PQN-59 and GTBP-1 contribute to stress granule formation but are not essential for their assembly in C. elegans embryos

Abbatemarco, Simona, Bondaz, Alexandra, Schwager, Francoise, Wang, Jing, Hammell, Christopher M, Gotta, Monica (October 2021) PQN-59 and GTBP-1 contribute to stress granule formation but are not essential for their assembly in C. elegans embryos. Journal of Cell Science. ISSN 0021-9533

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Abstract

When exposed to stressful conditions, eukaryotic cells respond by inducing the formation of cytoplasmic ribonucleoprotein complexes called stress granules. Here we use C. elegans to study two proteins that are important for stress granule assembly in human cells: PQN-59, the human UBAP2L ortholog, and GTBP-1, the human G3BP1/2 ortholog. Both proteins assemble into stress granules in the embryo and in the germline when C. elegans is exposed to stressful conditions. None of the two proteins is essential for the assembly of stress-induced granules, as shown by the single and combined depletions by RNAi, and neither pqn-59 nor gtbp-1 mutant embryos show higher sensitivity to stress than control embryos. We find that pqn-59 mutants display reduced progeny and a high percentage of embryonic lethality, phenotypes that are not dependent on stress exposure and that are not shared with gtbp-1 mutants. Our data indicate that, in contrast to human cells, PQN-59 and GTBP-1 are not required for stress granule formation but that PQN-59 is important for C. elegans development.

Item Type: Paper
Subjects: bioinformatics
organism description > animal > C elegans
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
organism description > animal
organism description > animal behavior
organism description > animal > developmental stage
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > helicase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
organism description > animal behavior > stress
CSHL Authors:
Communities: CSHL labs > Hammell C. lab
CSHL Cancer Center Program
CSHL Cancer Center Program > Gene Regulation and Inheritance Program
SWORD Depositor: CSHL Elements
Depositing User: CSHL Elements
Date: 18 October 2021
Date Deposited: 27 Oct 2021 13:33
Last Modified: 09 Feb 2024 20:59
PMCID: PMC8645233
URI: https://repository.cshl.edu/id/eprint/40396

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