Regulation of Connexin32 by ephrin receptors and T-cell protein-tyrosine phosphatase

Andrew J. Trease, Hanjun Li, Gaelle Spagnol, Li Zheng, Kelly L. Stauch, Paul L Sorgen

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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 in vitro kinase-screening assay, which identified ephrin (Eph) receptor family members as tyrosine kinases that phosphorylate Cx32. We found that EphB1 and EphA1 phosphorylate the Cx32CT domain residue Tyr243. Unlike for Cx43, the tyrosine phosphorylation of the Cx32CT increased gap junction intercellular communication. We also demonstrated that T-cell protein-tyrosine phosphatase dephosphorylates pTyr243. The data presented above along with additional examples throughout the literature of gap junction regulation by kinases, indicate that one cannot extrapolate the effect of a kinase on one connexin to another.

Original languageEnglish (US)
Pages (from-to)341-350
Number of pages10
JournalJournal of Biological Chemistry
Issue number1
StatePublished - Jan 4 2019

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Regulation of Connexin32 by ephrin receptors and T-cell protein-tyrosine phosphatase'. Together they form a unique fingerprint.

Cite this