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Identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies

Nesprins are highly conserved spectrin repeat–containing scaffold proteins predominantly known to function at the nuclear envelope (NE). However, nesprin isoforms are emerging with localizations and scaffolding functions at sites away from the NE, suggesting their functions are more diverse than ori...

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Detalles Bibliográficos
Autores principales: Rajgor, Dipen, Hanley, Jonathan G., Shanahan, Catherine M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5170611/
https://www.ncbi.nlm.nih.gov/pubmed/27733621
http://dx.doi.org/10.1091/mbc.E16-06-0346
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author Rajgor, Dipen
Hanley, Jonathan G.
Shanahan, Catherine M.
author_facet Rajgor, Dipen
Hanley, Jonathan G.
Shanahan, Catherine M.
author_sort Rajgor, Dipen
collection PubMed
description Nesprins are highly conserved spectrin repeat–containing scaffold proteins predominantly known to function at the nuclear envelope (NE). However, nesprin isoforms are emerging with localizations and scaffolding functions at sites away from the NE, suggesting their functions are more diverse than originally thought. In this study, we combined nesprin-1 coimmunoprecipitations with mass spectrometry to identify novel nesprin-1 binding partners for isoforms that localize to subcellular compartments beyond the NE. We show that one of these interactors, matrin-3 (matr3), localizes to mRNA processing bodies (PBs), where we have previously shown a nesprin-1 isoform to localize. Furthermore, we show that Matr3 is part of PB mRNP complexes, is a regulator of miRNA-mediated gene silencing, and possibly shuttles to stress granules in stressed cells. More importantly, we identify a new C-terminally truncated Matr3 isoform that is likely to be involved in these functions and PB localization. This study highlights several novel nesprin-1 binding partners and a new function and localization for Matr3 in cytoplasmic RNA granules.
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spelling pubmed-51706112017-02-16 Identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies Rajgor, Dipen Hanley, Jonathan G. Shanahan, Catherine M. Mol Biol Cell Articles Nesprins are highly conserved spectrin repeat–containing scaffold proteins predominantly known to function at the nuclear envelope (NE). However, nesprin isoforms are emerging with localizations and scaffolding functions at sites away from the NE, suggesting their functions are more diverse than originally thought. In this study, we combined nesprin-1 coimmunoprecipitations with mass spectrometry to identify novel nesprin-1 binding partners for isoforms that localize to subcellular compartments beyond the NE. We show that one of these interactors, matrin-3 (matr3), localizes to mRNA processing bodies (PBs), where we have previously shown a nesprin-1 isoform to localize. Furthermore, we show that Matr3 is part of PB mRNP complexes, is a regulator of miRNA-mediated gene silencing, and possibly shuttles to stress granules in stressed cells. More importantly, we identify a new C-terminally truncated Matr3 isoform that is likely to be involved in these functions and PB localization. This study highlights several novel nesprin-1 binding partners and a new function and localization for Matr3 in cytoplasmic RNA granules. The American Society for Cell Biology 2016-12-01 /pmc/articles/PMC5170611/ /pubmed/27733621 http://dx.doi.org/10.1091/mbc.E16-06-0346 Text en © 2016 Rajgor et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Rajgor, Dipen
Hanley, Jonathan G.
Shanahan, Catherine M.
Identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies
title Identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies
title_full Identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies
title_fullStr Identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies
title_full_unstemmed Identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies
title_short Identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies
title_sort identification of novel nesprin-1 binding partners and cytoplasmic matrin-3 in processing bodies
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5170611/
https://www.ncbi.nlm.nih.gov/pubmed/27733621
http://dx.doi.org/10.1091/mbc.E16-06-0346
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