TY  - JOUR
AU  - Lemke, Moritz
AU  - Lakomek, Nils Alexander
AU  - Groth, Georg
TI  - Structural dynamics of the plant hormone receptor ETR1 in a native‐like membrane environment
JO  - FEBS letters
VL  - 599
IS  - 22
SN  - 0014-5793
CY  - Chichester
PB  - Wiley
M1  - FZJ-2026-00756
SP  - 3381 - 3391
PY  - 2025
AB  - 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.
LB  - PUB:(DE-HGF)16
DO  - DOI:10.1002/1873-3468.70153
UR  - https://juser.fz-juelich.de/record/1052091
ER  -