Paul L. Sorgen

TL;DR: The structure of the connexin43 carboxyl-terminal domain is characterized to assess its ability to interact with domains from ZO-1 and c-Src and it is demonstrated that the structural characteristics of a disordered Cx43CT are advantageous for signaling between different binding partners that may be important in describing the mechanism of channel closure or internalization in response to pathophysiological stimuli.

TL;DR: These data provide the first demonstration of chemically induced structural order and binding between cytoplasmic connexin domains and are proposed to be the receptor.

TL;DR: Analysis of 15N transverse, longitudinal and 15N{1H} nuclear Overhauser effect relaxation measurements yielded overall rotational correlation times of 8 to 12 nsec, similar to a 15–20 kDalton protein tumbling isotropically in solution, and consistent with the high quality NMR data observed.

TL;DR: It is shown that Cx43 is phosphorylated on S365 in cultured cells and heart tissue and can serve a “gatekeeper” function that may represent a mechanism to protect cells from ischemia and phorbol ester-induced down-regulation of channel conductance.

TL;DR: It is found that post-MI p-cSrc interacts with ZO-1 as Cx43 begins to decrease its interaction with Zo-1 and undergo initial loss of intercalated disk localization, indicating shifts in Cx 43 protein partners may underlie, in part, arrhythmogenesis in the post- MI heart.