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Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs
Cellular function is based on protein–protein interactions. A large proportion of these interactions involves the binding of short linear motifs (SLiMs) by folded globular domains. These interactions are regulated by post-translational modifications, such as phosphorylation, that create and break mo...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8786283/ https://www.ncbi.nlm.nih.gov/pubmed/34989786 http://dx.doi.org/10.1042/BCJ20200714 |
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author | Kliche, Johanna Ivarsson, Ylva |
author_facet | Kliche, Johanna Ivarsson, Ylva |
author_sort | Kliche, Johanna |
collection | PubMed |
description | Cellular function is based on protein–protein interactions. A large proportion of these interactions involves the binding of short linear motifs (SLiMs) by folded globular domains. These interactions are regulated by post-translational modifications, such as phosphorylation, that create and break motif binding sites or tune the affinity of the interactions. In addition, motif-based interactions are involved in targeting serine/threonine kinases and phosphatases to their substrate and contribute to the specificity of the enzymatic actions regulating which sites are phosphorylated. Here, we review how SLiM-based interactions assist in determining the specificity of serine/threonine kinases and phosphatases, and how phosphorylation, in turn, affects motif-based interactions. We provide examples of SLiM-based interactions that are turned on/off, or are tuned by serine/threonine phosphorylation and exemplify how this affects SLiM-based protein complex formation. |
format | Online Article Text |
id | pubmed-8786283 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-87862832022-02-01 Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs Kliche, Johanna Ivarsson, Ylva Biochem J Structural Biology Cellular function is based on protein–protein interactions. A large proportion of these interactions involves the binding of short linear motifs (SLiMs) by folded globular domains. These interactions are regulated by post-translational modifications, such as phosphorylation, that create and break motif binding sites or tune the affinity of the interactions. In addition, motif-based interactions are involved in targeting serine/threonine kinases and phosphatases to their substrate and contribute to the specificity of the enzymatic actions regulating which sites are phosphorylated. Here, we review how SLiM-based interactions assist in determining the specificity of serine/threonine kinases and phosphatases, and how phosphorylation, in turn, affects motif-based interactions. We provide examples of SLiM-based interactions that are turned on/off, or are tuned by serine/threonine phosphorylation and exemplify how this affects SLiM-based protein complex formation. Portland Press Ltd. 2022-01-14 2022-01-06 /pmc/articles/PMC8786283/ /pubmed/34989786 http://dx.doi.org/10.1042/BCJ20200714 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by/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) (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Structural Biology Kliche, Johanna Ivarsson, Ylva Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs |
title | Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs |
title_full | Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs |
title_fullStr | Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs |
title_full_unstemmed | Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs |
title_short | Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs |
title_sort | orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8786283/ https://www.ncbi.nlm.nih.gov/pubmed/34989786 http://dx.doi.org/10.1042/BCJ20200714 |
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