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@ARTICLE{Lemke:1052091,
author = {Lemke, Moritz and Lakomek, Nils Alexander and Groth, Georg},
title = {{S}tructural dynamics of the plant hormone receptor {ETR}1
in a native‐like membrane environment},
journal = {FEBS letters},
volume = {599},
number = {22},
issn = {0014-5793},
address = {Chichester},
publisher = {Wiley},
reportid = {FZJ-2026-00756},
pages = {3381 - 3391},
year = {2025},
abstract = {Ethylene (C2H4) regulates plant processes, such as
germination, fruit ripening, and stress responses, impacting
nutrition and food quality. The membrane-bound receptor ETR1
from Arabidopsis thaliana is a model for ethylene signaling,
but both full-length and the soluble cytoplasmic domain have
resisted crystallization. We present high-resolution NMR
spectra of full-length ETR1 reconstituted in lipid
nanodiscs, overcoming limitations and enhancing sample
uniformity. ETR1 shows high internal dynamics with regions
decoupled from the transmembrane domain, possibly explaining
past crystallization failures and reflecting functional
flexibility. Introduction of Cu(I), an essential cofactor
for ethylene binding, stiffened receptor dynamics,
suggesting a stabilizing role in signal transmission. This
work demonstrates nanodisc-based strategies as powerful
tools for resolving membrane protein structures in plant
signaling.},
cin = {IBI-7},
ddc = {610},
cid = {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 = {10.1002/1873-3468.70153},
url = {https://juser.fz-juelich.de/record/1052091},
}