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Related Experiment Videos

Galpha12 differentially regulates Na+-H+ exchanger isoforms

X Lin1, T A Voyno-Yasenetskaya, R Hooley

  • 1Department of Stomatology, University of California, San Francisco, California 94143, USA.

The Journal of Biological Chemistry
|September 13, 1996
PubMed
Summary
This summary is machine-generated.

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Guanine nucleotide-binding proteins (GTPases) regulate ion transport. This study identifies G12 alpha subunit as an inhibitor of the Na+-H+ exchanger NHE1, contrasting with G13

Area of Science:

  • Molecular Biology
  • Cell Physiology
  • Signal Transduction

Background:

  • Guanine nucleotide-binding proteins (GTPases) are known to stimulate Na+-H+ exchange, increasing intracellular H+ efflux.
  • Specific GTPases like Gq, G13, Ras, Cdc42, and Rho activate this process.
  • GTPases that inhibit Na+-H+ exchange have not been identified, despite evidence from neurotransmitter studies.

Purpose of the Study:

  • To investigate the role of GTPases in the inhibition of Na+-H+ exchange.
  • To determine if the G12 alpha subunit is involved in regulating the Na+-H+ exchanger 1 (NHE1).

Main Methods:

  • Transient expression of mutationally activated Galpha12 in HEK293 cells and CCL39 fibroblasts.
  • Analysis of Na+-H+ exchanger (NHE) isoform activity in NHE-deficient AP1 cells stably expressing specific NHE isoforms.

Related Experiment Videos

  • Comparison of the effects of activated Galpha12 and Galpha13 on NHE1, NHE2, and NHE3 activity.

    • Main Results:

    • Mutationally activated Galpha12 inhibited serum- and Galpha13-stimulated NHE1 activity.
    • Activated Galpha12 inhibited NHE1 but stimulated NHE2 and NHE3 activities in AP1 cells.
    • Activated Galpha13 stimulated all three tested NHE isoforms (NHE1, NHE2, and NHE3).

    Conclusions:

    • The alpha subunit of G12 (Galpha12) actively inhibits the Na+-H+ exchanger NHE1.
    • Galpha12 and Galpha13 exhibit opposing effects on NHE1 activity, despite parallel roles in other cellular processes.
    • This study identifies a novel inhibitory role for a GTPase in regulating ion transport.