Look for the Scaffold: Multifaceted Regulation of Enzyme Activity by 14-3-3 Proteins.
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F24%3A00598245" target="_blank" >RIV/67985823:_____/24:00598245 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00216208:11310/24:10485787
Výsledek na webu
<a href="https://www.biomed.cas.cz/physiolres/pdf/2024/73_S401.pdf" target="_blank" >https://www.biomed.cas.cz/physiolres/pdf/2024/73_S401.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.33549/physiolres.935306" target="_blank" >10.33549/physiolres.935306</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Look for the Scaffold: Multifaceted Regulation of Enzyme Activity by 14-3-3 Proteins.
Popis výsledku v původním jazyce
Enzyme activity is regulated by several mechanisms, including phosphorylation. Phosphorylation is a key signal transduction process in all eukaryotic cells and is thus crucial for virtually all cellular processes. In addition to its direct effect on protein structure, phosphorylation also affects protein-protein interactions, such as binding to scaffolding 14-3-3 proteins, which selectively recognize phosphorylated motifs. These interactions then modulate the catalytic activity, cellular localisation and interactions of phosphorylated enzymes through different mechanisms. The aim of this mini-review is to highlight several examples of 14-3-3 protein-dependent mechanisms of enzyme regulation previously studied in our laboratory over the past decade. More specifically, we address here the regulation of the human enzymes ubiquitin ligase Nedd4-2, procaspase-2, calciumcalmodulin dependent kinases CaMKK1/2, and death-associated protein kinase 2 (DAPK2) and yeast neutral trehalase Nth1.
Název v anglickém jazyce
Look for the Scaffold: Multifaceted Regulation of Enzyme Activity by 14-3-3 Proteins.
Popis výsledku anglicky
Enzyme activity is regulated by several mechanisms, including phosphorylation. Phosphorylation is a key signal transduction process in all eukaryotic cells and is thus crucial for virtually all cellular processes. In addition to its direct effect on protein structure, phosphorylation also affects protein-protein interactions, such as binding to scaffolding 14-3-3 proteins, which selectively recognize phosphorylated motifs. These interactions then modulate the catalytic activity, cellular localisation and interactions of phosphorylated enzymes through different mechanisms. The aim of this mini-review is to highlight several examples of 14-3-3 protein-dependent mechanisms of enzyme regulation previously studied in our laboratory over the past decade. More specifically, we address here the regulation of the human enzymes ubiquitin ligase Nedd4-2, procaspase-2, calciumcalmodulin dependent kinases CaMKK1/2, and death-associated protein kinase 2 (DAPK2) and yeast neutral trehalase Nth1.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10609 - Biochemical research methods
Návaznosti výsledku
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
Ostatní
Rok uplatnění
2024
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Physiological Research
ISSN
0862-8408
e-ISSN
1802-9973
Svazek periodika
73
Číslo periodika v rámci svazku
Suppl.1
Stát vydavatele periodika
CZ - Česká republika
Počet stran výsledku
12
Strana od-do
"S401"-"S412"
Kód UT WoS článku
001295308400022
EID výsledku v databázi Scopus
2-s2.0-85202716552