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Phosphorylation of G3BP1-S149 does not influence stress granule assembly
Tourrière et al. (2003. J. Cell Biol. https://doi.org/10.1083/jcb.200212128) reported that G3BP1-S149 dephosphorylation promotes stress granule formation. We show that constructs used to establish this conclusion contain additional mutations causing these phenotypes, and that S149 phosphorylation st...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6605800/ https://www.ncbi.nlm.nih.gov/pubmed/31171631 http://dx.doi.org/10.1083/jcb.201801214 |
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author | Panas, Marc D. Kedersha, Nancy Schulte, Tim Branca, Rui M. Ivanov, Pavel Anderson, Paul |
author_facet | Panas, Marc D. Kedersha, Nancy Schulte, Tim Branca, Rui M. Ivanov, Pavel Anderson, Paul |
author_sort | Panas, Marc D. |
collection | PubMed |
description | Tourrière et al. (2003. J. Cell Biol. https://doi.org/10.1083/jcb.200212128) reported that G3BP1-S149 dephosphorylation promotes stress granule formation. We show that constructs used to establish this conclusion contain additional mutations causing these phenotypes, and that S149 phosphorylation status does not change upon stress. |
format | Online Article Text |
id | pubmed-6605800 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-66058002020-01-01 Phosphorylation of G3BP1-S149 does not influence stress granule assembly Panas, Marc D. Kedersha, Nancy Schulte, Tim Branca, Rui M. Ivanov, Pavel Anderson, Paul J Cell Biol Letters Tourrière et al. (2003. J. Cell Biol. https://doi.org/10.1083/jcb.200212128) reported that G3BP1-S149 dephosphorylation promotes stress granule formation. We show that constructs used to establish this conclusion contain additional mutations causing these phenotypes, and that S149 phosphorylation status does not change upon stress. Rockefeller University Press 2019-07-01 2019-06-06 /pmc/articles/PMC6605800/ /pubmed/31171631 http://dx.doi.org/10.1083/jcb.201801214 Text en © 2019 Panas et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Letters Panas, Marc D. Kedersha, Nancy Schulte, Tim Branca, Rui M. Ivanov, Pavel Anderson, Paul Phosphorylation of G3BP1-S149 does not influence stress granule assembly |
title | Phosphorylation of G3BP1-S149 does not influence stress granule assembly |
title_full | Phosphorylation of G3BP1-S149 does not influence stress granule assembly |
title_fullStr | Phosphorylation of G3BP1-S149 does not influence stress granule assembly |
title_full_unstemmed | Phosphorylation of G3BP1-S149 does not influence stress granule assembly |
title_short | Phosphorylation of G3BP1-S149 does not influence stress granule assembly |
title_sort | phosphorylation of g3bp1-s149 does not influence stress granule assembly |
topic | Letters |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6605800/ https://www.ncbi.nlm.nih.gov/pubmed/31171631 http://dx.doi.org/10.1083/jcb.201801214 |
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