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Unique and conserved features of the plant ER-shaping GTPase RHD3

The architectural integrity of the endoplasmic reticulum (ER) network depends on the function of membrane-associated dynamin-like GTPases that include metazoan atlastins, plant RHD3 and yeast Sey1p. The evidence that these proteins are sufficient to drive membrane fusion of reconstituted proteolipos...

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Autores principales: Stefano, Giovanni, Brandizzi, Federica
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4013103/
https://www.ncbi.nlm.nih.gov/pubmed/24812592
http://dx.doi.org/10.4161/cl.28217
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author Stefano, Giovanni
Brandizzi, Federica
author_facet Stefano, Giovanni
Brandizzi, Federica
author_sort Stefano, Giovanni
collection PubMed
description The architectural integrity of the endoplasmic reticulum (ER) network depends on the function of membrane-associated dynamin-like GTPases that include metazoan atlastins, plant RHD3 and yeast Sey1p. The evidence that these proteins are sufficient to drive membrane fusion of reconstituted proteoliposomes, and that loss-of-function mutations lead to conspicuous ER shape defects indicates that atlastins, RHD3 and Sey1p promote ER membrane fusion. However, complementation experiments in reciprocal loss-of-function backgrounds have also suggested that RHD3 and Sey1p may be not functionally equivalent, supporting that ER fusion mechanisms may be not entirely conserved in eukaryotes. In this Letter, we provide a brief overview of the field as well as evidence that may explain the functional differences of the plant and yeast ER-shaping dynamin-like GTPases.
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spelling pubmed-40131032014-05-09 Unique and conserved features of the plant ER-shaping GTPase RHD3 Stefano, Giovanni Brandizzi, Federica Cell Logist Letter from the Editor The architectural integrity of the endoplasmic reticulum (ER) network depends on the function of membrane-associated dynamin-like GTPases that include metazoan atlastins, plant RHD3 and yeast Sey1p. The evidence that these proteins are sufficient to drive membrane fusion of reconstituted proteoliposomes, and that loss-of-function mutations lead to conspicuous ER shape defects indicates that atlastins, RHD3 and Sey1p promote ER membrane fusion. However, complementation experiments in reciprocal loss-of-function backgrounds have also suggested that RHD3 and Sey1p may be not functionally equivalent, supporting that ER fusion mechanisms may be not entirely conserved in eukaryotes. In this Letter, we provide a brief overview of the field as well as evidence that may explain the functional differences of the plant and yeast ER-shaping dynamin-like GTPases. Landes Bioscience 2014-02-28 /pmc/articles/PMC4013103/ /pubmed/24812592 http://dx.doi.org/10.4161/cl.28217 Text en Copyright © 2014 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Letter from the Editor
Stefano, Giovanni
Brandizzi, Federica
Unique and conserved features of the plant ER-shaping GTPase RHD3
title Unique and conserved features of the plant ER-shaping GTPase RHD3
title_full Unique and conserved features of the plant ER-shaping GTPase RHD3
title_fullStr Unique and conserved features of the plant ER-shaping GTPase RHD3
title_full_unstemmed Unique and conserved features of the plant ER-shaping GTPase RHD3
title_short Unique and conserved features of the plant ER-shaping GTPase RHD3
title_sort unique and conserved features of the plant er-shaping gtpase rhd3
topic Letter from the Editor
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4013103/
https://www.ncbi.nlm.nih.gov/pubmed/24812592
http://dx.doi.org/10.4161/cl.28217
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