FEBS Letters
Volume 582, Issue 2 , Pages 165-170, 23 January 2008

Cx23, a connexin with only four extracellular-loop cysteines, forms functional gap junction channels and hemichannels

Edited by Takashi Gojobori

  • M. Kathryn Iovine

      Affiliations

    • Lehigh University, Department of Biological Sciences, 111 Research Drive, Bethlehem, PA 18015, United States
    • Corresponding Author InformationCorresponding author. Fax: +1 610 758 4004.
  • ,
  • Anna M. Gumpert

      Affiliations

    • Lehigh University, Department of Biological Sciences, 111 Research Drive, Bethlehem, PA 18015, United States
  • ,
  • Matthias M. Falk

      Affiliations

    • Lehigh University, Department of Biological Sciences, 111 Research Drive, Bethlehem, PA 18015, United States
  • ,
  • Tamra C. Mendelson

      Affiliations

    • University of Maryland Baltimore County, Department of Biological Sciences, 1000 Hilltop Circle, Baltimore, MD 21250, United States

Received 27 July 2007; received in revised form 7 November 2007; accepted 28 November 2007. published online 06 December 2007.

Abstract 

Gap junction channels may be comprised of either connexin or pannexin proteins (innexins and pannexins). Membrane topologies of both families are similar, but sequence similarity is lacking. Recently, connexin-like sequences have been identified in mammalian and zebrafish genomes that have only four conserved cysteines in the extracellular domains (Cx23), a feature of the pannexins. Phylogenetic analyses of the non-canonical “C4” connexins reveal that these sequences are indeed connexins. Functional assays reveal that the Cx23 gap junctions are capable of sharing neurobiotin, and further, that Cx23 connexins form hemichannels in vitro.

Keywords: Gap junction, Connexin, Zebrafish, Pannexin, Cx23

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PII: S0014-5793(07)01233-1

doi:10.1016/j.febslet.2007.11.079

FEBS Letters
Volume 582, Issue 2 , Pages 165-170, 23 January 2008