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JKK-1(3E), a JKK-1 mutant with predicted phosphomimetic amino acid substitutions

Phosphomimetic substitutions have been instrumental in understanding the role of phosphorylation in protein function. Here we describe the design and construction of a predicted phosphomimetic allele of the JUN kinase kinase gene jkk-1 in C. elegans. To generate the phosphomimetic kinase mutant JKK-...

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Autores principales: Busack, Inka, Bringmann, Henrik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10082396/
https://www.ncbi.nlm.nih.gov/pubmed/37038480
http://dx.doi.org/10.17912/micropub.biology.000785
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author Busack, Inka
Bringmann, Henrik
author_facet Busack, Inka
Bringmann, Henrik
author_sort Busack, Inka
collection PubMed
description Phosphomimetic substitutions have been instrumental in understanding the role of phosphorylation in protein function. Here we describe the design and construction of a predicted phosphomimetic allele of the JUN kinase kinase gene jkk-1 in C. elegans. To generate the phosphomimetic kinase mutant JKK-1(3E), we edited jkk-1 to introduce three amino acid substitutions, S274E, S278E and S280E. The resulting strain is homozygous viable and extends the survival of L1-arrested larvae. This survival-extending phenotype suggests that the phosphomimetic mutations might promote activation of JKK-1 during the arrest. This jkk-1 potential gain-of-function allele might be useful for studying the regulation and functions of JKK-1.
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spelling pubmed-100823962023-04-09 JKK-1(3E), a JKK-1 mutant with predicted phosphomimetic amino acid substitutions Busack, Inka Bringmann, Henrik MicroPubl Biol Materials and Reagents Phosphomimetic substitutions have been instrumental in understanding the role of phosphorylation in protein function. Here we describe the design and construction of a predicted phosphomimetic allele of the JUN kinase kinase gene jkk-1 in C. elegans. To generate the phosphomimetic kinase mutant JKK-1(3E), we edited jkk-1 to introduce three amino acid substitutions, S274E, S278E and S280E. The resulting strain is homozygous viable and extends the survival of L1-arrested larvae. This survival-extending phenotype suggests that the phosphomimetic mutations might promote activation of JKK-1 during the arrest. This jkk-1 potential gain-of-function allele might be useful for studying the regulation and functions of JKK-1. Caltech Library 2023-03-24 /pmc/articles/PMC10082396/ /pubmed/37038480 http://dx.doi.org/10.17912/micropub.biology.000785 Text en Copyright: © 2023 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 Materials and Reagents
Busack, Inka
Bringmann, Henrik
JKK-1(3E), a JKK-1 mutant with predicted phosphomimetic amino acid substitutions
title JKK-1(3E), a JKK-1 mutant with predicted phosphomimetic amino acid substitutions
title_full JKK-1(3E), a JKK-1 mutant with predicted phosphomimetic amino acid substitutions
title_fullStr JKK-1(3E), a JKK-1 mutant with predicted phosphomimetic amino acid substitutions
title_full_unstemmed JKK-1(3E), a JKK-1 mutant with predicted phosphomimetic amino acid substitutions
title_short JKK-1(3E), a JKK-1 mutant with predicted phosphomimetic amino acid substitutions
title_sort jkk-1(3e), a jkk-1 mutant with predicted phosphomimetic amino acid substitutions
topic Materials and Reagents
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10082396/
https://www.ncbi.nlm.nih.gov/pubmed/37038480
http://dx.doi.org/10.17912/micropub.biology.000785
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