Arsenic-sensing domain controls ACR3 transporter trafficking and function in Marchantia polymorpha
Authors: Mizio, K., Bonter, I., Zbieralski, K., Dolzblasz, A., Tomaszewska, P., Staszewski, J., Wawrzycka, D., Reymer, A., Bialek, W., Kriechbaumer, V., Haseloff, J., Wysocki, R., Maciaszczyk-Dziubinska, E.
Category: Plant Biology
Model Organism: Marchantia polymorpha
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The study characterizes MpACR3, the ACR3 transporter orthologue from the liverwort Marchantia polymorpha, demonstrating its role as a metalloid/proton antiporter that confers arsenic resistance and moderate antimony tolerance. An N‑terminal arsenic‑sensing domain controls MpACR3 trafficking from the Golgi to the plasma membrane upon As(III) binding, and a conserved arginine motif influences both membrane accumulation and transport activity, indicating a plant‑specific adaptation to arsenic toxicity.