Phosphoproteomics Meets Chemical Genetics: Approaches for Global Mapping and Deciphering the Phosphoproteome

International Journal of Molecular Sciences

卷:21

Matus Jurcik¹  Lubos Cipak¹  Jan Jurcik¹  Ingrid Cipakova¹  Tomas Selicky¹  Michaela Osadska¹  Erika Stupenova²  Barbara Sivakova³  Peter Barath³ 

[1] Cancer Research Institute, Biomedical Research Center, Slovak Academy of Sciences, Dubravska cesta 9, 845 05 Bratislava, Slovakia;

[2] Department of Membrane Biochemistry, Institute of Animal Biochemistry and Genetics, Centre of Biosciences, Slovak Academy of Sciences, Dubravska cesta 9, 840 05 Bratislava, Slovakia;

[3] Institute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, 845 38 Bratislava, Slovakia;

关键词: protein kinase;    phosphorylation;    chemical genetics;    conditional ATP analog-sensitive mutants;    mass spectrometry;    phosphoproteomics;   

DOI  :  10.3390/ijms21207637

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown