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Type: Journal article
Title: Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses
Author: Hocking, B.
Conn, S.
Manohar, M.
Xu, B.
Athman, A.
Stancombe, M.
Webb, A.
Hirschi, K.
Gilliham, M.
Citation: Journal of Experimental Botany, 2017; 68(15):4171-4183
Publisher: Oxford University Press
Issue Date: 2017
ISSN: 0022-0957
Statement of
Bradleigh Hocking, Simon J. Conn, Murli Manohar, Bo Xu, Asmini Athman, Matthew A. Stancombe, Alex R. Webb, Kendal D. Hirschi and Matthew Gilliham
Abstract: Arabidopsis thaliana cation exchangers (CAX1 and CAX3) are closely related tonoplast-localized calcium/proton (Ca²⁺/H⁺) antiporters that contribute to cellular Ca²⁺ homeostasis. CAX1 and CAX3 were previously shown to interact in yeast; however, the function of this complex in plants has remained elusive. Here, we demonstrate that expression of CAX1 and CAX3 occurs in guard cells. Additionally, CAX1 and CAX3 are co-expressed in mesophyll tissue in response to wounding or flg22 treatment, due to the induction of CAX3 expression. Having shown that the transporters can be co-expressed in the same cells, we demonstrate that CAX1 and CAX3 can form homomeric and heteromeric complexes in plants. Consistent with the formation of a functional CAX1-CAX3 complex, CAX1 and CAX3 integrated into the yeast genome suppressed a Ca²⁺-hypersensitive phenotype of mutants defective in vacuolar Ca²⁺ transport, and demonstrated enzyme kinetics different from those of either CAX protein expressed by itself. We demonstrate that the interactions between CAX proteins contribute to the functioning of stomata, because stomata were more closed in cax1-1, cax3-1, and cax1-1/cax3-1 loss-of-function mutants due to an inability to buffer Ca²⁺ effectively. We hypothesize that the formation of CAX1-CAX3 complexes may occur in the mesophyll to affect intracellular Ca²⁺ signaling during defense responses.
Keywords: Calcium; guard cells; homeostasis; mesophyll; protein interaction; signalling; transport
Rights: © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
RMID: 0030072185
DOI: 10.1093/jxb/erx209
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