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The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
V. Obsilova, T. Obsil
Language English Country Switzerland
Document type Journal Article, Review
Grant support
20-00058S and 19-00121S
Grantová Agentura České Republiky
RVO:67985823 of the Institute of Physiology
Czech Academy of Sciences
NLK
Free Medical Journals
from 2000
Freely Accessible Science Journals
from 2000
PubMed Central
from 2007
Europe PubMed Central
from 2007
ProQuest Central
from 2000-03-01
Open Access Digital Library
from 2000-01-01
Open Access Digital Library
from 2007-01-01
Health & Medicine (ProQuest)
from 2000-03-01
ROAD: Directory of Open Access Scholarly Resources
from 2000
PubMed
33233473
DOI
10.3390/ijms21228824
Knihovny.cz E-resources
- MeSH
- Allosteric Regulation genetics MeSH
- Apoptosis genetics MeSH
- Phosphorylation genetics MeSH
- Humans MeSH
- p38 Mitogen-Activated Protein Kinases genetics MeSH
- Protein Kinases genetics MeSH
- 14-3-3 Proteins genetics MeSH
- Signal Transduction genetics MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Review MeSH
Phosphorylation by kinases governs many key cellular and extracellular processes, such as transcription, cell cycle progression, differentiation, secretion and apoptosis. Unsurprisingly, tight and precise kinase regulation is a prerequisite for normal cell functioning, whereas kinase dysregulation often leads to disease. Moreover, the functions of many kinases are regulated through protein-protein interactions, which in turn are mediated by phosphorylated motifs and often involve associations with the scaffolding and chaperon protein 14-3-3. Therefore, the aim of this review article is to provide an overview of the state of the art on 14-3-3-mediated kinase regulation, focusing on the most recent mechanistic insights into these important protein-protein interactions and discussing in detail both their structural aspects and functional consequences.
References provided by Crossref.org
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