Cysteine Substitution and Labeling Provide Insight into Channelrhodopsin-2 Ion Conductance

Biochemistry
Ryan Richards, Robert E Dempski

Abstract

Channelrhodopsin-2 is a light-activated cation channel. However, the mechanism of ion conductance is unresolved. Here, we performed cysteine scanning mutagenesis on transmembrane domain 7 followed by labeling with a methanethiosulfonate compound. Analysis of our results shows that residues that line the putative pore and interface with adjacent transmembrane domains 1 and 3, as proposed by our channelrhodopsin-2 homology model, affect ion conductance, decay kinetics, and/or off kinetics. Combined, these results suggest that negative charges at the extracellular side of transmembrane domain 7 funnel cations into the pore.

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Citations

Mar 12, 2021·Biophysical Journal·Monika R VanGordonSusan B Rempe
Dec 7, 2018·Analytical Biochemistry·Lindsey PrignanoRobert E Dempski

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