Hauptseite > Publikationsdatenbank > Channelrhodopsin‐2 Oligomerization in Cell Membrane Revealed by Photo‐Activated Localization Microscopy > print

001     1023075
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024 7 _ |a 10.1002/anie.202307555
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100 1 _ |a Bestsennaia, Ekaterina
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245 _ _ |a Channelrhodopsin‐2 Oligomerization in Cell Membrane Revealed by Photo‐Activated Localization Microscopy
260 _ _ |a Weinheim
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520 _ _ |a Microbialrhodopsinsare retinalmembraneproteinsthat founda broadapplicationin optogenetics.Theoligomericstate of rhodopsinsis importantfor their functionalityand stability.Of particularinterestis the oligomericstate in the cellularnativemembraneenvironment.Fluorescencemicroscopyprovidespowerfultools to determinetheoligomericstate of membraneproteinsdirectlyin cells. Amongthese methodsis quantitativephotoactivatedlocalizationmicroscopy(qPALM)allowingthe investigationof molecularorganizationat the level of singleproteinclusters.Here,we applyqPALMto investigatethe oligomericstate of the first and most used optogenetictool Channelrhodopsin-2(ChR2)in the plasmamembraneof eukaryoticcells. ChR2appearedpredominantlyas a dimerin the cell membraneanddid not form higheroligomers.The disulfidebondsbetweenCys34and Cys36of adjacentChR2monomerswere notrequiredfor dimerformationand mutationsdisruptingthese bondsresultedin only partialmonomerizationof ChR2.The monomericfractionincreasedwhenthe total concentrationof mutantChR2in the membranewas low. Thedissociationconstantwas estimatedfor this partiallymonomerizedmutantChR2as 2.2�0.9 proteins/μm2. Our findingsare importantfor understandingthe mechanisticbasis of ChR2activityas well as for improvingexistingand developingfutureoptogenetictools.
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700 1 _ |a Gensch, Thomas
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700 1 _ |a Borshchevskiy, Valentin
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