Molecular cloning and functional characterization of the Aplysia FMRFamide-gated Na+ channel

Furukawa, Yasuo; Miyawaki, Y; Abe, Genbu

doi:10.1007/s00424-005-1498-z

Cited by 33 publications

(30 citation statements)

References 39 publications

(86 reference statements)

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“…In the case of the mammalian nervous system, light-or ligand-gated ion channels from non mammalian species have provided a source for such proteins (Zemelman et al, 2002;Nagel et al, 2003;Banghart et al, 2004;Kramer et al, 2005;Boyden et al, 2005;Li et al, 2005;Herlitze and Landmesser, 2006;Parrish et al, 2006;Chambers et al, 2006). Therefore, in this study we have investigated the potential utility of heterologously expressing the invertebrate FMRFamide-gated sodium channel (FaNaC) (Lingueglia et al, 1995;Jeziorski et al, 2000;Perry et al, 2001;Furukawa et al, 2006) in mammalian neurons for their selective activation.…”

Section: Introductionmentioning

confidence: 99%

“…FaNaC was initially cloned from Helix aspersa (Lingueglia et al, 1995), but others have also been found in Helisoma trivolis, Lymnaea stagnalis, and Aplysia kurodai (Lingueglia et al, 1995;Jeziorski et al, 2000;Perry et al, 2001;Furukawa et al, 2006). FaNaCs are activated by the amidated peptide FMRFamide (Price and Greenberg, 1977) and are primarily permeated by sodium ions (Lingueglia et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

“…Importantly, when heterologously expressed in cell lines or oocytes, activation of FaNaC shows little desensitization (Lingueglia et al, 1995;Green and Cottrell, 1999;Jeziorski et al, 2000;Green and Cottrell, 2002). Of the different species, FaNaC from H. aspersa (HaFaNaC) has a higher affinity for FMRFamide, produces larger currents than FaNaC from other species (Lingueglia et al, 1995;Jeziorski et al, 2000;Perry et al, 2001;Furukawa et al, 2006). Thus, HaFaNaC may be the best candidate of the FaNaC proteins for gene targeted activation of mammalian neurons.…”

Section: Introductionmentioning

confidence: 99%

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Heterologous expression of the invertebrate FMRFamide–gated sodium channel as a mechanism to selectively activate mammalian neurons

Schanuel¹,

Bell²,

Henderson³

et al. 2008

Neuroscience

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Considerable effort has been directed toward the development of methods to selectively activate specific subtypes of neurons. Focus has been placed on the heterologous expression of proteins that are capable of exciting neurons in which they are expressed. Here we describe the heterologous expression of the invertebrate FMRFamide-gated sodium channel from Helix aspersa (HaFaNaC) in hippocampal slice cultures. HaFaNaC was co-expressed with a fluorescent protein (GFP, dsRed or tdTomato) in CA3 pyramidal neurons of rat hippocampal slice cultures using single cell electroporation. Pressure application of the agonist FMRFamide to HaFaNaC-expressing neuronal somata produced large prolonged depolarizations and bursts of action potentials (AP). FMRFamide responses were inhibited by amiloride (100 µM). In contrast, pressure application of FMRFamide to the axons of neurons expressing HaFaNaC produced no response. Fusion of GFP to the N-terminus of HaFaNaC showed that GFP-HaFaNaC was absent from axons. Bath application of FMRFamide produced persistent AP firing in HaFaNaC-expressing neurons. This FMRFamide-induced increase in the frequency of APs was dose-dependent. The concentrations of FMRFamide required to activate HaFaNaC-expressing neurons were below that required to activate the homologous acid sensing ion channel normally found in mammalian neurons. Furthermore, the mammalian neuropeptides neuropeptide FF and RFRP-1, which have amidated RF C-termini, did not affect HaFaNaCexpressing neurons. Antagonists of NPFF receptors (BIBP3226) also had no effect on HaFaNaC. Therefore, we suggest that heterologous-expression of HaFaNaC in mammalian neurons could be a useful method to selectively and persistently excite specific subtypes of neurons in intact nervous tissue.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Heterologous expression of the invertebrate FMRFamide–gated sodium channel as a mechanism to selectively activate mammalian neurons

Schanuel¹,

Bell²,

Henderson³

et al. 2008

Neuroscience

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show abstract

“…The first physiologic evidence that an ion channel can be directly activated by a neuropeptide (FMRFamide) was obtained in the snail Helix (4). This FMRFamide-activated Na + channel (FaNaC) could be blocked by amiloride and was shown to belong to the DEG/ENaC family of ion channels (5,6). Ion channels directly gated by RFamide neuropeptides were later discovered in Hydra magnipapillata, a fresh-water cnidarian (7)(8)(9)(10)(11).…”

mentioning

confidence: 99%

Dual signaling of Wamide myoinhibitory peptides through a peptide‐gated channel and a GPCR in Platynereis

et al. 2018

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Neuropeptides commonly signal by metabotropic GPCRs. In some mollusks and cnidarians, RFamide neuropeptides mediate fast ionotropic signaling by peptide-gated ion channels that belong to the DEG/ENaC family. Here we describe a neuropeptide system with a dual mode of signaling by both a peptide-gated ion channel and a GPCR. We identified and characterized a peptide-gated channel in the marine annelid Platynereis dumerilii that is specifically activated by Wamide myoinhibitory peptides derived from the same proneuropeptide. The myoinhibitory peptide-gated ion channel (MGIC) belongs to the DEG/ENaC family and is paralogous to RFamide-gated ion channels. Platynereis myoinhibitory peptides also activate a previously described GPCR, MAG. We measured the potency of all Wamides on both MGIC and MAG and identified peptides that preferentially activate one or the other receptor. Analysis of a single-cell transcriptome resource indicates that MGIC and MAG signal in distinct target neurons. The identification of a Wamide-gated ion channel suggests that peptide-gated channels are more diverse and widespread in animals than previously appreciated. The possibility of neuropeptide signaling by both ionotropic and metabotropic receptors to different target cells in the same organism highlights an additional level of complexity in peptidergic signaling networks.-Schmidt, A., Bauknecht, P., Williams, E. A., Augustinowski, K., Gründer, S., Jékely, G. Dual signaling of Wamide myoinhibitory peptides through a peptide-gated channel and a GPCR in Platynereis.

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“…The first physiological evidence that an ion channel can be directly activated by a neuropeptide (FMRFamide) was obtained in the snail Helix (4). This FMRFamide-activated Na + channel (FaNaCh) could be blocked by amiloride and was shown to belong to the DEG/ENaC family of ion channels (5,6). Ion channels directly gated by RFamide neuropeptides were later discovered in Hydra magnipapillata, a fresh-water cnidarian (7)(8)(9)(10)(11).…”

Section: Introductionmentioning

confidence: 99%

Dual signaling of Wamide myoinhibitory peptides through a peptide-gated channel and a GPCR in Platynereis

Schmidt

Bauknecht

Williams

et al. 2018

Preprint

View full text Add to dashboard Cite

Neuropeptides commonly signal by metabotropic G-protein coupled receptors (GPCRs). In some mollusks and cnidarians, RFamide neuropeptides mediate fast ionotropic signaling by peptidegated ion channels that belong to the DEG/ENaC family. Here we describe a neuropeptide system with a dual mode of signaling by both a peptide-gated channel and a GPCR. We identified and characterised a peptide-gated channel in the marine annelid Platynereis dumerilii that is specifically activated by Wamide myoinhibitory peptides derived from the same proneuropeptide. The myoinhibitory peptide-gated ion channel (MGIC) belongs to the DEG/ENaC family and is paralogous to RFamide-gated channels. Platynereis myoinhibitory peptides also activate a previously described GPCR, MAG. We measured the potency of all Wamides on both MGIC and MAG and identified peptides that preferentially activate one or the other receptor. Analysis of a single-cell transcriptome resource indicates that MGIC and MAG signal to distinct target neurons. The identification of a Wamide-gated channel suggests that peptide-gated channels are more diverse and widespread in animals than previously appreciated. The possibility of neuropeptide signaling by both ionotropic and metabotropic receptors to different target cells in the same organism highlights an additional level of complexity in peptidergic signaling networks.

show abstract

Molecular cloning and functional characterization of the Aplysia FMRFamide-gated Na+ channel

Cited by 33 publications

References 39 publications

Heterologous expression of the invertebrate FMRFamide–gated sodium channel as a mechanism to selectively activate mammalian neurons

Heterologous expression of the invertebrate FMRFamide–gated sodium channel as a mechanism to selectively activate mammalian neurons

Dual signaling of Wamide myoinhibitory peptides through a peptide‐gated channel and a GPCR in Platynereis

Dual signaling of Wamide myoinhibitory peptides through a peptide-gated channel and a GPCR in Platynereis

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