Mechanosensitive unpaired innexin channels in C. elegans touch neurons

Rachele Sangaletti, Gerhard Dahl, Laura Bianchi

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Invertebrate innexin proteins share sequence homology with vertebrate pannexins and general membrane topology with both pannexins and connexins. While connexins form gap junctions that mediate intercellular communication, pannexins are thought to function exclusively as plasma membrane channels permeable to both ions and small molecules. Undoubtedly, certain innexins function as gap junction proteins. However, due to sequence similarity to pannexins, it was postulated that innexins also function as plasma membrane channels. Indeed, some of the leech innexins were found to mediate ATP release as unpaired membrane channels with shared pharmacology to pannexin channels. We show here thatCaenorhabditis elegans touch-sensing neurons express a mechanically gated innexin channel with a conductance of ∼1 nS and voltage-dependent and K+-selective subconductance state. We also show that C. elegans touch neurons take up ethidium bromide through a mechanism that is activated and blocked by innexin activating stimuli and inhibitors, respectively. Finally, we present evidence that touch neurons' innexins are required for cell death induced by chemical ischemia. Our work demonstrates that innexins function as plasma membrane channels in native C. elegans neurons, where they may play a role in pathological cell death.

Original languageEnglish (US)
Pages (from-to)C966-C977
JournalAmerican Journal of Physiology - Cell Physiology
Volume307
Issue number10
DOIs
StatePublished - Nov 15 2014

Keywords

  • C. elegans
  • Electrophysiology

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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