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Homotypic fusion of endoplasmic reticulum membranes in plant cells

The endoplasmic reticulum (ER) is a membrane-bounded organelle whose membrane comprises a network of tubules and sheets. The formation of these characteristic shapes and maintenance of their continuity through homotypic membrane fusion appears to be critical for the proper functioning of the ER. The...

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Autores principales: Zhang, Miao, Hu, Junjie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3866526/
https://www.ncbi.nlm.nih.gov/pubmed/24385977
http://dx.doi.org/10.3389/fpls.2013.00514
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author Zhang, Miao
Hu, Junjie
author_facet Zhang, Miao
Hu, Junjie
author_sort Zhang, Miao
collection PubMed
description The endoplasmic reticulum (ER) is a membrane-bounded organelle whose membrane comprises a network of tubules and sheets. The formation of these characteristic shapes and maintenance of their continuity through homotypic membrane fusion appears to be critical for the proper functioning of the ER. The atlastins (ATLs), a family of ER-localized dynamin-like GTPases, have been identified as fusogens of the ER membranes in metazoans. Mutations of the ATL proteins in mammalian cells cause morphological defects in the ER, and purified Drosophila ATL mediates membrane fusion in vitro. Plant cells do not possess ATL, but a family of similar GTPases, named root hair defective 3 (RHD3), are likely the functional orthologs of ATLs. In this review, we summarize recent advances in our understanding of how RHD3 proteins play a role in homotypic ER fusion. We also discuss the possible physiological significance of forming a tubular ER network in plant cells.
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spelling pubmed-38665262014-01-02 Homotypic fusion of endoplasmic reticulum membranes in plant cells Zhang, Miao Hu, Junjie Front Plant Sci Plant Science The endoplasmic reticulum (ER) is a membrane-bounded organelle whose membrane comprises a network of tubules and sheets. The formation of these characteristic shapes and maintenance of their continuity through homotypic membrane fusion appears to be critical for the proper functioning of the ER. The atlastins (ATLs), a family of ER-localized dynamin-like GTPases, have been identified as fusogens of the ER membranes in metazoans. Mutations of the ATL proteins in mammalian cells cause morphological defects in the ER, and purified Drosophila ATL mediates membrane fusion in vitro. Plant cells do not possess ATL, but a family of similar GTPases, named root hair defective 3 (RHD3), are likely the functional orthologs of ATLs. In this review, we summarize recent advances in our understanding of how RHD3 proteins play a role in homotypic ER fusion. We also discuss the possible physiological significance of forming a tubular ER network in plant cells. Frontiers Media S.A. 2013-12-18 /pmc/articles/PMC3866526/ /pubmed/24385977 http://dx.doi.org/10.3389/fpls.2013.00514 Text en Copyright © 2013 Zhang and Hu. http://creativecommons.org/licenses/by/3.0/ 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
Zhang, Miao
Hu, Junjie
Homotypic fusion of endoplasmic reticulum membranes in plant cells
title Homotypic fusion of endoplasmic reticulum membranes in plant cells
title_full Homotypic fusion of endoplasmic reticulum membranes in plant cells
title_fullStr Homotypic fusion of endoplasmic reticulum membranes in plant cells
title_full_unstemmed Homotypic fusion of endoplasmic reticulum membranes in plant cells
title_short Homotypic fusion of endoplasmic reticulum membranes in plant cells
title_sort homotypic fusion of endoplasmic reticulum membranes in plant cells
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3866526/
https://www.ncbi.nlm.nih.gov/pubmed/24385977
http://dx.doi.org/10.3389/fpls.2013.00514
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