[HTML][HTML] Characterization of the pH-dependent interaction between the gap junction protein connexin43 carboxyl terminus and cytoplasmic loop domains
BJ Hirst-Jensen, P Sahoo, F Kieken, M Delmar… - Journal of biological …, 2007 - ASBMB
A prevailing view regarding the regulation of connexin43 (Cx43) gap junction channels is
that, upon intracellular acidification, the carboxyl-terminal domain (Cx43CT) moves toward
the channel opening to interact with specific residues acting as a receptor site. Previous
studies have demonstrated a direct, pH-dependent interaction between the Cx43CT and a
Cx43 cytoplasmic loop (Cx43CL) peptide. This interaction was dependent on α-helical
formation for the peptide in response to acidification; more recent studies have shown that …
that, upon intracellular acidification, the carboxyl-terminal domain (Cx43CT) moves toward
the channel opening to interact with specific residues acting as a receptor site. Previous
studies have demonstrated a direct, pH-dependent interaction between the Cx43CT and a
Cx43 cytoplasmic loop (Cx43CL) peptide. This interaction was dependent on α-helical
formation for the peptide in response to acidification; more recent studies have shown that …