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Calcineurin

The serine/threonine phosphatase calcineurin acts as a crucial connection between calcium signaling the phosphorylation states of numerous important substrates. These substrates include, but are not limited to, transcription factors, receptors and channels, proteins associated with mitochondria, and...

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Autor principal: Creamer, Trevor P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7456046/
https://www.ncbi.nlm.nih.gov/pubmed/32859215
http://dx.doi.org/10.1186/s12964-020-00636-4
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author Creamer, Trevor P.
author_facet Creamer, Trevor P.
author_sort Creamer, Trevor P.
collection PubMed
description The serine/threonine phosphatase calcineurin acts as a crucial connection between calcium signaling the phosphorylation states of numerous important substrates. These substrates include, but are not limited to, transcription factors, receptors and channels, proteins associated with mitochondria, and proteins associated with microtubules. Calcineurin is activated by increases in intracellular calcium concentrations, a process that requires the calcium sensing protein calmodulin binding to an intrinsically disordered regulatory domain in the phosphatase. Despite having been studied for around four decades, the activation of calcineurin is not fully understood. This review largely focuses on what is known about the activation process and highlights aspects that are currently not understood.
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spelling pubmed-74560462020-08-31 Calcineurin Creamer, Trevor P. Cell Commun Signal Review The serine/threonine phosphatase calcineurin acts as a crucial connection between calcium signaling the phosphorylation states of numerous important substrates. These substrates include, but are not limited to, transcription factors, receptors and channels, proteins associated with mitochondria, and proteins associated with microtubules. Calcineurin is activated by increases in intracellular calcium concentrations, a process that requires the calcium sensing protein calmodulin binding to an intrinsically disordered regulatory domain in the phosphatase. Despite having been studied for around four decades, the activation of calcineurin is not fully understood. This review largely focuses on what is known about the activation process and highlights aspects that are currently not understood. BioMed Central 2020-08-28 /pmc/articles/PMC7456046/ /pubmed/32859215 http://dx.doi.org/10.1186/s12964-020-00636-4 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Review
Creamer, Trevor P.
Calcineurin
title Calcineurin
title_full Calcineurin
title_fullStr Calcineurin
title_full_unstemmed Calcineurin
title_short Calcineurin
title_sort calcineurin
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7456046/
https://www.ncbi.nlm.nih.gov/pubmed/32859215
http://dx.doi.org/10.1186/s12964-020-00636-4
work_keys_str_mv AT creamertrevorp calcineurin