Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective

The Arabidopsis AAA ATPase SKD1 is essential for ESCRT-dependent endosomal sorting by mediating the disassembly of the ESCRTIII complex in an ATP-dependent manner. In this study, we show that SKD1 localizes to messenger ribonucleoprotein complexes upon heat stress. Consistent with this, the interact...

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Autores principales: Wolff, Heike, Jakoby, Marc, Stephan, Lisa, Koebke, Eva, Hülskamp, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Plant Science
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8264791/
https://www.ncbi.nlm.nih.gov/pubmed/34249042
http://dx.doi.org/10.3389/fpls.2021.670499
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author Wolff, Heike
Jakoby, Marc
Stephan, Lisa
Koebke, Eva
Hülskamp, Martin
author_facet Wolff, Heike
Jakoby, Marc
Stephan, Lisa
Koebke, Eva
Hülskamp, Martin
author_sort Wolff, Heike
collection PubMed
description The Arabidopsis AAA ATPase SKD1 is essential for ESCRT-dependent endosomal sorting by mediating the disassembly of the ESCRTIII complex in an ATP-dependent manner. In this study, we show that SKD1 localizes to messenger ribonucleoprotein complexes upon heat stress. Consistent with this, the interactome of SKD1 revealed differential interactions under normal and stress conditions and included membrane transport proteins as well as proteins associated with RNA metabolism. Localization studies with selected interactome proteins revealed that not only RNA associated proteins but also several ESCRTIII and membrane trafficking proteins were recruited to messenger ribonucleoprotein granules after heat stress.
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spelling pubmed-82647912021-07-09 Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective Wolff, Heike Jakoby, Marc Stephan, Lisa Koebke, Eva Hülskamp, Martin Front Plant Sci Plant Science The Arabidopsis AAA ATPase SKD1 is essential for ESCRT-dependent endosomal sorting by mediating the disassembly of the ESCRTIII complex in an ATP-dependent manner. In this study, we show that SKD1 localizes to messenger ribonucleoprotein complexes upon heat stress. Consistent with this, the interactome of SKD1 revealed differential interactions under normal and stress conditions and included membrane transport proteins as well as proteins associated with RNA metabolism. Localization studies with selected interactome proteins revealed that not only RNA associated proteins but also several ESCRTIII and membrane trafficking proteins were recruited to messenger ribonucleoprotein granules after heat stress. Frontiers Media S.A. 2021-06-24 /pmc/articles/PMC8264791/ /pubmed/34249042 http://dx.doi.org/10.3389/fpls.2021.670499 Text en Copyright © 2021 Wolff, Jakoby, Stephan, Koebke and Hülskamp. https://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) and the copyright owner(s) 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
Wolff, Heike
Jakoby, Marc
Stephan, Lisa
Koebke, Eva
Hülskamp, Martin
Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective
title Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective
title_full Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective
title_fullStr Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective
title_full_unstemmed Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective
title_short Heat Stress-Dependent Association of Membrane Trafficking Proteins With mRNPs Is Selective
title_sort heat stress-dependent association of membrane trafficking proteins with mrnps is selective
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8264791/
https://www.ncbi.nlm.nih.gov/pubmed/34249042
http://dx.doi.org/10.3389/fpls.2021.670499
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