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Membrane nanodomains and transport functions in plant
Far from a homogeneous environment, biological membranes are highly structured with lipids and proteins segregating in domains of different sizes and dwell times. In addition, membranes are highly dynamics especially in response to environmental stimuli. Understanding the impact of the nanoscale org...
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/PMC8644385/ https://www.ncbi.nlm.nih.gov/pubmed/35235669 http://dx.doi.org/10.1093/plphys/kiab312 |
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author | Martinière, Alexandre Zelazny, Enric |
author_facet | Martinière, Alexandre Zelazny, Enric |
author_sort | Martinière, Alexandre |
collection | PubMed |
description | Far from a homogeneous environment, biological membranes are highly structured with lipids and proteins segregating in domains of different sizes and dwell times. In addition, membranes are highly dynamics especially in response to environmental stimuli. Understanding the impact of the nanoscale organization of membranes on cellular functions is an outstanding question. Plant channels and transporters are tightly regulated to ensure proper cell nutrition and signaling. Increasing evidence indicates that channel and transporter nano-organization within membranes plays an important role in these regulation mechanisms. Here, we review recent advances in the field of ion, water, but also hormone transport in plants, focusing on protein organization within plasma membrane nanodomains and its cellular and physiological impacts. |
format | Online Article Text |
id | pubmed-8644385 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-86443852021-12-06 Membrane nanodomains and transport functions in plant Martinière, Alexandre Zelazny, Enric Plant Physiol Focus Issue on Transport and Signaling Far from a homogeneous environment, biological membranes are highly structured with lipids and proteins segregating in domains of different sizes and dwell times. In addition, membranes are highly dynamics especially in response to environmental stimuli. Understanding the impact of the nanoscale organization of membranes on cellular functions is an outstanding question. Plant channels and transporters are tightly regulated to ensure proper cell nutrition and signaling. Increasing evidence indicates that channel and transporter nano-organization within membranes plays an important role in these regulation mechanisms. Here, we review recent advances in the field of ion, water, but also hormone transport in plants, focusing on protein organization within plasma membrane nanodomains and its cellular and physiological impacts. Oxford University Press 2021-07-13 /pmc/articles/PMC8644385/ /pubmed/35235669 http://dx.doi.org/10.1093/plphys/kiab312 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 Martinière, Alexandre Zelazny, Enric Membrane nanodomains and transport functions in plant |
title | Membrane nanodomains and transport functions in plant |
title_full | Membrane nanodomains and transport functions in plant |
title_fullStr | Membrane nanodomains and transport functions in plant |
title_full_unstemmed | Membrane nanodomains and transport functions in plant |
title_short | Membrane nanodomains and transport functions in plant |
title_sort | membrane nanodomains and transport functions in plant |
topic | Focus Issue on Transport and Signaling |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8644385/ https://www.ncbi.nlm.nih.gov/pubmed/35235669 http://dx.doi.org/10.1093/plphys/kiab312 |
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