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Disruption of C. elegans embryonic P granules upon dlc-1(RNAi) is not associated with P granule component loss

Dynein light chain (DLC-1) is a light chain component of the dynein motor complex, it functions as an allosteric regulator of multi-subunit protein complexes and promotes P granule integrity in the C. elegans embryo. P granules are RNA-protein complexes located in the C. elegans germline that are im...

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Autores principales: Ellenbecker, Mary, Voronina, Ekaterina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9772925/
https://www.ncbi.nlm.nih.gov/pubmed/36568482
http://dx.doi.org/10.17912/micropub.biology.000700
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author Ellenbecker, Mary
Voronina, Ekaterina
author_facet Ellenbecker, Mary
Voronina, Ekaterina
author_sort Ellenbecker, Mary
collection PubMed
description Dynein light chain (DLC-1) is a light chain component of the dynein motor complex, it functions as an allosteric regulator of multi-subunit protein complexes and promotes P granule integrity in the C. elegans embryo. P granules are RNA-protein complexes located in the C. elegans germline that are important for RNA regulation and fertility. To further study the role of DLC-1 during C. elegans embryogenesis we performed quantitative tandem mass tag mass spectrometry on embryos after dlc-1 knock down. The amount of core P granule components and nucleoporin proteins did not change after dlc-1(RNAi). These results show that DLC-1 does not help regulate P granule protein levels and support the model that DLC-1 facilitates phase separation of P granule components in vivo .
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spelling pubmed-97729252022-12-23 Disruption of C. elegans embryonic P granules upon dlc-1(RNAi) is not associated with P granule component loss Ellenbecker, Mary Voronina, Ekaterina MicroPubl Biol New Finding Dynein light chain (DLC-1) is a light chain component of the dynein motor complex, it functions as an allosteric regulator of multi-subunit protein complexes and promotes P granule integrity in the C. elegans embryo. P granules are RNA-protein complexes located in the C. elegans germline that are important for RNA regulation and fertility. To further study the role of DLC-1 during C. elegans embryogenesis we performed quantitative tandem mass tag mass spectrometry on embryos after dlc-1 knock down. The amount of core P granule components and nucleoporin proteins did not change after dlc-1(RNAi). These results show that DLC-1 does not help regulate P granule protein levels and support the model that DLC-1 facilitates phase separation of P granule components in vivo . Caltech Library 2022-12-06 /pmc/articles/PMC9772925/ /pubmed/36568482 http://dx.doi.org/10.17912/micropub.biology.000700 Text en Copyright: © 2022 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
Ellenbecker, Mary
Voronina, Ekaterina
Disruption of C. elegans embryonic P granules upon dlc-1(RNAi) is not associated with P granule component loss
title Disruption of C. elegans embryonic P granules upon dlc-1(RNAi) is not associated with P granule component loss
title_full Disruption of C. elegans embryonic P granules upon dlc-1(RNAi) is not associated with P granule component loss
title_fullStr Disruption of C. elegans embryonic P granules upon dlc-1(RNAi) is not associated with P granule component loss
title_full_unstemmed Disruption of C. elegans embryonic P granules upon dlc-1(RNAi) is not associated with P granule component loss
title_short Disruption of C. elegans embryonic P granules upon dlc-1(RNAi) is not associated with P granule component loss
title_sort disruption of c. elegans embryonic p granules upon dlc-1(rnai) is not associated with p granule component loss
topic New Finding
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9772925/
https://www.ncbi.nlm.nih.gov/pubmed/36568482
http://dx.doi.org/10.17912/micropub.biology.000700
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