Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Huang, Ya-Nan, Yang, Shun-Ying, Li, Jun-Lin, Wang, Shao-Fei, Wang, Jia-Jin, Hao, Dong-Li, Su, Yan-Hua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2021
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
_version_ 1784610084675911680
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
work_keys_str_mv AT huangyanan therectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT yangshunying therectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT lijunlin therectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT wangshaofei therectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT wangjiajin therectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT haodongli therectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT suyanhua therectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT huangyanan rectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT yangshunying rectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT lijunlin rectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT wangshaofei rectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT wangjiajin rectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT haodongli rectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2
AT suyanhua rectificationcontrolandphysiologicalrelevanceofpotassiumchannelosakt2