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• W2076749701 abstract "The β-strands of GFP form a rigid barrel that protects the chromophore from external influence. Herein, we identified specific mutations in β-strand 7 that render the chromophore sensitive to interactions of GFP with another protein domain. In the process of converting the FRET-based protein kinase A (PKA) sensor AKAR2 into a single-wavelength PKA sensor containing a GFP and a quencher, we discovered that the quencher was not required and that the sensor response relied on changes in GFP intrinsic fluorescence. The identified mutations in β-strand 7 render GFP fluorescence intensity and lifetime sensitive to conformational changes of the PKA-sensing domain. In addition, sensors engineered from the GCaMP2 calcium indicator to incorporate a conformation-sensitive GFP (csGFP) exhibited calcium-dependent fluorescence changes. We further demonstrate that single GFP sensors report PKA dynamics in dendritic spines of neurons from brain slices on 2-photon imaging with a high signal-to-baseline ratio and minimal photobleaching. The susceptibility of GFP variants to dynamic interactions with other protein domains provides a new approach to generate single wavelength biosensors for high-resolution imaging." @default.
• W2076749701 created "2016-06-24" @default.
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• W2076749701 date "2013-12-12" @default.
• W2076749701 modified "2023-10-15" @default.
• W2076749701 title "Single‐fluorophore biosensors based on conformation‐sensitive GFP variants" @default.
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• W2076749701 doi "https://doi.org/10.1096/fj.13-240507" @default.
• W2076749701 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3929668" @default.
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• W2076749701 hasPublicationYear "2013" @default.
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