| Literature DB >> 32423651 |
Colleen M Castellani1, Ana P Torres-Ocampo2, Jens Breffke3, Adam B White4, James J Chambers5, Margaret M Stratton2, Thomas J Maresca6.
Abstract
Förster resonance energy transfer (FRET)-based sensors have been powerful tools in cell biologists' toolkit for decades. Informed by fundamental understanding of fluorescent proteins, protein-protein interactions, and the structural biology of reporter components, researchers have been able to employ creative design approaches to build sensors that are uniquely capable of probing a wide range of phenomena in living cells including visualization of localized calcium signaling, sub-cellular activity gradients, and tension generation to name but a few. While FRET sensors have significantly impacted many fields, one must also be cognizant of the limitations to conventional, intensity-based FRET measurements stemming from variation in probe concentration, sensitivity to photobleaching, and bleed-through between the FRET fluorophores. Fluorescence lifetime imaging microscopy (FLIM) largely overcomes the limitations of intensity-based FRET measurements. In general terms, FLIM measures the time, which for the reporters described in this chapter is nanoseconds (ns), between photon absorption and emission by a fluorophore. When FLIM is applied to FRET sensors (FLIM-FRET), measurement of the donor fluorophore lifetime provides valuable information such as FRET efficiency and the percentage of reporters engaged in FRET. This chapter introduces fundamental principles of FLIM-FRET toward informing the practical application of the technique and, using two established FRET reporters as proofs of concept, outlines how to use a commercially available FLIM system.Entities:
Keywords: Camui; Cdk1; CyclinB1; FLIM; FRET; TCSPC
Mesh:
Substances:
Year: 2020 PMID: 32423651 PMCID: PMC8006575 DOI: 10.1016/bs.mcb.2020.02.002
Source DB: PubMed Journal: Methods Cell Biol ISSN: 0091-679X Impact factor: 1.441