Functional coupling between sodium-activated potassium channels and voltage-dependent persistent sodium currents in cricket Kenyon cells

Takahashi, Izumi; Yamada, Masami

doi:10.1152/jn.00087.2015

Cited by 10 publications

(14 citation statements)

References 42 publications

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“…To test the hypothesis that Na + influx through NALCN activates SLO2.1, we first performed whole-cell patch clamp on primary human MSMCs treated with the SLO1 K + channel blocker tetraethylammonium (TEA) ( Figure 1A ) (Khan, Smith, Morrison, & Ashford, 1993). Consistent with our previous findings in MSMCs (Ferreira et al, 2019) and others’ findings in neurons (Hage & Salkoff, 2012; Takahashi & Yoshino, 2015), addition of 80 mM extracellular Na + led to an 80-100% increase in K + currents at +80 mV and at -60 mV ( Figure 1B ), confirming that SLO2.1 is an Na + -activated K + channel. Next, because NALCN is a leak channel, we performed similar experiments in the presence of the Na + leak channel blocker gadolinium (Gd 3+ ) and found that 10 µM Gd 3+ completely inhibited the K + current activated by addition of extracellular Na + ( Figure 1C-E) .…”

Section: Resultssupporting

confidence: 92%

A novel sodium signaling complex regulates uterine activity

Ferreira

Amazu

Molina

et al. 2020

Preprint

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At the end of pregnancy, the uterus transitions from a quiescent state to an excitable, contractile state. These changes are linked to depolarization of the myometrial smooth muscle cell (MSMC) resting membrane potential. The membrane potential is primarily determined by the balance between an outward potassium (K+) leak current and an inward sodium (Na+) leak current. We recently described a Na+-activated K+ channel (SLO2.1) and a non-selective Na+ leak channel (NALCN) in human MSMCs. Here, we asked whether these channels function together. We show that SLO2.1 currents are activated by an inward NALCN-dependent Na+ leak current, leading to MSMC hyperpolarization. The regulation of the membrane potential by NALCN/SLO2.1 activity modulates both Ca2+ entry through VDCCs, and myometrial contractility. Finally, NALCN and SLO2.1 are in proximity to one another in human MSMCs. We conclude that SLO2.1 and NALCN function together to regulate human MSMC membrane potential and excitability.

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Section: Resultssupporting

confidence: 92%

A novel sodium signaling complex regulates uterine activity

Ferreira

Amazu

Molina

et al. 2020

Preprint

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“…Previous reports showed that neuronal K Na channel activity decreased when sodium entry pathways were blocked, suggesting that Na V channels reside in close proximity to K Na channels (17,46). Moreover, a coimmunolocalization was previously observed between the Slack K Na channel and Na V 1.8 in DRG neurons (16).…”

Section: Magi-1 Mediated Coupling Between Slack K Na Channels and Na mentioning

confidence: 79%

Magi‐1 scaffolds Na _v 1‐8 and Slack K _Na channels in dorsal root ganglion neurons regulating excitability and pain

et al. 2019

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Voltage‐dependent sodium (Nav) 1.8 channels regulate action potential generation in nociceptive neurons, identifying them as putative analgesic targets. Here, we show that Nav1.8 channel plasma membrane localization, retention, and stability occur through a direct interaction with the postsynaptic density‐95/discs large/zonula occludens‐l‐and WW domain‐containing scaffold protein called membrane‐associated guanylate kinase with inverted orientation (Magi)‐l. The neurophysiological roles of Magi‐1 are largely unknown, but we found that dorsal root ganglion (DRG)‐specific knockdown of Magi‐1 attenuated thermal nociception and acute inflammatory pain and produced deficits in Nav1.8 protein expression. A competing cell‐penetrating peptide mimetic derived from the Nav1.8 WW binding motif decreased sodium currents, reduced Nav1.8 protein expression, and produced hypoexcitability. Remarkably, a phosphorylated variant of the very same peptide caused an opposing increase in Nav1.8 surface expression and repetitive firing. Likewise, in vivo, the peptides produced diverging effects on nocifensive behavior. Additionally, we found that Magi‐1 bound to sequence like a calcium‐activated potassium channel sodium‐activated (Slack) potassium channels, demonstrating macrocomplexing with Nav1.8 channels. Taken together, these findings emphasize Magi‐1 as an essential scaffold for ion transport in DRG neurons and a central player in pain.—Pryce, K. D., Powell, R., Agwa, D., Evely, K. M., Sheehan, G. D., Nip, A., Tomasello, D. L., Gururaj, S., Bhattacharjee, A. Magi‐1 scaffolds Nav1.8 and Slack KNa channels in dorsal root ganglion neurons regulating excitability and pain. FASEB J. 33, 7315–7330 (2019). http://www.fasebj.org

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“…Notably, studies of central cultured neurons dissociated from olfactory bulbs have reported a strong relationship between K Na channels and persistent Na ϩ channels (Budelli et al 2009;Hage and Salkoff 2012). Recently, similar functional coupling was demonstrated in Kenyon cells of the cricket G. bimaculatus (Takahashi and Yoshino 2015). This coupling mechanism has been shown to play an important role in producing membrane oscillation because this oscillation is eliminated by applying the persistent Na ϩ channel blocker TTX or the K Na channel blocker quinidine (Inoue et al 2014).…”

Section: Discussionmentioning

confidence: 77%

Nitric oxide/cGMP/PKG signaling pathway activated by M₁-type muscarinic acetylcholine receptor cascade inhibits Na⁺-activated K⁺currents in Kenyon cells

Hasebe

Yamada

2016

Journal of Neurophysiology

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activity in Kenyon cells of crickets (Gryllus bimaculatus). We found that two different NO donors, S-nitrosoglutathione (GSNO) and S-nitroso-N-acetyl-DL-penicillamine(SNAP), strongly suppressed K Na channel currents. Additionally, this inhibitory effect of GSNO on K Na channel activity was diminished by 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one (ODQ), an inhibitor of soluble guanylate cyclase (sGC), and KT5823, an inhibitor of protein kinase G (PKG). Next, we analyzed the role of ACh in the NO signaling cascade. ACh strongly suppressed K Na channel currents, similar to NO donors. Furthermore, this inhibitory effect of ACh was blocked by pirenzepine, an M 1 muscarinic ACh receptor antagonist, but not by 1,1-dimethyl-4-diphenylacetoxypiperidinium iodide (4-DAMP) and mecamylamine, an M 3 muscarinic ACh receptor antagonist and a nicotinic ACh receptor antagonist, respectively. The ACh-induced inhibition of K Na channel currents was also diminished by the PLC inhibitor U73122 and the calmodulin antagonist W-7. Finally, we found that ACh inhibition was blocked by the nitric oxide synthase (NOS) inhibitor N G -nitro-L-arginine methyl ester (L-NAME). These results suggested that the ACh signaling cascade promotes NO production by activating NOS and NO inhibits K Na channel currents via the sGC/cGMP/PKG signaling cascade in Kenyon cells.

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Functional coupling between sodium-activated potassium channels and voltage-dependent persistent sodium currents in cricket Kenyon cells

Abstract: Takahashi I, Yoshino M. Functional coupling between sodiumactivated potassium channels and voltage-dependent persistent sodium currents in cricket Kenyon cells.

Cited by 10 publications

References 42 publications

A novel sodium signaling complex regulates uterine activity

A novel sodium signaling complex regulates uterine activity

Magi‐1 scaffolds Na _v 1‐8 and Slack K _Na channels in dorsal root ganglion neurons regulating excitability and pain

Nitric oxide/cGMP/PKG signaling pathway activated by M₁-type muscarinic acetylcholine receptor cascade inhibits Na⁺-activated K⁺currents in Kenyon cells

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Functional coupling between sodium-activated potassium channels and voltage-dependent persistent sodium currents in cricket Kenyon cells

Abstract: Takahashi I, Yoshino M. Functional coupling between sodiumactivated potassium channels and voltage-dependent persistent sodium currents in cricket Kenyon cells.

Cited by 10 publications

References 42 publications

A novel sodium signaling complex regulates uterine activity

A novel sodium signaling complex regulates uterine activity

Magi‐1 scaffolds Na v 1‐8 and Slack K Na channels in dorsal root ganglion neurons regulating excitability and pain

Nitric oxide/cGMP/PKG signaling pathway activated by M1-type muscarinic acetylcholine receptor cascade inhibits Na+-activated K+currents in Kenyon cells

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Magi‐1 scaffolds Na _v 1‐8 and Slack K _Na channels in dorsal root ganglion neurons regulating excitability and pain

Nitric oxide/cGMP/PKG signaling pathway activated by M₁-type muscarinic acetylcholine receptor cascade inhibits Na⁺-activated K⁺currents in Kenyon cells