Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability

Randy F. Stout, David C. Spray

Research output: Contribution to journalArticle

Abstract

Gap junctions are cellular contact sites composed of clustered connexin transmembrane proteins that act in dual capacities as channels for direct intercellular exchange of small molecules and as structural adhesion complexes known as gap junction nexuses. Depending on the connexin isoform, the cluster of channels (the gap junction plaque) can be stably or fluidly arranged. Here we used confocal microscopy and mutational analysis to identify the residues within the connexin proteins that determine gap junction plaque stability. We found that stability is altered by changing redox balance using a reducing agent-indicating gap junction nexus stability is modifiable. Stability of the arrangement of connexins is thought to regulate intercellular communication by establishing an ordered supramolecular platform. By identifying the residues that establish plaque stability, these studies lay the groundwork for exploration of mechanisms by which gap junction nexus stability modulates intercellular communication.

Original languageEnglish (US)
Pages (from-to)2757-2764
Number of pages8
JournalMolecular Biology of the Cell
Volume28
Issue number21
DOIs
StatePublished - Oct 15 2017

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Connexins
Gap Junctions
Cysteine
Reducing Agents
Confocal Microscopy
Oxidation-Reduction
Protein Isoforms
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Cysteine residues in the cytoplasmic carboxy terminus of connexins dictate gap junction plaque stability. / Stout, Randy F.; Spray, David C.

In: Molecular Biology of the Cell, Vol. 28, No. 21, 15.10.2017, p. 2757-2764.

Research output: Contribution to journalArticle

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