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Structural insights into the functional roles of 14-3-3 proteins
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SYSNO ASEP 0562211 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Structural insights into the functional roles of 14-3-3 proteins Author(s) Obšilová, Veronika (FGU-C) RID, ORCID, SAI
Obšil, T. (CZ)Article number 1016071 Source Title Frontiers in molecular biosciences
Roč. 9, Sep 16 (2022)Number of pages 15 s. Language eng - English Country CH - Switzerland Keywords 14-3-3 proteins ; protein-protein interactions ; phosphorylation ; molecular mechanism ; scaffolding ; adaptor protein OECD category Biochemistry and molecular biology R&D Projects GA21-02080S GA ČR - Czech Science Foundation (CSF) GA19-00121S GA ČR - Czech Science Foundation (CSF) Method of publishing Open access Institutional support FGU-C - RVO:67985823 UT WOS 000862707900001 EID SCOPUS 85139222950 DOI 10.3389/fmolb.2022.1016071 Annotation Signal transduction cascades efficiently transmit chemical and/or physical signals from the extracellular environment to intracellular compartments, thereby eliciting an appropriate cellular response. Most often, these signaling processes are mediated by specific protein-protein interactions involving hundreds of different receptors, enzymes, transcription factors, and signaling, adaptor and scaffolding proteins. Among them, 14-3-3 proteins are a family of highly conserved scaffolding molecules expressed in all eukaryotes, where they modulate the function of other proteins, primarily in a phosphorylation-dependent manner. Through these binding interactions, 14-3-3 proteins participate in key cellular processes, such as cell-cycle control, apoptosis, signal transduction, energy metabolism, and protein trafficking. To date, several hundreds of 14-3-3 binding partners have been identified, including protein kinases, phosphatases, receptors and transcription factors, which have been implicated in the onset of various diseases. As such, 14-3-3 proteins are promising targets for pharmaceutical interventions. However, despite intensive research into their protein-protein interactions, our understanding of the molecular mechanisms whereby 14-3-3 proteins regulate the functions of their binding partners remains insufficient. This review article provides an overview of the current state of the art of the molecular mechanisms whereby 14-3-3 proteins regulate their binding partners, focusing on recent structural studies of 14-3-3 protein complexes. Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2023 Electronic address https://doi.org/10.3389/fmolb.2022.1016071
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