The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases

Phosphorylation by kinases governs many key cellular and extracellular processes, such as transcription, cell cycle progression, differentiation, secretion and apoptosis. Unsurprisingly, tight and precise kinase regulation is a prerequisite for normal cell functioning, whereas kinase dysregulation o...

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Main Authors: Veronika Obsilova, Tomas Obsil
Format: Article
Language:English
Published: MDPI AG 2020-11-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/21/22/8824
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author Veronika Obsilova
Tomas Obsil
author_facet Veronika Obsilova
Tomas Obsil
author_sort Veronika Obsilova
collection DOAJ
description Phosphorylation by kinases governs many key cellular and extracellular processes, such as transcription, cell cycle progression, differentiation, secretion and apoptosis. Unsurprisingly, tight and precise kinase regulation is a prerequisite for normal cell functioning, whereas kinase dysregulation often leads to disease. Moreover, the functions of many kinases are regulated through protein–protein interactions, which in turn are mediated by phosphorylated motifs and often involve associations with the scaffolding and chaperon protein 14-3-3. Therefore, the aim of this review article is to provide an overview of the state of the art on 14-3-3-mediated kinase regulation, focusing on the most recent mechanistic insights into these important protein–protein interactions and discussing in detail both their structural aspects and functional consequences.
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spelling doaj.art-0d75edde0b9e458288c605fc9d4ea25f2023-11-20T21:51:02ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-012122882410.3390/ijms21228824The 14-3-3 Proteins as Important Allosteric Regulators of Protein KinasesVeronika Obsilova0Tomas Obsil1Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, 25250 Vestec, Czech RepublicDepartment of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, 25250 Vestec, Czech RepublicPhosphorylation by kinases governs many key cellular and extracellular processes, such as transcription, cell cycle progression, differentiation, secretion and apoptosis. Unsurprisingly, tight and precise kinase regulation is a prerequisite for normal cell functioning, whereas kinase dysregulation often leads to disease. Moreover, the functions of many kinases are regulated through protein–protein interactions, which in turn are mediated by phosphorylated motifs and often involve associations with the scaffolding and chaperon protein 14-3-3. Therefore, the aim of this review article is to provide an overview of the state of the art on 14-3-3-mediated kinase regulation, focusing on the most recent mechanistic insights into these important protein–protein interactions and discussing in detail both their structural aspects and functional consequences.https://www.mdpi.com/1422-0067/21/22/882414-3-3kinasephosphorylationRAF kinaseASK1CaMKK2
spellingShingle Veronika Obsilova
Tomas Obsil
The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
International Journal of Molecular Sciences
14-3-3
kinase
phosphorylation
RAF kinase
ASK1
CaMKK2
title The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
title_full The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
title_fullStr The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
title_full_unstemmed The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
title_short The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
title_sort 14 3 3 proteins as important allosteric regulators of protein kinases
topic 14-3-3
kinase
phosphorylation
RAF kinase
ASK1
CaMKK2
url https://www.mdpi.com/1422-0067/21/22/8824
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