The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F24%3A00583021" target="_blank" >RIV/67985823:_____/24:00583021 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/24:10477858

Výsledek na webu

<a href="https://doi.org/10.3389/fmolb.2024.1327014" target="_blank" >https://doi.org/10.3389/fmolb.2024.1327014</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3389/fmolb.2024.1327014" target="_blank" >10.3389/fmolb.2024.1327014</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways

Popis výsledku v původním jazyce

Cell signaling regulates several physiological processes by receiving, processing, and transmitting signals between the extracellular and intracellular environments. In signal transduction, phosphorylation is a crucial effector as the most common posttranslational modification. Selectively recognizing specific phosphorylated motifs of target proteins and modulating their functions through binding interactions, the yeast 14-3-3 proteins Bmh1 and Bmh2 are involved in catabolite repression, carbon metabolism, endocytosis, and mitochondrial retrograde signaling, among other key cellular processes. These conserved scaffolding molecules also mediate crosstalk between ubiquitination and phosphorylation, the spatiotemporal control of meiosis, and the activity of ion transporters Trk1 and Nha1. In humans, deregulation of analogous processes triggers the development of serious diseases, such as diabetes, cancer, viral infections, microbial conditions and neuronal and age-related diseases. Accordingly, the aim of this review article is to provide a brief overview of the latest findings on the functions of yeast 14-3-3 proteins, focusing on their role in modulating the aforementioned processes.

Název v anglickém jazyce

The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways

Popis výsledku anglicky

Cell signaling regulates several physiological processes by receiving, processing, and transmitting signals between the extracellular and intracellular environments. In signal transduction, phosphorylation is a crucial effector as the most common posttranslational modification. Selectively recognizing specific phosphorylated motifs of target proteins and modulating their functions through binding interactions, the yeast 14-3-3 proteins Bmh1 and Bmh2 are involved in catabolite repression, carbon metabolism, endocytosis, and mitochondrial retrograde signaling, among other key cellular processes. These conserved scaffolding molecules also mediate crosstalk between ubiquitination and phosphorylation, the spatiotemporal control of meiosis, and the activity of ion transporters Trk1 and Nha1. In humans, deregulation of analogous processes triggers the development of serious diseases, such as diabetes, cancer, viral infections, microbial conditions and neuronal and age-related diseases. Accordingly, the aim of this review article is to provide a brief overview of the latest findings on the functions of yeast 14-3-3 proteins, focusing on their role in modulating the aforementioned processes.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10609 - Biochemical research methods

Projekt

<a href="/cs/project/GA23-04686S" target="_blank" >GA23-04686S: Úloha vápníku a proteinu 14-3-3 v regulaci lidské ubikvitin ligásy Nedd4-2</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

Frontiers in molecular biosciences

ISSN

2296-889X

e-ISSN

2296-889X

Svazek periodika

11

Číslo periodika v rámci svazku

Jan 24

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

12

Strana od-do

1327014

Kód UT WoS článku

001157336400001

EID výsledku v databázi Scopus

2-s2.0-85184217430