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TitleStructural basis of CAX1 autoinhibition by its amino-terminal domain in Arabidopsis thaliana.
Journal, issue, pagesNat Plants, Vol. 11, Issue 10, Page 2072-2083, Year 2025
Publish dateSep 2, 2025
AuthorsKun Wang / Chunhui Ma / Guanglin Chen / Zhisen Yang / Yongxiang Gao / Zhiyong Zhang / Xin Liu / Linfeng Sun /
PubMed AbstractCalcium homeostasis is tightly regulated due to the essential roles of calcium ions (Ca) in various cellular processes. CAX1 in Arabidopsis thaliana (AtCAX1) serves as a Ca/H exchanger transporting ...Calcium homeostasis is tightly regulated due to the essential roles of calcium ions (Ca) in various cellular processes. CAX1 in Arabidopsis thaliana (AtCAX1) serves as a Ca/H exchanger transporting excess cytosolic Ca into the vacuole, which is modulated by kinase phosphorylation in response to diverse signals. However, the regulatory mechanism remains unclear. Here we present the structures of wild-type AtCAX1 in an inactivated state and a phosphomimetic mutant in an activated state. In the wild-type structure, the amino-terminal region forms an α-helix that blocks the transport tunnel, thus inhibiting its transport activity. In contrast, in the phosphomimetic mutant structure, this blocking helix is released from the tunnel, leading to AtCAX1 activation. Conformational changes are also observed in the transmembrane domain. Together, these findings provide insights into the transport mechanism of the Ca/H exchangers and set up a basis for future studies of the regulation of calcium homeostasis in plants.
External linksNat Plants / PubMed:40897811
MethodsEM (single particle)
Resolution3.4 Å
Structure data

65301

9vsd

EMDB-65301, PDB-9vsd:
Structure of the phosphomimetic mutant CAX1 in Arabidopsis thaliana in the apo state
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSPORT PROTEIN / Calcium;Transporter;Proton;CAX1

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