Journal
CIRCULATION RESEARCH
Volume 95, Issue 4, Pages 22-28Publisher
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1161/01.RES.0000140737.62245.c5
Keywords
connexin43; gap junction; pH gating
Funding
- NHLBI NIH HHS [P01-HL-39707] Funding Source: Medline
- NIGMS NIH HHS [R01-GM-5769] Funding Source: Medline
- NIMH NIH HHS [MH65459] Funding Source: Medline
- NINDS NIH HHS [NS41282, NS07098] Funding Source: Medline
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Connexin43 (Cx43) channels reside in at least 3 states: closed, open, or residual. It is hypothesized that the residual state results from the interaction of an intracellular gating element with structures at the vestibule of the pore. Recently, we showed in vitro that there is an intramolecular interaction of the carboxyl-terminal domain (referred to as CT) with a region in the cytoplasmic loop of Cx43 (amino acids 119 to 144; referred to as L2). Here, we assessed whether the L2 region was able to interact with the gating particle in a functional channel. Cx43 channels were recorded in the presence of a peptide corresponding to the L2 region, delivered via the patch pipette. This manipulation did not modify unitary conductance, but decreased the frequency of transitions into the residual state, prolonged open time, and altered the voltage dependence of the channel in a manner analogous to that observed after truncation of the CT domain. The latter correlated with the ability of the peptide to bind to the CT domain, as determined by mirror resonance spectroscopy. Overall, we propose that the L2 acts as a receptor that interacts with a flexible intracellular gating element during channel gating. The full text of this article is available online at http://circres.ahajournals.org.
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