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Genetically encoded biosensors for visualizing live-cell biochemical activity at super-resolution
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Genetically encoded biosensors for visualizing live-cell biochemical activity at super-resolution
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Journal Article
Genetically encoded biosensors for visualizing live-cell biochemical activity at super-resolution
2017
Overview
New fluorescent biosensors enable the first super-resolution imaging of enzyme activity in live cells via fluorescence fluctuation increase by contact (FLINC).
Compartmentalized biochemical activities are essential to all cellular processes, but there is no generalizable method to visualize dynamic protein activities in living cells at a resolution commensurate with cellular compartmentalization. Here, we introduce a new class of fluorescent biosensors that detect biochemical activities in living cells at a resolution up to threefold better than the diffraction limit. These 'FLINC' biosensors use binding-induced changes in protein fluorescence dynamics to translate kinase activities or protein–protein interactions into changes in fluorescence fluctuations, which are quantifiable through stochastic optical fluctuation imaging. A protein kinase A (PKA) biosensor allowed us to resolve minute PKA activity microdomains on the plasma membranes of living cells and to uncover the role of clustered anchoring proteins in organizing these activity microdomains. Together, these findings suggest that biochemical activities of the cell are spatially organized into an activity architecture whose structural and functional characteristics can be revealed by these new biosensors.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ 14/63
/ 96/10
/ Biomedical Engineering/Biotechnology
/ Biosensing Techniques - methods
/ Coding
/ Cyclic AMP-Dependent Protein Kinases - analysis
/ Cyclic AMP-Dependent Protein Kinases - metabolism
/ Enzymes
/ Fluorescence Resonance Energy Transfer - methods
/ Green Fluorescent Proteins - metabolism
/ Humans
/ Kinases
/ Microscopy - instrumentation
/ Protein Interaction Mapping - methods
/ Protein-protein interactions
/ Proteins
