Pannexin channels are not gap junction hemichannels

Gina E. Sosinsky, Daniela Boassa, Rolf Dermietzel, Heather S. Duffy, Dale W. Laird, Brian A. MacVicar, Christian C. Naus, Silvia Penuela, Eliana Scemes, David C. Spray, Roger J. Thompson, Hong Bo Zhao, Gerhard Dahl

Research output: Contribution to journalComment/debate

276 Scopus citations


Pannexins, a class of membrane channels, bear significant sequence homology with the invertebrate gap junction proteins, innexins, and more distant similarities in their membrane topologies and pharmacological sensitivities with the gap junction proteins, connexins. However, the functional role for the pannexin oligomers or pannexons, is different from connexin oligomers, the connexons. Many pannexin publications have used the term " hemichannels" to describe pannexin oligomers while others use the term "channels" instead. This has led to confusion within the literature about the function of pannexins that promotes the idea that pannexons serve as gap junction hemichannels and thus, have an assembly and functional state as gap junctional intercellular channels. Here, we present the case that unlike the connexin gap junction intercellular channels, so far, pannexin oligomers have repeatedly been shown to be channels that are functional in single membranes, but not as intercellular channels in appositional membranes. Hence, they should be referred to as channels and not hemichannels. Thus, we advocate that in the absence of firm evidence that pannexins form gap junctions, the use of the term "hemichannel" be discontinued within the pannexin literature.

Original languageEnglish
Issue number3
StatePublished - 2011


  • ATP signaling
  • Connexin
  • Connexon
  • Innexins
  • Intercellular communication
  • Pannexin
  • Pannexon
  • Purinergic receptors

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry


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