Structural insights into the functional roles of 14-3-3 proteins
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 involvi...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2022-09-01
|
| Series: | Frontiers in Molecular Biosciences |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/fmolb.2022.1016071/full |
| _version_ | 1828145637177163776 |
|---|---|
| author | Veronika Obsilova Tomas Obsil |
| author_facet | Veronika Obsilova Tomas Obsil |
| author_sort | Veronika Obsilova |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-11T20:34:27Z |
| format | Article |
| id | doaj.art-a5c0432fcfb24598a3bac6e9734c118d |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-04-11T20:34:27Z |
| publishDate | 2022-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-a5c0432fcfb24598a3bac6e9734c118d2022-12-22T04:04:24ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2022-09-01910.3389/fmolb.2022.10160711016071Structural insights into the functional roles of 14-3-3 proteinsVeronika Obsilova0Tomas Obsil1Institute of Physiology of the Czech Academy of Sciences, Laboratory of Structural Biology of Signaling Proteins, Division BIOCEV, Vestec, CzechiaDepartment of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, CzechiaSignal 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.https://www.frontiersin.org/articles/10.3389/fmolb.2022.1016071/full14-3-3 proteinsprotein-protein interactionsphosphorylationmolecular mechanismscaffoldingadaptor protein |
| spellingShingle | Veronika Obsilova Tomas Obsil Structural insights into the functional roles of 14-3-3 proteins Frontiers in Molecular Biosciences 14-3-3 proteins protein-protein interactions phosphorylation molecular mechanism scaffolding adaptor protein |
| title | Structural insights into the functional roles of 14-3-3 proteins |
| title_full | Structural insights into the functional roles of 14-3-3 proteins |
| title_fullStr | Structural insights into the functional roles of 14-3-3 proteins |
| title_full_unstemmed | Structural insights into the functional roles of 14-3-3 proteins |
| title_short | Structural insights into the functional roles of 14-3-3 proteins |
| title_sort | structural insights into the functional roles of 14 3 3 proteins |
| topic | 14-3-3 proteins protein-protein interactions phosphorylation molecular mechanism scaffolding adaptor protein |
| url | https://www.frontiersin.org/articles/10.3389/fmolb.2022.1016071/full |
| work_keys_str_mv | AT veronikaobsilova structuralinsightsintothefunctionalrolesof1433proteins AT tomasobsil structuralinsightsintothefunctionalrolesof1433proteins |