Phosphorylation of human CEACAM1-LF by PKA and GSK3β promotes its interaction with β-catenin.
CEACAM1
GSK3β
MS
NMR
PKA
molecular modeling
β-catenin
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
11 2021
11 2021
Historique:
received:
18
07
2021
revised:
05
10
2021
accepted:
12
10
2021
pubmed:
18
10
2021
medline:
18
12
2021
entrez:
17
10
2021
Statut:
ppublish
Résumé
CEACAM1-LF, a homotypic cell adhesion adhesion molecule, transduces intracellular signals via a 72 amino acid cytoplasmic domain that contains two immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and a binding site for β-catenin. Phosphorylation of Ser503 by PKC in rodent CEACAM1 was shown to affect bile acid transport or hepatosteatosis via the level of ITIM phosphorylation, but the phosphorylation of the equivalent residue in human CEACAM1 (Ser508) was unclear. Here we studied this analogous phosphorylation by NMR analysis of the
Identifiants
pubmed: 34656562
pii: S0021-9258(21)01111-X
doi: 10.1016/j.jbc.2021.101305
pmc: PMC8564729
pii:
doi:
Substances chimiques
Antigens, CD
0
CD66 antigens
0
CTNNB1 protein, human
0
Cell Adhesion Molecules
0
beta Catenin
0
GSK3B protein, human
EC 2.7.11.1
Glycogen Synthase Kinase 3 beta
EC 2.7.11.1
Cyclic AMP-Dependent Protein Kinases
EC 2.7.11.11
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
101305Subventions
Organisme : NCI NIH HHS
ID : P30 CA033572
Pays : United States
Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.