Cargando…
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...
Autores principales: | , , |
---|---|
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 |
_version_ | 1782483794059591680 |
---|---|
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. |
format | Online Article Text |
id | pubmed-5170611 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT rajgordipen identificationofnovelnesprin1bindingpartnersandcytoplasmicmatrin3inprocessingbodies AT hanleyjonathang identificationofnovelnesprin1bindingpartnersandcytoplasmicmatrin3inprocessingbodies AT shanahancatherinem identificationofnovelnesprin1bindingpartnersandcytoplasmicmatrin3inprocessingbodies |