibuchi K
- Subjects
- Amino Acid Sequence, Mass Spectrometry, Phosphorylation drug effects, Substrate Specificity, rho-Associated Kinases chemistry, Protein Kinase Inhibitors chemistry, Proteomics, rho-Associated Kinases metabolism
- Abstract
Protein phosphorylation is a major and essential post-translational modification in eukaryotic cells that plays a critical role in various cellular processes. Recent progresses in mass spectrometry techniques have enabled the effective identification and analysis of protein phosphorylation. Mass spectrometry-based approaches in investigating protein phosphorylation are very powerful and informative and can further improve our understanding of protein phosphorylation as a whole, but they cannot determine the upstream kinases involved. We introduce several studies that attempted to uncover the relationships between various kinases of interest and substrates, including two methods we developed: an in vitro approach termed the kinase-interacting substrate screening (KISS) method and an in vivo approach termed the phosphatase inhibitor and kinase inhibitor substrate screening (PIKISS) method. This article is part of a Special Issue entitled: Inhibitors of Protein Kinases., (Copyright © 2015 Elsevier B.V. All rights reserved.)
- Published
- 2015
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