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Post-translational modifications and stress adaptation: the paradigm of FKBP51

Adaptation to stress is a fundamental requirement to cope with changing environmental conditions that pose a threat to the homeostasis of cells and organisms. Post-translational modifications (PTMs) of proteins represent a possibility to quickly produce proteins with new features demanding relativel...

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Detalles Bibliográficos
Autor principal: Rein, Theo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7200631/
https://www.ncbi.nlm.nih.gov/pubmed/32318709
http://dx.doi.org/10.1042/BST20190332
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author Rein, Theo
author_facet Rein, Theo
author_sort Rein, Theo
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description Adaptation to stress is a fundamental requirement to cope with changing environmental conditions that pose a threat to the homeostasis of cells and organisms. Post-translational modifications (PTMs) of proteins represent a possibility to quickly produce proteins with new features demanding relatively little cellular resources. FK506 binding protein (FKBP) 51 is a pivotal stress protein that is involved in the regulation of several executers of PTMs. This mini-review discusses the role of FKBP51 in the function of proteins responsible for setting the phosphorylation, ubiquitination and lipidation of other proteins. Examples include the kinases Akt1, CDK5 and GSK3β, the phosphatases calcineurin, PP2A and PHLPP, and the ubiquitin E3-ligase SKP2. The impact of FKBP51 on PTMs of signal transduction proteins significantly extends the functional versatility of this protein. As a stress-induced protein, FKBP51 uses re-setting of PTMs to relay the effect of stress on various signaling pathways.
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spelling pubmed-72006312020-05-13 Post-translational modifications and stress adaptation: the paradigm of FKBP51 Rein, Theo Biochem Soc Trans Review Articles Adaptation to stress is a fundamental requirement to cope with changing environmental conditions that pose a threat to the homeostasis of cells and organisms. Post-translational modifications (PTMs) of proteins represent a possibility to quickly produce proteins with new features demanding relatively little cellular resources. FK506 binding protein (FKBP) 51 is a pivotal stress protein that is involved in the regulation of several executers of PTMs. This mini-review discusses the role of FKBP51 in the function of proteins responsible for setting the phosphorylation, ubiquitination and lipidation of other proteins. Examples include the kinases Akt1, CDK5 and GSK3β, the phosphatases calcineurin, PP2A and PHLPP, and the ubiquitin E3-ligase SKP2. The impact of FKBP51 on PTMs of signal transduction proteins significantly extends the functional versatility of this protein. As a stress-induced protein, FKBP51 uses re-setting of PTMs to relay the effect of stress on various signaling pathways. Portland Press Ltd. 2020-04-29 2020-04-22 /pmc/articles/PMC7200631/ /pubmed/32318709 http://dx.doi.org/10.1042/BST20190332 Text en © 2020 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) .
spellingShingle Review Articles
Rein, Theo
Post-translational modifications and stress adaptation: the paradigm of FKBP51
title Post-translational modifications and stress adaptation: the paradigm of FKBP51
title_full Post-translational modifications and stress adaptation: the paradigm of FKBP51
title_fullStr Post-translational modifications and stress adaptation: the paradigm of FKBP51
title_full_unstemmed Post-translational modifications and stress adaptation: the paradigm of FKBP51
title_short Post-translational modifications and stress adaptation: the paradigm of FKBP51
title_sort post-translational modifications and stress adaptation: the paradigm of fkbp51
topic Review Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7200631/
https://www.ncbi.nlm.nih.gov/pubmed/32318709
http://dx.doi.org/10.1042/BST20190332
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