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Phase separation dynamics of the C. elegans PGL-1 P granule protein in oocytes are sensitive to heat stress
Phase separation has emerged as a widespread process of organizing the cytoplasm of diverse eukaryotic cells. In C. elegans oocytes, several RNA binding proteins are condensed into germ granules called P granules. Prior studies studying the phase transitions of RNA binding proteins in response to in...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Caltech Library
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8463931/ https://www.ncbi.nlm.nih.gov/pubmed/34585104 http://dx.doi.org/10.17912/micropub.biology.000476 |
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author | Watkins, Brooklynne Schisa, Jennifer A. |
author_facet | Watkins, Brooklynne Schisa, Jennifer A. |
author_sort | Watkins, Brooklynne |
collection | PubMed |
description | Phase separation has emerged as a widespread process of organizing the cytoplasm of diverse eukaryotic cells. In C. elegans oocytes, several RNA binding proteins are condensed into germ granules called P granules. Prior studies studying the phase transitions of RNA binding proteins in response to increased temperature have suggested that PGL-1 decondenses in oocytes in response to heat. Here, we confirm this finding with a new reporter strain and demonstrate the sensitivity of PGL-1 to temperature changes. |
format | Online Article Text |
id | pubmed-8463931 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Caltech Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-84639312021-09-27 Phase separation dynamics of the C. elegans PGL-1 P granule protein in oocytes are sensitive to heat stress Watkins, Brooklynne Schisa, Jennifer A. MicroPubl Biol New Finding Phase separation has emerged as a widespread process of organizing the cytoplasm of diverse eukaryotic cells. In C. elegans oocytes, several RNA binding proteins are condensed into germ granules called P granules. Prior studies studying the phase transitions of RNA binding proteins in response to increased temperature have suggested that PGL-1 decondenses in oocytes in response to heat. Here, we confirm this finding with a new reporter strain and demonstrate the sensitivity of PGL-1 to temperature changes. Caltech Library 2021-09-24 /pmc/articles/PMC8463931/ /pubmed/34585104 http://dx.doi.org/10.17912/micropub.biology.000476 Text en Copyright: © 2021 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | New Finding Watkins, Brooklynne Schisa, Jennifer A. Phase separation dynamics of the C. elegans PGL-1 P granule protein in oocytes are sensitive to heat stress |
title | Phase separation dynamics of the C. elegans PGL-1 P granule protein in oocytes are sensitive to heat stress |
title_full | Phase separation dynamics of the C. elegans PGL-1 P granule protein in oocytes are sensitive to heat stress |
title_fullStr | Phase separation dynamics of the C. elegans PGL-1 P granule protein in oocytes are sensitive to heat stress |
title_full_unstemmed | Phase separation dynamics of the C. elegans PGL-1 P granule protein in oocytes are sensitive to heat stress |
title_short | Phase separation dynamics of the C. elegans PGL-1 P granule protein in oocytes are sensitive to heat stress |
title_sort | phase separation dynamics of the c. elegans pgl-1 p granule protein in oocytes are sensitive to heat stress |
topic | New Finding |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8463931/ https://www.ncbi.nlm.nih.gov/pubmed/34585104 http://dx.doi.org/10.17912/micropub.biology.000476 |
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