<i>C. elegans</i> STK39/SPAK ortholog-mediated inhibition of ClC anion channel activity is regulated by WNK-independent ERK kinase signaling

Falin, Rebecca A.; Mitsuya, Hiroaki; Strange, Kevin

doi:10.1152/ajpcell.00343.2010

Cited by 19 publications

(17 citation statements)

References 58 publications

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“…38 GCK-3 is an ortholog of the mammalian STK39/SPAK kinase. SPAK and the closely related kinase OSR1 regulate the activity of the volume sensitive K-Cl and Na-K-2Cl cotransporters and play central roles in systemic salt and water homeostasis.…”

Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

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Strange¹

2011

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Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

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Strange¹

2011

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“…These kinases are phosphorylated by WNK (with-no-K[Lys]) kinases [3,[7][8][9][10], which thus similarly impact on ion transport and blood pressure [9][10][11][12][13][14][15][16][17]. SPAK and OSR1 regulate several carriers [18][19][20][21] [36][37][38][39][40][41][42][43][44][45]. Functions sensitive to WNK-OSR1/SPAK kinases include neuronal excitability [32,46].…”

Section: Introductionmentioning

confidence: 99%

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

Elvira¹,

Singh²,

Warsi³

et al. 2016

Cell Physiol Biochem

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Background/Aims: The oxidative stress-responsive kinase 1 (OSR1) and the serine/threonine kinases SPAK (SPS1-related proline/alanine-rich kinase) are under the control of WNK (with-no-K [Lys]) kinases. OSR1 and SPAK participate in diverse functions including cell volume regulation and neuronal excitability. Cell volume and neuronal excitation are further modified by the large conductance Ca²⁺-activated K⁺ channels (maxi K⁺ channel or BK channels). An influence of OSR1 and/or SPAK on BK channel activity has, however, never been shown. The present study thus explored whether OSR1 and/or SPAK modify the activity of BK channels. Methods: cRNA encoding the Ca²⁺ insensitive BK channel mutant BK^{M513I+Δ899-903} was injected into Xenopus laevis oocytes without or with additional injection of cRNA encoding wild-type OSR1 or wild-type SPAK, constitutively active ^T185EOSR1, catalytically inactive ^D164AOSR1, constitutively active ^T233ESPAK or catalytically inactive ^D212ASPAK. K⁺ channel activity was measured utilizing dual electrode voltage clamp. Results: BK channel activity in BK^{M513I+Δ899-903} expressing oocytes was significantly decreased by co-expression of OSR1 or SPAK. The effect of wild-type OSR1/SPAK was mimicked by ^T185EOSR1 and ^T233ESPAK, but not by ^D164AOSR1 or ^D212ASPAK. Conclusions: OSR1 and SPAK suppress BK channels, an effect possibly contributing to cell volume regulation and neuroexcitability.

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“…The kinases are phosphorylated by WNK (with-no-K[Lys] kinases) [1,7,8,9,10], which similarly contribute to the regulation of ion transport and blood pressure [9,10,11,12,13,14,15,16,17]. SPAK and OSR1 stimulate NaCl (NCC) and Na + , K + , 2Cl - (NKCC) co-transporters [4,5,6,7,8,11,18,19,20,21,22,23,24,25,26] as well as a number of ion channels [27,28,29,30]. SPAK/OSR1 are expressed in intestine [31].…”

Section: Introductionmentioning

confidence: 99%

Up-Regulation of Intestinal Phosphate Transporter NaPi-IIb (SLC34A2) by the Kinases SPAK and OSR1

Fezai

Elvira

Warsi

et al. 2015

Kidney Blood Press Res

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Background/Aims: SPAK (SPS1-related proline/alanine-rich kinase) and OSR1 (oxidative stress-responsive kinase 1), kinases controlled by WNK (with-no-K[Lys] kinase), are powerful regulators of cellular ion transport and blood pressure. Observations in gene-targeted mice disclosed an impact of SPAK/OSR1 on phosphate metabolism. The present study thus tested whether SPAK and/or OSR1 contributes to the regulation of the intestinal Na⁺-coupled phosphate co-transporter NaPi-IIb (SLC34A2). Methods: cRNA encoding NaPi-IIb was injected into Xenopus laevis oocytes without or with additional injection of cRNA encoding wild-type SPAK, constitutively active ^T233ESPAK, WNK insensitive ^T233ASPAK, catalytically inactive ^D212ASPAK, wild-type OSR1, constitutively active ^T185EOSR1, WNK insensitive ^T185AOSR1 or catalytically inactive ^D164AOSR1. The phosphate (1 mM)-induced inward current (I_Pi) was taken as measure of phosphate transport. Results: I_Pi was observed in NaPi-IIb expressing oocytes but not in water injected oocytes, and was significantly increased by co-expression of SPAK, ^T233ESPAK, OSR1, ^T185EOSR1 or SPAK+OSR1, but not by co-expression of ^T233ASPAK, ^D212ASPAK, ^T185AOSR1, or ^D164AOSR1. SPAK and OSR1 both increased the maximal transport rate of the carrier. Conclusions: SPAK and OSR1 are powerful stimulators of the intestinal Na⁺-coupled phosphate co-transporter NaPi-IIb.

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C. elegans STK39/SPAK ortholog-mediated inhibition of ClC anion channel activity is regulated by WNK-independent ERK kinase signaling

Cited by 19 publications

References 58 publications

Putting the pieces together

Putting the pieces together

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

Up-Regulation of Intestinal Phosphate Transporter NaPi-IIb (SLC34A2) by the Kinases SPAK and OSR1

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