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Interactions between plant endomembrane systems and the actin cytoskeleton

Membrane trafficking, organelle movement, and morphogenesis in plant cells are mainly controlled by the actin cytoskeleton. Not all proteins that regulate the cytoskeleton and membrane dynamics in animal systems have functional homologs in plants, especially for those proteins that form the bridge b...

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Detalles Bibliográficos
Autores principales: Wang, Pengwei, Hussey, Patrick J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4460326/
https://www.ncbi.nlm.nih.gov/pubmed/26106403
http://dx.doi.org/10.3389/fpls.2015.00422
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author Wang, Pengwei
Hussey, Patrick J.
author_facet Wang, Pengwei
Hussey, Patrick J.
author_sort Wang, Pengwei
collection PubMed
description Membrane trafficking, organelle movement, and morphogenesis in plant cells are mainly controlled by the actin cytoskeleton. Not all proteins that regulate the cytoskeleton and membrane dynamics in animal systems have functional homologs in plants, especially for those proteins that form the bridge between the cytoskeleton and membrane; the membrane-actin adaptors. Their nature and function is only just beginning to be elucidated and this field has been greatly enhanced by the recent identification of the NETWORKED (NET) proteins, which act as membrane-actin adaptors. In this review, we will summarize the role of the actin cytoskeleton and its regulatory proteins in their interaction with endomembrane compartments and where they potentially act as platforms for cell signaling and the coordination of other subcellular events.
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spelling pubmed-44603262015-06-23 Interactions between plant endomembrane systems and the actin cytoskeleton Wang, Pengwei Hussey, Patrick J. Front Plant Sci Plant Science Membrane trafficking, organelle movement, and morphogenesis in plant cells are mainly controlled by the actin cytoskeleton. Not all proteins that regulate the cytoskeleton and membrane dynamics in animal systems have functional homologs in plants, especially for those proteins that form the bridge between the cytoskeleton and membrane; the membrane-actin adaptors. Their nature and function is only just beginning to be elucidated and this field has been greatly enhanced by the recent identification of the NETWORKED (NET) proteins, which act as membrane-actin adaptors. In this review, we will summarize the role of the actin cytoskeleton and its regulatory proteins in their interaction with endomembrane compartments and where they potentially act as platforms for cell signaling and the coordination of other subcellular events. Frontiers Media S.A. 2015-06-09 /pmc/articles/PMC4460326/ /pubmed/26106403 http://dx.doi.org/10.3389/fpls.2015.00422 Text en Copyright © 2015 Wang and Hussey. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Wang, Pengwei
Hussey, Patrick J.
Interactions between plant endomembrane systems and the actin cytoskeleton
title Interactions between plant endomembrane systems and the actin cytoskeleton
title_full Interactions between plant endomembrane systems and the actin cytoskeleton
title_fullStr Interactions between plant endomembrane systems and the actin cytoskeleton
title_full_unstemmed Interactions between plant endomembrane systems and the actin cytoskeleton
title_short Interactions between plant endomembrane systems and the actin cytoskeleton
title_sort interactions between plant endomembrane systems and the actin cytoskeleton
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4460326/
https://www.ncbi.nlm.nih.gov/pubmed/26106403
http://dx.doi.org/10.3389/fpls.2015.00422
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