Abstract
Ciona voltage sensitive phosphatase (Ci-VSP) is an unique enzyme discovered first in asicdian genome, in which phosphatase activity is regulated by transmembrane potential. Ci-VSP consists of a phosphatase domain and a preceding voltage sensing domain (VSD) which is homologous to the S1-S4 transmembrane domain found in conventional voltage-gated ionic channels. Possible mechanism of Ci-VSP should be that changes in transmembrane potential elicit conformational changes in the VSD, which then induce conformational changes in the phosphatase domain, regulating enzymatic activity. Analogously, by replacing the phosphatase domain with two fluorescent proteins that act as fluorescence resonance energy transfer (FRET) donor and acceptor, it is expected that transmembrane potential can be optically probed as FRET readout. Using two new coral fluorescent proteins, we developed such a membrane potential reporter, named Mermaid, that displays 40% changes in emission ratio per 100 mV change, allowing for visualization of spatiotemporal dynamics in electrical activities of excitable cells. Notably, Mermaid has fast on-off kinetics at warm temperatures and can report voltage spikes comparable to action potentials.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
