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@ARTICLE{Bestsennaia:1024667,
author = {Bestsennaia, Ekaterina and Maslov, Ivan and Balandin, Taras
and Alekseev, Alexey and Yudenko, Anna and Abu Shamseye,
Assalla and Zabelskii, Dmitrii and Baumann, Arnd and
Catapano, Claudia and Karathanasis, Christos and Gordeliy,
Valentin and Heilemann, Mike and Gensch, Thomas and
Borshchevskiy, Valentin},
title = {{C}hannelrhodopsin‐2 {O}ligomerization in {C}ell
{M}embrane {R}evealed by {P}hoto‐{A}ctivated
{L}ocalization {M}icroscopy},
journal = {Angewandte Chemie},
volume = {136},
number = {11},
issn = {0932-2132},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {FZJ-2024-02340},
pages = {e202307555},
year = {2024},
note = {We are thankful to Fedor Tsybrov for the help with
thepreparation of plasmids. V.B. acknowledges DAAD
YoungTalents Programme Line A. V.G. acknowledges his
HGFProfessorship. I.M. acknowledges FWO Research
FoundationFlanders (G0B9922N) and BOF UHasselt(BOF21BL11).
C.C., C.K. and M.H. gratefully acknowledgethe Deutsche
Forschungsgemeinschaft (grants CRC1507 andCRC807) for
financial support. The work was done in theframework of
CEA(IBS)–HGF(FZJ) STC 5.1 specific agreement.Open Access
funding enabled and organized byProjekt DEAL.},
abstract = {Microbial rhodopsins are retinal membrane proteins that
found a broad application in optogenetics. The oligomeric
state of rhodopsins is important for their functionality and
stability. Of particular interest is the oligomeric state in
the cellular native membrane environment. Fluorescence
microscopy provides powerful tools to determine the
oligomeric state of membrane proteins directly in cells.
Among these methods is quantitative photoactivated
localization microscopy (qPALM) allowing the investigation
of molecular organization at the level of single protein
clusters. Here, we apply qPALM to investigate the oligomeric
state of the first and most used optogenetic tool
Channelrhodopsin-2 (ChR2) in the plasma membrane of
eukaryotic cells. ChR2 appeared predominantly as a dimer in
the cell membrane and did not form higher oligomers. The
disulfide bonds between Cys34 and Cys36 of adjacent ChR2
monomers were not required for dimer formation and mutations
disrupting these bonds resulted in only partial
monomerization of ChR2. The monomeric fraction increased
when the total concentration of mutant ChR2 in the membrane
was low. The dissociation constant was estimated for this
partially monomerized mutant ChR2 as 2.2±0.9 proteins/μm2.
Our findings are important for understanding the mechanistic
basis of ChR2 activity as well as for improving existing and
developing future optogenetic tools.},
cin = {IBI-1 / IBI-7},
ddc = {660},
cid = {I:(DE-Juel1)IBI-1-20200312 / I:(DE-Juel1)IBI-7-20200312},
pnm = {5241 - Molecular Information Processing in Cellular Systems
(POF4-524)},
pid = {G:(DE-HGF)POF4-5241},
typ = {PUB:(DE-HGF)16},
doi = {10.1002/ange.202307555},
url = {https://juser.fz-juelich.de/record/1024667},
}