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FEBS Lett. 2014 Apr 17;588(8):1230-7. doi: 10.1016/j.febslet.2014.01.042. Epub 2014 Feb 1.

Structure and closure of connexin gap junction channels.

Author information

1
Cellular and Structural Physiology Institute (CeSPI), Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan; Department of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan. Electronic address: atsu@cespi.nagoya-u.ac.jp.

Abstract

Connexin gap junctions comprise assembled channels penetrating two plasma membranes for which gating regulation is associated with a variety of factors, including voltage, pH, Ca(2+), and phosphorylation. Functional studies have established that various parts of the connexin peptides are related to channel closure and electrophysiology studies have provided several working models for channel gating. The corresponding structural models supporting these findings, however, are not sufficient because only small numbers of closed connexin structures have been reported. To fully understand the gating mechanisms, the channels should be visualized in both the open and closed states. Electron crystallography and X-ray crystallography studies recently revealed three-dimensional structures of connexin channels in a couple of states in which the main difference is the conformation of the N-terminal domain, which have helped to clarify the structure in regard to channel closure. Here the closure models for connexin gap junction channels inferred from structural and functional studies are described in the context of each domain of the connexin protein associated with gating modulation.

KEYWORDS:

Connexin; Electron microscopy; Function; Gating; Structure; X-ray crystallography

PMID:
24492007
DOI:
10.1016/j.febslet.2014.01.042
[Indexed for MEDLINE]
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