Journal
CELL STRUCTURE AND FUNCTION
Volume 43, Issue 1, Pages 61-74Publisher
JAPAN SOC CELL BIOLOGY
DOI: 10.1247/csf.18003
Keywords
kinase; FRET; phosphorylation; KTR
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Funding
- CREST
- JST [JPMJCR1654]
- JSPS KAKENHI Grants [JP16H01447, 26290053, 16H01425, 16KT0069]
- Hori Sciences and Arts Foundation
- Takeda Science Foundation
- Nakajima Foundation
- Grants-in-Aid for Scientific Research [15J08196, 17J08016] Funding Source: KAKEN
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Protein kinases play pivotal roles in intracellular signal transduction, and dysregulation of kinases leads to pathological results such as malignant tumors. Kinase activity has hitherto been measured by biochemical methods such as in vitro phosphorylation assay and western blotting. However, these methods are less useful to explore spatial and temporal changes in kinase activity and its cell-to-cell variation. Recent advances in fluorescent proteins and live-cell imaging techniques enable us to visualize kinase activity in living cells with high spatial and temporal resolutions. Several genetically encoded kinase activity reporters, which are based on the modes of action of kinase activation and phosphorylation, are currently available. These reporters are classified into single-fluorophore kinase activity reporters and Forster (or fluorescence) resonance energy transfer (FRET)-based kinase activity reporters. Here, we introduce the principles of genetically encoded kinase activity reporters, and discuss the advantages and disadvantages of these reporters.
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