Research in the Thévenin Lab is focused on understanding how phosphorylation (a type of chemical modification) by kinases regulates protein-protein interactions and gap junction function. Gap junctions are cellular structures necessary for direct cell-cell communication within tissues. We study Connexin 43 (Cx43) – a membrane protein constituent of GJs. Cx43 can be phosphorylated by several kinases on over 15 sites, all necessary for the proper regulation of GJ function and cellular homeostasis. Our lab has uncovered specific phosphorylation events that help Cx43 function as a molecular scaffold and regulator of oncogenic proteins such as Src.
Experimental approaches in our lab include protein expression and purification from E.coli, kinase assays, mammalian cell culture, pull-downs and co-immunoprecipitation, western blotting, immunofluorescence by confocal microscopy, molecular cloning and mutagenesis, cellular fractionation, and various cell assays (viability, migration, apoptosis).
Our lab recently moved from Moravian University to Lafayette College (Summer 2025)
We are funded by the NIH R15 AREA Grant (1R15GM148)
