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Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule

Destabilizing domains are conditionally unstable protein domains that can be fused to a protein of interest resulting in degradation of the fusion protein in the absence of stabilizing ligand. These engineered protein domains enable rapid, reversible and dose-dependent control of protein expression...

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Detalles Bibliográficos
Autores principales: Cho, Ukrae, Zimmerman, Stephanie M., Chen, Ling-chun, Owen, Elliot, Kim, Jesse V., Kim, Stuart K., Wandless, Thomas J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3750007/
https://www.ncbi.nlm.nih.gov/pubmed/23991108
http://dx.doi.org/10.1371/journal.pone.0072393
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author Cho, Ukrae
Zimmerman, Stephanie M.
Chen, Ling-chun
Owen, Elliot
Kim, Jesse V.
Kim, Stuart K.
Wandless, Thomas J.
author_facet Cho, Ukrae
Zimmerman, Stephanie M.
Chen, Ling-chun
Owen, Elliot
Kim, Jesse V.
Kim, Stuart K.
Wandless, Thomas J.
author_sort Cho, Ukrae
collection PubMed
description Destabilizing domains are conditionally unstable protein domains that can be fused to a protein of interest resulting in degradation of the fusion protein in the absence of stabilizing ligand. These engineered protein domains enable rapid, reversible and dose-dependent control of protein expression levels in cultured cells and in vivo. To broaden the scope of this technology, we have engineered new destabilizing domains that perform well at temperatures of 20–25°C. This raises the possibility that our technology could be adapted for use at any temperature. We further show that these new destabilizing domains can be used to regulate protein concentrations in C. elegans. These data reinforce that DD can function in virtually any organism and temperature.
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spelling pubmed-37500072013-08-29 Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule Cho, Ukrae Zimmerman, Stephanie M. Chen, Ling-chun Owen, Elliot Kim, Jesse V. Kim, Stuart K. Wandless, Thomas J. PLoS One Research Article Destabilizing domains are conditionally unstable protein domains that can be fused to a protein of interest resulting in degradation of the fusion protein in the absence of stabilizing ligand. These engineered protein domains enable rapid, reversible and dose-dependent control of protein expression levels in cultured cells and in vivo. To broaden the scope of this technology, we have engineered new destabilizing domains that perform well at temperatures of 20–25°C. This raises the possibility that our technology could be adapted for use at any temperature. We further show that these new destabilizing domains can be used to regulate protein concentrations in C. elegans. These data reinforce that DD can function in virtually any organism and temperature. Public Library of Science 2013-08-22 /pmc/articles/PMC3750007/ /pubmed/23991108 http://dx.doi.org/10.1371/journal.pone.0072393 Text en © 2013 Cho et al http://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 properly credited.
spellingShingle Research Article
Cho, Ukrae
Zimmerman, Stephanie M.
Chen, Ling-chun
Owen, Elliot
Kim, Jesse V.
Kim, Stuart K.
Wandless, Thomas J.
Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule
title Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule
title_full Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule
title_fullStr Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule
title_full_unstemmed Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule
title_short Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule
title_sort rapid and tunable control of protein stability in caenorhabditis elegans using a small molecule
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3750007/
https://www.ncbi.nlm.nih.gov/pubmed/23991108
http://dx.doi.org/10.1371/journal.pone.0072393
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