Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 21, Issue 20, Pages -Publisher
MDPI
DOI: 10.3390/ijms21207637
Keywords
protein kinase; phosphorylation; chemical genetics; conditional ATP analog-sensitive mutants; mass spectrometry; phosphoproteomics
Funding
- Slovak Research and Development Agency [APVV-16-0120]
- VEGA [2/0026/18, 2/0039/19]
- Operational Program Integrated Infrastructure for the project, center for advanced therapies of the chronic inflammatory diseases of the musculoskeletal system [313011W410]
- European Regional Development Fund
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Protein kinases are important enzymes involved in the regulation of various cellular processes. To function properly, each protein kinase phosphorylates only a limited number of proteins among the thousands present in the cell. This provides a rapid and dynamic regulatory mechanism that controls biological functions of the proteins. Despite the importance of protein kinases, most of their substrates remain unknown. Recently, the advances in the fields of protein engineering, chemical genetics, and mass spectrometry have boosted studies on identification of bona fide substrates of protein kinases. Among the various methods in protein kinase specific substrate identification, genetically engineered protein kinases and quantitative phosphoproteomics have become promising tools. Herein, we review the current advances in the field of chemical genetics in analog-sensitive protein kinase mutants and highlight selected strategies for identifying protein kinase substrates and studying the dynamic nature of protein phosphorylation.
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