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Gap junction channel gating modulated through protein phosphorylation.

Alonso P Moreno1, Alan F Lau

  • 1Department of Internal Medicine, University of Utah, Nora Eccles Cardiovascular Research and Training Institute, Salt Lake City, UT 84112, USA. moreno@cvrti.utah.edu

Progress in Biophysics and Molecular Biology
|May 18, 2007
PubMed
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Protein phosphorylation regulates intercellular communication by altering gap junction channel gating. This review explores current research on how phosphorylation modifies connexin, pannexin, and innexin channel function.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein phosphorylation is a critical post-translational modification regulating membrane protein function.
  • Gap junction channels, formed by connexins, pannexins, and innexins, are vital for intercellular communication.
  • Phosphorylation of connexins affects tyrosine, serine, and threonine residues, impacting channel function.

Purpose of the Study:

  • To review current research on the molecular mechanisms of phosphorylation in gap junction channel gating.
  • To elucidate how phosphorylation triggers and modulates the function of connexin, pannexin, and innexin channels.

Main Methods:

  • Literature review of current research on protein phosphorylation and gap junction channels.
  • Analysis of studies investigating kinase activation/inactivation and its effect on intercellular communication.

Related Experiment Videos

  • Synthesis of findings related to altered channel gating properties due to phosphorylation.

    • Main Results:

    • Phosphorylation significantly impacts intercellular communication by altering gap junction channel properties.
    • While numerous kinases affect channel function, the precise molecular mechanisms remain incompletely understood.
    • Current research focuses on elucidating how specific phosphorylation events modulate channel gating.

    Conclusions:

    • Phosphorylation is a key regulator of gap junction channel gating and intercellular communication.
    • Further research is needed to fully understand the molecular mechanisms by which phosphorylation alters channel function.
    • This review highlights current advancements in understanding phosphorylation's role in connexin, pannexin, and innexin channel modulation.