OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel
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 excit...
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| Format: | Article |
| Language: | English |
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Cell Physiol Biochem Press GmbH & Co KG
2016-04-01
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| Series: | Cellular Physiology and Biochemistry |
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| Online Access: | http://www.karger.com/Article/FullText/443105 |
| _version_ | 1818466192869818368 |
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| author | Bernat Elvira Yogesh Singh Jamshed Warsi Carlos Munoz Florian Lang |
| author_facet | Bernat Elvira Yogesh Singh Jamshed Warsi Carlos Munoz Florian Lang |
| author_sort | Bernat Elvira |
| collection | DOAJ |
| description | 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 BKM513I+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 BKM513I+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. |
| first_indexed | 2024-04-13T20:55:58Z |
| format | Article |
| id | doaj.art-09cf8b3994a54fcd8ef9d727f023157d |
| institution | Directory Open Access Journal |
| issn | 1015-8987 1421-9778 |
| language | English |
| last_indexed | 2024-04-13T20:55:58Z |
| publishDate | 2016-04-01 |
| publisher | Cell Physiol Biochem Press GmbH & Co KG |
| record_format | Article |
| series | Cellular Physiology and Biochemistry |
| spelling | doaj.art-09cf8b3994a54fcd8ef9d727f023157d2022-12-22T02:30:19ZengCell Physiol Biochem Press GmbH & Co KGCellular Physiology and Biochemistry1015-89871421-97782016-04-013841652166210.1159/000443105443105OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ ChannelBernat ElviraYogesh SinghJamshed WarsiCarlos MunozFlorian LangBackground/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 BKM513I+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 BKM513I+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.http://www.karger.com/Article/FullText/443105Neuronal excitationBK channelsOxidative stress-responsive kinase 1SPS1-related proline/alanine-rich kinaseWNK |
| spellingShingle | Bernat Elvira Yogesh Singh Jamshed Warsi Carlos Munoz Florian Lang OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel Cellular Physiology and Biochemistry Neuronal excitation BK channels Oxidative stress-responsive kinase 1 SPS1-related proline/alanine-rich kinase WNK |
| title | OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel |
| title_full | OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel |
| title_fullStr | OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel |
| title_full_unstemmed | OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel |
| title_short | OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel |
| title_sort | osr1 and spak sensitivity of large conductance ca2 activated k channel |
| topic | Neuronal excitation BK channels Oxidative stress-responsive kinase 1 SPS1-related proline/alanine-rich kinase WNK |
| url | http://www.karger.com/Article/FullText/443105 |
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