Structural insights into the functional roles of 14-3-3 proteins

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F22%3A00562211" target="_blank" >RIV/67985823:_____/22:00562211 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/22:10453415

Result on the web

<a href="https://doi.org/10.3389/fmolb.2022.1016071" target="_blank" >https://doi.org/10.3389/fmolb.2022.1016071</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3389/fmolb.2022.1016071" target="_blank" >10.3389/fmolb.2022.1016071</a>

Result language

angličtina

Original language name

Structural insights into the functional roles of 14-3-3 proteins

Original language 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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2022

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Frontiers in molecular biosciences

ISSN

2296-889X

e-ISSN

2296-889X

Volume of the periodical

9

Issue of the periodical within the volume

Sep 16

Country of publishing house

CH - SWITZERLAND

Number of pages

15

Pages from-to

1016071

UT code for WoS article

000862707900001

EID of the result in the Scopus database

2-s2.0-85139222950