Connexin43 Carboxyl-Terminal Domain Directly Interacts with β-Catenin

Autor: Matthew Cervantes, Mirtha Gutierrez, Gabriella Moore, Cleofes Sarmiento, Ishika Basu, Li Zheng, Andrew J. Trease, Paul L. Sorgen, Gaelle Spagnol
Jazyk: angličtina
Rok vydání: 2018
Předmět:
0301 basic medicine
Magnetic Resonance Spectroscopy
Catalysis
Article
Protein Structure
Secondary
Inorganic Chemistry
lcsh:Chemistry
03 medical and health sciences
Phosphoserine
0302 clinical medicine
Protein Domains
Animals
Humans
Amino Acid Sequence
Physical and Theoretical Chemistry
Cx43
β-catenin
phosphorylation
Molecular Biology
lcsh:QH301-705.5
Spectroscopy
beta Catenin
Regulation of gene expression
Transcriptional activity
Chemistry
Circular Dichroism
Organic Chemistry
Gap junction
Wnt signaling pathway
General Medicine
Surface Plasmon Resonance
Computer Science Applications
Cell biology
Rats
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
Catenin
Connexin 43
cardiovascular system
Phosphorylation
sense organs
biological phenomena
cell phenomena
and immunity
030217 neurology & neurosurgery
Homeostasis
Proto-oncogene tyrosine-protein kinase Src
Protein Binding
Zdroj: International Journal of Molecular Sciences; Volume 19; Issue 6; Pages: 1562
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 19, Iss 6, p 1562 (2018)
ISSN: 1422-0067
DOI: 10.3390/ijms19061562
Popis: Activation of Wnt signaling induces Connexin43 (Cx43) expression via the transcriptional activity of β-catenin, and results in the enhanced accumulation of the Cx43 protein and the formation of gap junction channels. In response to Wnt signaling, β-catenin co-localizes with the Cx43 protein itself as part of a complex at the gap junction plaque. Work from several labs have also shown indirect evidence of this interaction via reciprocal co-immunoprecipitation. Our goal for the current study was to identify whether β-catenin directly interacts with Cx43, and if so, the location of that direct interaction. Identifying residues involved in direct protein–protein interaction is of importance when they are correlated to the phosphorylation of Cx43, as phosphorylation can modify the binding affinities of Cx43 regulatory protein partners. Therefore, combining the location of a protein partner interaction on Cx43 along with the phosphorylation pattern under different homeostatic and pathological conditions will be crucial information for any potential therapeutic intervention. Here, we identified that β-catenin directly interacts with the Cx43 carboxyl-terminal domain, and that this interaction would be inhibited by the Src phosphorylation of Cx43CT residues Y265 and Y313.
Databáze: OpenAIRE
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