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Related Experiment Videos

Multiple structural elements in voltage-dependent Ca2+ channels support their inhibition by G proteins

J F Zhang1, P T Ellinor, R W Aldrich

  • 1Department of Molecular and Cellular Physiology, Stanford University, California 94305, USA.

Neuron
|November 1, 1996
PubMed
Summary

Molecular determinants of calcium channel responsiveness to G protein inhibition were studied. Essential structural elements for G protein modulation reside in multiple calcium channel domains, not solely the I-II loop.

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Area of Science:

  • Molecular pharmacology
  • Neuroscience
  • Ion channel physiology

Background:

  • Receptor-coupled G proteins modulate calcium (Ca2+) channel activity.
  • Different Ca2+ channel subtypes (N-type, P/Q-type, L-type) exhibit varying sensitivities to G protein inhibition.
  • The precise molecular mechanisms underlying these differential responses are not fully understood.

Purpose of the Study:

  • To investigate the molecular determinants of Ca2+ channel responsiveness to G protein-coupled receptor (GPCR) inhibition.
  • To identify specific structural regions within Ca2+ channel alpha1 subunits responsible for differential G protein modulation.
  • To test the hypothesis that G protein subunits and Ca2+ channel beta subunits compete at the I-II loop.

Main Methods:

  • Experiments conducted in Xenopus oocytes expressing various Ca2+ channel alpha1 subunits (alpha1B, alpha1A, alpha1C).

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  • Site-directed mutagenesis and chimera construction to alter specific domains of alpha1 subunits, including the I-II loop, motif I, and C-terminus.
  • Assessment of G protein-mediated inhibition of Ca2+ channel currents.

    • Main Results:

    • Alpha1B (N-type) channels showed significantly greater inhibition by G proteins than alpha1A (P/Q-type) channels; alpha1C (L-type) channels were unresponsive.
    • Mutations or replacements of the I-II loop did not alter G protein-mediated inhibition, refuting competition at this site.
    • Full interconversion of modulatory behavior between alpha1B and alpha1A channels required swapping both motif I and the C-terminus.

    Conclusions:

    • Essential structural elements conferring differential G protein modulation are distributed across multiple domains of Ca2+ channel alpha1 subunits.
    • The I-II loop is not the sole determinant for differential G protein modulation.
    • Complex interactions involving motif I and the C-terminus are critical for fine-tuning G protein-calcium channel coupling.