A critical evaluation of protein kinase regulation by activation loop autophosphorylation.
activation
allostery
biochemistry
chemical biology
dimerization
inhibition
kinase
molecular biophysics
phosphorylation
structural biology
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
20 07 2023
20 07 2023
Historique:
received:
31
03
2023
accepted:
07
07
2023
medline:
21
7
2023
pubmed:
20
7
2023
entrez:
20
7
2023
Statut:
epublish
Résumé
Phosphorylation of proteins is a ubiquitous mechanism of regulating their function, localization, or activity. Protein kinases, enzymes that use ATP to phosphorylate protein substrates are, therefore, powerful signal transducers in eukaryotic cells. The mechanism of phosphoryl-transfer is universally conserved among protein kinases, which necessitates the tight regulation of kinase activity for the orchestration of cellular processes with high spatial and temporal fidelity. In response to a stimulus, many kinases enhance their own activity by autophosphorylating a conserved amino acid in their activation loop, but precisely how this reaction is performed is controversial. Classically, kinases that autophosphorylate their activation loop are thought to perform the reaction in
Identifiants
pubmed: 37470698
doi: 10.7554/eLife.88210
pii: 88210
pmc: PMC10359097
doi:
pii:
Substances chimiques
Protein Kinases
EC 2.7.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Austrian Science Fund FWF
ID : P30584
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : P33066
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : W1261
Pays : Austria
Informations de copyright
© 2023, Reinhardt and Leonard.
Déclaration de conflit d'intérêts
RR, TL No competing interests declared
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