The development of FRET (fluorescence resonance energy transfer)-based sensors for measuring cAMP has opened the door to sophisticated insights into single-cell cAMP dynamics. cAMP can be measured in distinct cell populations and even in distinct microdomains within cells. However, there is still only limited information on cAMP dynamics in excitable cells, particularly as a function of the activity of voltage-gated Ca2+ channels. A major reason for this is the pH shifts that can occur in excitable cells and their effects on fluorescent proteins.
- fluorescence resonance energy transfer (FRET)
Signalling 2011: a Biochemical Society Centenary Celebration: A Biochemical Society Focused Meeting held at the University of Edinburgh, U.K., 8–10 June 2011. Organized and Edited by Nicholas Brindle (Leicester, U.K.), Simon Cook (The Babraham Institute, U.K.), Jeff McIlhinney (Oxford, U.K.), Simon Morley (University of Sussex, U.K.), Sandip Patel (University College London, U.K.), Susan Pyne (University of Strathclyde, U.K.), Colin Taylor (Cambridge, U.K.), Alan Wallace (AstraZeneca, U.K.) and Stephen Yarwood (Glasgow, U.K.).
Abbreviations: AC, adenylate cyclase; camps, cAMP sensor; CCE, capacitative Ca2+ entry; CFP, cyan fluorescent protein; CNG, cyclic nucleotide-gated; ECFP, enhanced CFP; EGFP, enhanced green fluorescent protein; Epac, exchange protein directly activated by cAMP; EYFP, enhanced yellow fluorescent protein; FRET, fluorescence resonance energy transfer; GFP, green fluorescent protein; HCN2, hyperpolarization-activated CNG channel 2; mTFP1, monomeric teal fluorescent protein 1; NHE1, Na+/H+ exchanger 1; PKA, protein kinase A; VGCC, voltage-gated Ca2+ channel; YFP, yellow fluorescent protein
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