Arsenic-sensing domain controls ACR3 transporter trafficking in Marchantia polymorpha.
8 affiliations
- 1Department of Genetics and Cell Physiology, Faculty of Biological Sciences, University of Wroclaw, Kanonia 6/8, 50-328 Wroclaw, Poland.
- 2Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge CB2 3EA, United Kingdom.
- 3Department of Plant Developmental Biology, Faculty of Biological Sciences, University of Wroclaw, Kanonia 6/8, 50-328 Wroclaw, Poland.
- 4Genetics and Genome Biology, University of Leicester, Leicester LE1 7RH, United Kingdom.
- 5Department of Chemistry and Molecular Biology, University of Gothenburg, Göteborg 405 30, Sweden.
- 6Université Grenoble Alpes, Inserm U 1209, CNRS UMR 5309, ReTraD, Institute for Advanced Biosciences, Grenoble 38000, France.
- 7Department of Biophysics, Faculty of Biotechnology, University of Wroclaw, F. Joliot-Curie 14a, 50-383 Wroclaw, Poland.
- 8School of Biological and Medical Sciences and Centre for Bioimaging, Oxford Brookes University, Gipsy Lane, Headington, Oxford OX3 0BP, United Kingdom.
Abstract
Arsenic is a toxic, carcinogenic metalloid that threatens human health through contaminated water and food. Arsenite [As(III)] efflux mediated by ACR3 transporters is an ancient detoxification mechanism conserved across prokaryotes, fungi, algae, and non-angiosperm land plants, yet plant ACR3 proteins remain poorly characterized. Here, we show that MpACR3, the ACR3 ortholog from the model liverwort Marchantia polymorpha, contains an arsenic-responsive N-terminal domain that regulates intracellular trafficking. Under nonstress conditions, MpACR3 is detected in Golgi bodies as well as at the plasma membrane (PM) in plant cells, whereas As(III) promotes its relocalization to the PM. As(III) interacts with a cysteine-rich N-terminal region and stabilizes this domain, as shown by arsenite-biotin competition and increased protease resistance. Together with molecular dynamics simulations, which predict As(III)-dependent changes in secondary structure and surface properties, these findings support a model in which ligand-induced remodeling of the N-terminus modulates MpACR3 retention and trafficking. We further identify a di-arginine-containing LRCRF motif in which leucine and arginine residues are required for intracellular retention, whereas cysteine and phenylalanine residues are required for As(III)-induced relocalization to the PM. The broad conservation of related N-terminal domains in plant ACR3 transporters suggests that arsenic-regulated trafficking is a conserved plant adaptation to arsenic toxicity.
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BibTeX
@article{bonter2026arsenicsensing,
title = {{Arsenic-sensing domain controls ACR3 transporter trafficking in Marchantia polymorpha.}},
author = {Ignacy Bonter and Katarzyna Mizio and Alicja Dolzblasz and Paulina Tomaszewska and Kacper Zbieralski and Jacek Staszewski and Donata Wawrzycka and Anna Reymer and Wojciech Bialek and Verena Kriechbaumer and Jim Haseloff and Robert Wysocki and Ewa Maciaszczyk-Dziubinska},
journal = {The Plant cell},
year = {2026},
month = oct,
doi = {10.1093/plcell/koag306},
url = {https://europepmc.org/article/MED/42837615},
note = {CC BY},
}
RIS
TY - JOUR
TI - Arsenic-sensing domain controls ACR3 transporter trafficking in Marchantia polymorpha.
AU - Ignacy Bonter
AU - Katarzyna Mizio
AU - Alicja Dolzblasz
AU - Paulina Tomaszewska
AU - Kacper Zbieralski
AU - Jacek Staszewski
AU - Donata Wawrzycka
AU - Anna Reymer
AU - Wojciech Bialek
AU - Verena Kriechbaumer
AU - Jim Haseloff
AU - Robert Wysocki
AU - Ewa Maciaszczyk-Dziubinska
PY - 2026
DA - 2026/10/01
JO - The Plant cell
DO - 10.1093/plcell/koag306
UR - https://europepmc.org/article/MED/42837615
AB - Arsenic is a toxic, carcinogenic metalloid that threatens human health through contaminated water and food. Arsenite [As(III)] efflux mediated by ACR3 transporters is an ancient detoxification mechanism conserved across prokaryotes, fungi, algae, and non-angiosperm land plants, yet plant ACR3 proteins remain poorly characterized. Here, we show that MpACR3, the ACR3 ortholog from the model liverwort Marchantia polymorpha, contains an arsenic-responsive N-terminal domain that regulates intracellular trafficking. Under nonstress conditions, MpACR3 is detected in Golgi bodies as well as at the plasma membrane (PM) in plant cells, whereas As(III) promotes its relocalization to the PM. As(III) interacts with a cysteine-rich N-terminal region and stabilizes this domain, as shown by arsenite-biotin competition and increased protease resistance. Together with molecular dynamics simulations, which predict As(III)-dependent changes in secondary structure and surface properties, these findings support a model in which ligand-induced remodeling of the N-terminus modulates MpACR3 retention and trafficking. We further identify a di-arginine-containing LRCRF motif in which leucine and arginine residues are required for intracellular retention, whereas cysteine and phenylalanine residues are required for As(III)-induced relocalization to the PM. The broad conservation of related N-terminal domains in plant ACR3 transporters suggests that arsenic-regulated trafficking is a conserved plant adaptation to arsenic toxicity.
SN - 1040-4651
SN - 1532-298X
ER -