The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the epithelial Na+ channel α,β,γ-ENaC

B. Friedrich, Y. Feng, P. Cohen, T. Risler, A. Vandewalle, S. Bröer, J. Wang, D. Pearce, F. Lang (Lead / Corresponding author)

    Research output: Contribution to journalArticle

    62 Citations (Scopus)

    Abstract

    The serum- and glucocorticoid-inducible kinase 1 (SGK1) has been identified as a signalling molecule up-regulated by aldosterone, which stimulates the renal epithelial Na+ channel ENaC. It is therefore thought to participate in the antinatriuretic action of this hormone. More recently, two isoforms, SGK2 and SGK3, have been cloned. The present study was performed to establish whether SGK2 and SGK3 influence ENaC activity similarly to SGK1. Dual-electrode voltage-clamp experiments in Xenopus laevis oocytes expressing α,β,γ-ENaC with or without SGK1, SGK2 or SGK3 revealed a stimulatory effect of all three kinases on the amiloride-sensitive current (INa). To establish whether the SGK isoforms exert their effects through direct phosphorylation, we replaced the serine at the SGK consensus site of αENaC (αS622AENaC) by site-directed mutagenesis. αS622A,β,γ-ENaC was up-regulated similar to wild-type ENaC, suggesting that SGK isoforms do not act via direct phosphorylation of the transport proteins. In conclusion, SGK2 and SGK3 mimic the function of SGK1 and are likely to participate in the regulation of ENaC activity.

    Original languageEnglish
    Pages (from-to)693-696
    Number of pages4
    JournalPflugers Archiv European Journal of Physiology
    Volume445
    Issue number6
    DOIs
    Publication statusPublished - 1 Mar 2003

    Fingerprint

    Epithelial Sodium Channels
    Protein-Serine-Threonine Kinases
    Glucocorticoids
    Phosphotransferases
    Protein Isoforms
    Phosphorylation
    Amiloride
    Xenopus laevis
    Site-Directed Mutagenesis
    Aldosterone
    Mutagenesis
    Serine
    Oocytes
    Clamping devices
    Carrier Proteins
    Electrodes
    Hormones
    Kidney
    serum-inducible kinase
    Molecules

    Keywords

    • ENaC
    • Kidney
    • Protein kinases
    • Sodium channel
    • Sodium reabsorption

    Cite this

    Friedrich, B. ; Feng, Y. ; Cohen, P. ; Risler, T. ; Vandewalle, A. ; Bröer, S. ; Wang, J. ; Pearce, D. ; Lang, F. / The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the epithelial Na+ channel α,β,γ-ENaC. In: Pflugers Archiv European Journal of Physiology. 2003 ; Vol. 445, No. 6. pp. 693-696.
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    abstract = "The serum- and glucocorticoid-inducible kinase 1 (SGK1) has been identified as a signalling molecule up-regulated by aldosterone, which stimulates the renal epithelial Na+ channel ENaC. It is therefore thought to participate in the antinatriuretic action of this hormone. More recently, two isoforms, SGK2 and SGK3, have been cloned. The present study was performed to establish whether SGK2 and SGK3 influence ENaC activity similarly to SGK1. Dual-electrode voltage-clamp experiments in Xenopus laevis oocytes expressing α,β,γ-ENaC with or without SGK1, SGK2 or SGK3 revealed a stimulatory effect of all three kinases on the amiloride-sensitive current (INa). To establish whether the SGK isoforms exert their effects through direct phosphorylation, we replaced the serine at the SGK consensus site of αENaC (αS622AENaC) by site-directed mutagenesis. αS622A,β,γ-ENaC was up-regulated similar to wild-type ENaC, suggesting that SGK isoforms do not act via direct phosphorylation of the transport proteins. In conclusion, SGK2 and SGK3 mimic the function of SGK1 and are likely to participate in the regulation of ENaC activity.",
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    The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the epithelial Na+ channel α,β,γ-ENaC. / Friedrich, B.; Feng, Y.; Cohen, P.; Risler, T.; Vandewalle, A.; Bröer, S.; Wang, J.; Pearce, D.; Lang, F. (Lead / Corresponding author).

    In: Pflugers Archiv European Journal of Physiology, Vol. 445, No. 6, 01.03.2003, p. 693-696.

    Research output: Contribution to journalArticle

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    AU - Friedrich, B.

    AU - Feng, Y.

    AU - Cohen, P.

    AU - Risler, T.

    AU - Vandewalle, A.

    AU - Bröer, S.

    AU - Wang, J.

    AU - Pearce, D.

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