Cargando…

The uniqueness of the plant mitochondrial potassium channel

The ATP-inhibited Plant Mitochondrial K(+) Channel (PmitoK(ATP)) was discovered about fifteen years ago in Durum Wheat Mitochondria (DWM). PmitoKATP catalyses the electrophoretic K(+) uniport through the inner mitochondrial membrane; moreover, the co-operation between PmitoK(ATP) and (+)/H(+) antipo...

Descripción completa

Detalles Bibliográficos
Autores principales: Pastore, Donato, Soccio, Mario, Laus, Maura Nicoletta, Trono, Daniela
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Biochemistry and Molecular Biology 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4133908/
https://www.ncbi.nlm.nih.gov/pubmed/23977986
http://dx.doi.org/10.5483/BMBRep.2013.46.8.075
_version_ 1782330813601284096
author Pastore, Donato
Soccio, Mario
Laus, Maura Nicoletta
Trono, Daniela
author_facet Pastore, Donato
Soccio, Mario
Laus, Maura Nicoletta
Trono, Daniela
author_sort Pastore, Donato
collection PubMed
description The ATP-inhibited Plant Mitochondrial K(+) Channel (PmitoK(ATP)) was discovered about fifteen years ago in Durum Wheat Mitochondria (DWM). PmitoKATP catalyses the electrophoretic K(+) uniport through the inner mitochondrial membrane; moreover, the co-operation between PmitoK(ATP) and (+)/H(+) antiporter allows such a great operation of a K(+) cycle to collapse mitochondrial membrane potential (ΔΨ) and ΔpH, thus impairing protonmotive force (Δp). A possible physiological role of such ΔΨ control is the restriction of harmful reactive oxygen species (ROS) production under environmental/oxidative stress conditions. Interestingly, DWM lacking Δp were found to be nevertheless fully coupled and able to regularly accomplish ATP synthesis; this unexpected behaviour makes necessary to recast in some way the classical chemiosmotic model. In the whole, PmitoK(ATP) may oppose to large scale ROS production by lowering ΔΨ under environmental/oxidative stress, but, when stress is moderate, this occurs without impairing ATP synthesis in a crucial moment for cell and mitochondrial bioenergetics. [BMB Reports 2013; 46(8): 391-397]
format Online
Article
Text
id pubmed-4133908
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Korean Society for Biochemistry and Molecular Biology
record_format MEDLINE/PubMed
spelling pubmed-41339082014-09-16 The uniqueness of the plant mitochondrial potassium channel Pastore, Donato Soccio, Mario Laus, Maura Nicoletta Trono, Daniela BMB Rep Review Article The ATP-inhibited Plant Mitochondrial K(+) Channel (PmitoK(ATP)) was discovered about fifteen years ago in Durum Wheat Mitochondria (DWM). PmitoKATP catalyses the electrophoretic K(+) uniport through the inner mitochondrial membrane; moreover, the co-operation between PmitoK(ATP) and (+)/H(+) antiporter allows such a great operation of a K(+) cycle to collapse mitochondrial membrane potential (ΔΨ) and ΔpH, thus impairing protonmotive force (Δp). A possible physiological role of such ΔΨ control is the restriction of harmful reactive oxygen species (ROS) production under environmental/oxidative stress conditions. Interestingly, DWM lacking Δp were found to be nevertheless fully coupled and able to regularly accomplish ATP synthesis; this unexpected behaviour makes necessary to recast in some way the classical chemiosmotic model. In the whole, PmitoK(ATP) may oppose to large scale ROS production by lowering ΔΨ under environmental/oxidative stress, but, when stress is moderate, this occurs without impairing ATP synthesis in a crucial moment for cell and mitochondrial bioenergetics. [BMB Reports 2013; 46(8): 391-397] Korean Society for Biochemistry and Molecular Biology 2013-08 /pmc/articles/PMC4133908/ /pubmed/23977986 http://dx.doi.org/10.5483/BMBRep.2013.46.8.075 Text en Copyright © 2013, Korean Society for Biochemistry and Molecular Biology http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Pastore, Donato
Soccio, Mario
Laus, Maura Nicoletta
Trono, Daniela
The uniqueness of the plant mitochondrial potassium channel
title The uniqueness of the plant mitochondrial potassium channel
title_full The uniqueness of the plant mitochondrial potassium channel
title_fullStr The uniqueness of the plant mitochondrial potassium channel
title_full_unstemmed The uniqueness of the plant mitochondrial potassium channel
title_short The uniqueness of the plant mitochondrial potassium channel
title_sort uniqueness of the plant mitochondrial potassium channel
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4133908/
https://www.ncbi.nlm.nih.gov/pubmed/23977986
http://dx.doi.org/10.5483/BMBRep.2013.46.8.075
work_keys_str_mv AT pastoredonato theuniquenessoftheplantmitochondrialpotassiumchannel
AT socciomario theuniquenessoftheplantmitochondrialpotassiumchannel
AT lausmauranicoletta theuniquenessoftheplantmitochondrialpotassiumchannel
AT tronodaniela theuniquenessoftheplantmitochondrialpotassiumchannel
AT pastoredonato uniquenessoftheplantmitochondrialpotassiumchannel
AT socciomario uniquenessoftheplantmitochondrialpotassiumchannel
AT lausmauranicoletta uniquenessoftheplantmitochondrialpotassiumchannel
AT tronodaniela uniquenessoftheplantmitochondrialpotassiumchannel