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Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses
Arabidopsis thaliana cation exchangers (CAX1 and CAX3) are closely related tonoplast-localized calcium/proton (Ca(2+)/H(+)) antiporters that contribute to cellular Ca(2+) homeostasis. CAX1 and CAX3 were previously shown to interact in yeast; however, the function of this complex in plants has remain...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5853972/ https://www.ncbi.nlm.nih.gov/pubmed/28645169 http://dx.doi.org/10.1093/jxb/erx209 |
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author | Hocking, Bradleigh Conn, Simon J Manohar, Murli Xu, Bo Athman, Asmini Stancombe, Matthew A Webb, Alex R Hirschi, Kendal D Gilliham, Matthew |
author_facet | Hocking, Bradleigh Conn, Simon J Manohar, Murli Xu, Bo Athman, Asmini Stancombe, Matthew A Webb, Alex R Hirschi, Kendal D Gilliham, Matthew |
author_sort | Hocking, Bradleigh |
collection | PubMed |
description | Arabidopsis thaliana cation exchangers (CAX1 and CAX3) are closely related tonoplast-localized calcium/proton (Ca(2+)/H(+)) antiporters that contribute to cellular Ca(2+) 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 Ca(2+)-hypersensitive phenotype of mutants defective in vacuolar Ca(2+) 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 Ca(2+) effectively. We hypothesize that the formation of CAX1-CAX3 complexes may occur in the mesophyll to affect intracellular Ca(2+) signaling during defense responses. |
format | Online Article Text |
id | pubmed-5853972 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-58539722018-07-27 Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses Hocking, Bradleigh Conn, Simon J Manohar, Murli Xu, Bo Athman, Asmini Stancombe, Matthew A Webb, Alex R Hirschi, Kendal D Gilliham, Matthew J Exp Bot Research Papers Arabidopsis thaliana cation exchangers (CAX1 and CAX3) are closely related tonoplast-localized calcium/proton (Ca(2+)/H(+)) antiporters that contribute to cellular Ca(2+) 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 Ca(2+)-hypersensitive phenotype of mutants defective in vacuolar Ca(2+) 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 Ca(2+) effectively. We hypothesize that the formation of CAX1-CAX3 complexes may occur in the mesophyll to affect intracellular Ca(2+) signaling during defense responses. Oxford University Press 2017-07-10 2017-06-22 /pmc/articles/PMC5853972/ /pubmed/28645169 http://dx.doi.org/10.1093/jxb/erx209 Text en © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Papers Hocking, Bradleigh Conn, Simon J Manohar, Murli Xu, Bo Athman, Asmini Stancombe, Matthew A Webb, Alex R Hirschi, Kendal D Gilliham, Matthew Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses |
title | Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses |
title_full | Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses |
title_fullStr | Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses |
title_full_unstemmed | Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses |
title_short | Heterodimerization of Arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses |
title_sort | heterodimerization of arabidopsis calcium/proton exchangers contributes to regulation of guard cell dynamics and plant defense responses |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5853972/ https://www.ncbi.nlm.nih.gov/pubmed/28645169 http://dx.doi.org/10.1093/jxb/erx209 |
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