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Making Contact: VAP Targeting by Intracellular Pathogens

In naïve cells, the endoplasmic reticulum (ER) and the ER-resident Vesicle-associated membrane protein-Associated Proteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijacking...

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Detalles Bibliográficos
Autores principales: Murray, Rebecca, Derré, Isabelle
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE Publications 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6083021/
https://www.ncbi.nlm.nih.gov/pubmed/30101212
http://dx.doi.org/10.1177/2515256418775512
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author Murray, Rebecca
Derré, Isabelle
author_facet Murray, Rebecca
Derré, Isabelle
author_sort Murray, Rebecca
collection PubMed
description In naïve cells, the endoplasmic reticulum (ER) and the ER-resident Vesicle-associated membrane protein-Associated Proteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijacking of VAP by intracellular pathogens is a novel mechanism of host–pathogen interaction. Here, we summarize our recent findings showing that the Chlamydia inclusion membrane protein IncV tethers the ER to the inclusion membrane by binding to VAP via the molecular mimicry of two eukaryotic FFAT motifs. We extend the discussion to other microorganisms that have evolved similar mechanisms.
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spelling pubmed-60830212018-08-09 Making Contact: VAP Targeting by Intracellular Pathogens Murray, Rebecca Derré, Isabelle Contact (Thousand Oaks) News and Views In naïve cells, the endoplasmic reticulum (ER) and the ER-resident Vesicle-associated membrane protein-Associated Proteins (VAP) are common components of sites of membrane contacts that mediate the nonvesicular transfer of lipids between organelles. There is increasing recognition that the hijacking of VAP by intracellular pathogens is a novel mechanism of host–pathogen interaction. Here, we summarize our recent findings showing that the Chlamydia inclusion membrane protein IncV tethers the ER to the inclusion membrane by binding to VAP via the molecular mimicry of two eukaryotic FFAT motifs. We extend the discussion to other microorganisms that have evolved similar mechanisms. SAGE Publications 2018-05-17 /pmc/articles/PMC6083021/ /pubmed/30101212 http://dx.doi.org/10.1177/2515256418775512 Text en © The Author(s) 2018 https://creativecommons.org/licenses/by-nc/4.0/Creative Commons Non Commercial CC BY-NC: This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (https://creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage).
spellingShingle News and Views
Murray, Rebecca
Derré, Isabelle
Making Contact: VAP Targeting by Intracellular Pathogens
title Making Contact: VAP Targeting by Intracellular Pathogens
title_full Making Contact: VAP Targeting by Intracellular Pathogens
title_fullStr Making Contact: VAP Targeting by Intracellular Pathogens
title_full_unstemmed Making Contact: VAP Targeting by Intracellular Pathogens
title_short Making Contact: VAP Targeting by Intracellular Pathogens
title_sort making contact: vap targeting by intracellular pathogens
topic News and Views
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6083021/
https://www.ncbi.nlm.nih.gov/pubmed/30101212
http://dx.doi.org/10.1177/2515256418775512
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