Phosphorylation, compartmentalization, and cardiac function.
A kinase anchoring proteins
cardiac biology
cell signaling
protein kinase A
protein phosphorylation
spatial biology
Journal
IUBMB life
ISSN: 1521-6551
Titre abrégé: IUBMB Life
Pays: England
ID NLM: 100888706
Informations de publication
Date de publication:
04 2023
04 2023
Historique:
received:
13
07
2022
accepted:
15
09
2022
pmc-release:
01
04
2024
medline:
29
3
2023
pubmed:
1
10
2022
entrez:
30
9
2022
Statut:
ppublish
Résumé
Protein phosphorylation is a fundamental element of cell signaling. First discovered as a biochemical switch in glycogen metabolism, we now know that this posttranslational modification permeates all aspects of cellular behavior. In humans, over 540 protein kinases attach phosphate to acceptor amino acids, whereas around 160 phosphoprotein phosphatases remove phosphate to terminate signaling. Aberrant phosphorylation underlies disease, and kinase inhibitor drugs are increasingly used clinically as targeted therapies. Specificity in protein phosphorylation is achieved in part because kinases and phosphatases are spatially organized inside cells. A prototypic example is compartmentalization of the cyclic adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase A through association with A-kinase anchoring proteins. This configuration creates autonomous signaling islands where the anchored kinase is constrained in proximity to activators, effectors, and selected substates. This article primarily focuses on A kinase anchoring protein (AKAP) signaling in the heart with an emphasis on anchoring proteins that spatiotemporally coordinate excitation-contraction coupling and hypertrophic responses.
Identifiants
pubmed: 36177749
doi: 10.1002/iub.2677
pmc: PMC10049969
mid: NIHMS1839205
doi:
Substances chimiques
A Kinase Anchor Proteins
0
Cyclic AMP-Dependent Protein Kinases
EC 2.7.11.11
Protein Kinases
EC 2.7.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
353-369Subventions
Organisme : NIH HHS
ID : R01DK119192
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK119192
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK119186
Pays : United States
Organisme : NIDDK NIH HHS
ID : DK119186
Pays : United States
Organisme : NHLBI NIH HHS
ID : HL007828
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM048231
Pays : United States
Organisme : NHLBI NIH HHS
ID : HL160558
Pays : United States
Organisme : NIDDK NIH HHS
ID : DK119192
Pays : United States
Organisme : NIH HHS
ID : R01DK119186
Pays : United States
Informations de copyright
© 2022 International Union of Biochemistry and Molecular Biology.
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