Regulation of Connexin32 by ephrin receptors and T-cell protein-tyrosine phosphatase.
EphA1
EphB1
TC-PTP
connexin
ephrin
gap junction
intercellular communication
intrinsically disordered protein
nuclear magnetic resonance (NMR)
protein phosphorylation
tyrosine kinase
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:
04 01 2019
04 01 2019
Historique:
received:
08
05
2018
revised:
25
10
2018
pubmed:
8
11
2018
medline:
10
4
2019
entrez:
8
11
2018
Statut:
ppublish
Résumé
Gap junctions are intercellular conduits that permit the passage of ions, small metabolites, and signaling molecules between cells. Connexin32 (Cx32) is a major gap junction protein in the liver and brain. Phosphorylation is integral to regulating connexin assembly, degradation, and electrical and metabolic coupling, as well as to interactions with molecular partners. Cx32 contains two intracellular tyrosine residues, and tyrosine phosphorylation of Cx32 has been detected after activation of the epidermal growth factor receptor; however, the specific tyrosine residue and the functional implication of this phosphorylation remain unknown. To address the limited available information on Cx32 regulation by tyrosine kinases, here we used the Cx32 C-terminal (CT) domain in an
Identifiants
pubmed: 30401746
pii: S0021-9258(20)36902-7
doi: 10.1074/jbc.RA118.003883
pmc: PMC6322898
pii:
doi:
Substances chimiques
Connexin 43
0
Connexins
0
Receptor, EphA1
EC 2.7.10.1
Receptor, EphB1
EC 2.7.10.1
Protein Tyrosine Phosphatase, Non-Receptor Type 2
EC 3.1.3.48
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
341-350Subventions
Organisme : NIGMS NIH HHS
ID : P20 GM103427
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM072631
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL131712
Pays : United States
Informations de copyright
© 2019 Trease et al.
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