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Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
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Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

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OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel

Bernat Elvira, Yogesh Singh, Jamshed Warsi

    Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology
    |April 28, 2016
    PubMed
    Abstract

    Insights

    Oxidative stress-responsive kinase 1 (OSR1) and SPAK suppress large conductance Ca2+-activated K+ (BK) channels. This finding may impact cell volume regulation and neuronal excitability.

    Area of Science:

    • Molecular biology
    • Ion channel physiology
    • Cell signaling

    Background:

    • Oxidative stress-responsive kinase 1 (OSR1) and SPAK are regulated by WNK kinases and influence cell volume and neuronal excitability.
    • Large conductance Ca2+-activated K+ (BK) channels also modulate cell volume and neuronal excitation.
    • The interaction between OSR1/SPAK and BK channels has not been previously investigated.

    Purpose of the Study:

    • To investigate whether OSR1 and/or SPAK influence the activity of BK channels.

    Main Methods:

    • cRNA encoding a Ca2+-insensitive BK channel mutant was injected into Xenopus laevis oocytes.
    • Oocytes were co-injected with cRNA for wild-type or mutant forms of OSR1 or SPAK.
    • Potassium channel activity was measured using dual electrode voltage clamp.

    Main Results:

    • Co-expression of OSR1 or SPAK significantly decreased BK channel activity.
    • The suppressive effect of wild-type OSR1/SPAK was replicated by constitutively active mutants but not by catalytically inactive mutants.

    Conclusions:

    • OSR1 and SPAK actively suppress BK channel function.
    • This suppression may play a role in regulating cell volume and neuronal excitability.

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