Crystal structure reveals canonical recognition of the phosphorylated cytoplasmic loop of human alpha7 nicotinic acetylcholine receptor by 14-3-3 protein.
Domain-motif interaction
Intracellular loop
Neuronal receptors
Phosphorylation
Signaling
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
19 11 2023
19 11 2023
Historique:
received:
21
09
2023
accepted:
27
09
2023
medline:
1
11
2023
pubmed:
8
10
2023
entrez:
7
10
2023
Statut:
ppublish
Résumé
Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels composed of five homologous subunits. The homopentameric α7-nAChR, abundantly expressed in the brain, is involved in the regulation of the neuronal plasticity and memory and undergoes phosphorylation by protein kinase A (PKA). Here, we extracted native α7-nAChR from murine brain, validated its assembly by cryo-EM and showed that phosphorylation by PKA in vitro enables its interaction with the abundant human brain protein 14-3-3ζ. Bioinformatic analysis narrowed the putative 14-3-3-binding site down to the fragment of the intracellular loop (ICL) containing Ser365 (Q
Identifiants
pubmed: 37804592
pii: S0006-291X(23)01128-2
doi: 10.1016/j.bbrc.2023.09.086
pii:
doi:
Substances chimiques
14-3-3 Proteins
0
alpha7 Nicotinic Acetylcholine Receptor
0
Receptors, Nicotinic
0
Chrna7 protein, human
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
91-96Informations de copyright
Copyright © 2023 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.