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The rectification control and physiological relevance of potassium channel OsAKT2
AKT2 potassium (K(+)) channels are members of the plant Shaker family which mediate dual-directional K(+) transport with weak voltage-dependency. Here we show that OsAKT2 of rice (Oryza sativa) functions mainly as an inward rectifier with strong voltage-dependency and acutely suppressed outward acti...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8644434/ https://www.ncbi.nlm.nih.gov/pubmed/34601582 http://dx.doi.org/10.1093/plphys/kiab462 |
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author | Huang, Ya-Nan Yang, Shun-Ying Li, Jun-Lin Wang, Shao-Fei Wang, Jia-Jin Hao, Dong-Li Su, Yan-Hua |
author_facet | Huang, Ya-Nan Yang, Shun-Ying Li, Jun-Lin Wang, Shao-Fei Wang, Jia-Jin Hao, Dong-Li Su, Yan-Hua |
author_sort | Huang, Ya-Nan |
collection | PubMed |
description | AKT2 potassium (K(+)) channels are members of the plant Shaker family which mediate dual-directional K(+) transport with weak voltage-dependency. Here we show that OsAKT2 of rice (Oryza sativa) functions mainly as an inward rectifier with strong voltage-dependency and acutely suppressed outward activity. This is attributed to the presence of a unique K191 residue in the S4 domain. The typical bi-directional leak-like property was restored by a single K191R mutation, indicating that this functional distinction is an intrinsic characteristic of OsAKT2. Furthermore, the opposite R195K mutation of AtAKT2 changed the channel to an inward-rectifier similar to OsAKT2. OsAKT2 was modulated by OsCBL1/OsCIPK23, evoking the outward activity and diminishing the inward current. The physiological relevance in relation to the rectification diversity of OsAKT2 was addressed by functional assembly in the Arabidopsis (Arabidopsis thaliana) akt2 mutant. Overexpression (OE) of OsAKT2 complemented the K(+) deficiency in the phloem sap and leaves of the mutant plants but did not significantly contribute to the transport of sugars. However, the expression of OsAKT2-K191R overcame both the shortage of phloem K(+) and sucrose of the akt2 mutant, which was comparable to the effects of the OE of AtAKT2, while the expression of the inward mutation AtAKT2-R195K resembled the effects of OsAKT2. Additionally, OE of OsAKT2 ameliorated the salt tolerance of Arabidopsis. |
format | Online Article Text |
id | pubmed-8644434 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-86444342021-12-06 The rectification control and physiological relevance of potassium channel OsAKT2 Huang, Ya-Nan Yang, Shun-Ying Li, Jun-Lin Wang, Shao-Fei Wang, Jia-Jin Hao, Dong-Li Su, Yan-Hua Plant Physiol Focus Issue on Transport and Signaling AKT2 potassium (K(+)) channels are members of the plant Shaker family which mediate dual-directional K(+) transport with weak voltage-dependency. Here we show that OsAKT2 of rice (Oryza sativa) functions mainly as an inward rectifier with strong voltage-dependency and acutely suppressed outward activity. This is attributed to the presence of a unique K191 residue in the S4 domain. The typical bi-directional leak-like property was restored by a single K191R mutation, indicating that this functional distinction is an intrinsic characteristic of OsAKT2. Furthermore, the opposite R195K mutation of AtAKT2 changed the channel to an inward-rectifier similar to OsAKT2. OsAKT2 was modulated by OsCBL1/OsCIPK23, evoking the outward activity and diminishing the inward current. The physiological relevance in relation to the rectification diversity of OsAKT2 was addressed by functional assembly in the Arabidopsis (Arabidopsis thaliana) akt2 mutant. Overexpression (OE) of OsAKT2 complemented the K(+) deficiency in the phloem sap and leaves of the mutant plants but did not significantly contribute to the transport of sugars. However, the expression of OsAKT2-K191R overcame both the shortage of phloem K(+) and sucrose of the akt2 mutant, which was comparable to the effects of the OE of AtAKT2, while the expression of the inward mutation AtAKT2-R195K resembled the effects of OsAKT2. Additionally, OE of OsAKT2 ameliorated the salt tolerance of Arabidopsis. Oxford University Press 2021-10-02 /pmc/articles/PMC8644434/ /pubmed/34601582 http://dx.doi.org/10.1093/plphys/kiab462 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Focus Issue on Transport and Signaling Huang, Ya-Nan Yang, Shun-Ying Li, Jun-Lin Wang, Shao-Fei Wang, Jia-Jin Hao, Dong-Li Su, Yan-Hua The rectification control and physiological relevance of potassium channel OsAKT2 |
title | The rectification control and physiological relevance of potassium channel OsAKT2 |
title_full | The rectification control and physiological relevance of potassium channel OsAKT2 |
title_fullStr | The rectification control and physiological relevance of potassium channel OsAKT2 |
title_full_unstemmed | The rectification control and physiological relevance of potassium channel OsAKT2 |
title_short | The rectification control and physiological relevance of potassium channel OsAKT2 |
title_sort | rectification control and physiological relevance of potassium channel osakt2 |
topic | Focus Issue on Transport and Signaling |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8644434/ https://www.ncbi.nlm.nih.gov/pubmed/34601582 http://dx.doi.org/10.1093/plphys/kiab462 |
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