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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...

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Detalles Bibliográficos
Autores principales: Watkins, Brooklynne, Schisa, Jennifer A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2021
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.
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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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