Zebrafish TRPA1 Channels Are Required for Chemosensation But Not for Thermosensation or Mechanosensory Hair Cell Function

Prober, David A.; Zimmerman, Steven; Myers, Benjamin R.; McDermott, Brian M.; Kim, Seok Hyung; Caron, Sophie; Rihel, Jason; Solnica‐Krezel, Lilianna; Julius, David; Hudspeth, A. J.; Schier, Alexander F.

doi:10.1523/jneurosci.2740-08.2008

Cited by 156 publications

(171 citation statements)

References 77 publications

(127 reference statements)

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“…S1 A and B). These findings are in agreement with previous reports regarding the effect of mustard oil on zebrafish larvae (16,17). In contrast to WT larvae, mutants failed to move in response to mustard oil (Fig.…”

Section: Resultssupporting

confidence: 93%

RING finger protein 121 facilitates the degradation and membrane localization of voltage-gated sodium channels

Ogino

Low

Yamada

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Following their synthesis in the endoplasmic reticulum (ER), voltagegated sodium channels (Na V ) are transported to the membranes of excitable cells, where they often cluster, such as at the axon initial segment of neurons. Although the mechanisms by which Na V channels form and maintain clusters have been extensively examined, the processes that govern their transport and degradation have received less attention. Our entry into the study of these processes began with the isolation of a new allele of the zebrafish mutant alligator, which we found to be caused by mutations in the gene encoding really interesting new gene (RING) finger protein 121 (RNF121), an E3-ubiquitin ligase present in the ER and cis-Golgi compartments. Here we demonstrate that RNF121 facilitates two opposing fates of Na V channels: (i) ubiquitin-mediated proteasome degradation and (ii) membrane localization when coexpressed with auxiliary Na V β subunits. Collectively, these results indicate that RNF121 participates in the quality control of Na V channels during their synthesis and subsequent transport to the membrane.oltage-gated sodium channels (Na V ) are large (∼230 kDa) multipass transmembrane proteins (1). The Na V channel family is comprised of nine members (Na V 1.1-Na V 1.9), whose activity typically underlies the rising phase of action potentials in excitable cells. In excitable cells, Na V channels form complexes with auxiliary β subunits (Na V β 1-4 ) in the Golgi apparatus (2), a process that enhances the kinetics and membrane localization of Na V channels (3, 4). In addition to these roles, several Na V β subunits also function as cell adhesion molecules independent of Na V channels (5). At the axon initial segment (AIS) and nodes of Ranvier of neurons, Na V channels form clusters that facilitate the generation and propagation of action potentials. Although the molecular basis of Na V clustering at these sites has been extensively studied (6), the transport of Na V channels to these sites has been less explored. For instance, to date, only the annexin II light chain (p11) has been shown to associate with and facilitate the transport of Na V 1.8 to the plasma membrane (7). Furthermore, subsequent efforts revealed that p11 acts only on Na V 1.8 (8). Thus, the transport of other Na V channels remains unclear.In zebrafish, several studies have explored the contribution of Na V channels and their auxiliary Na V β subunits through the use of forward and reverse genetics. In brief, impairments in Na V 1.1, Na V 1.6a, and Na V β 1b have been shown to diminish touch-evoked escape responses and Na V channel activity in Rohon-Beard (RB) sensory neurons (9-11). In addition, two other mutants identified in forward genetic screens have been shown to affect Na V channel activity indirectly. The first, pigu, arises from a mutation in a GPItransamidase necessary for the proper localization of Na V channels (12). Although the genetic locus of the second mutation, macho (13,14), has yet to be identified, rough mapping indicates that it lies with...

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Section: Resultssupporting

confidence: 93%

RING finger protein 121 facilitates the degradation and membrane localization of voltage-gated sodium channels

Ogino

Low

Yamada

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…The two zebrafish TRPA1 paralogs (trpa 1a and trpa 1b) are expressed in sensory neurons of zebrafish larvae. TRPA1b is necessary for behavioral responses (increase of locomotor activity) to chemical irritants [43]. In the present experiment, allyl isothiocyanate and high concentrations of menthol induced rapid movement not only in zebrafish but also in medaka and goldfish, suggesting that fishes have cold nociception via TRPA1 receptors.…”

Section: Discussionsupporting

confidence: 48%

Menthol Induces Surgical Anesthesia and Rapid Movement in Fishes

Kasai¹,

Hososhima²,

Yun-Fei³

2014

TONEURJ

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Abstract:To determine whether fishes respond to menthol, Japanese medaka Oryzias latipes, goldfish Carassius auratus, and zebrafish Danio rerio were exposed to various types of menthol receptors agonists and the behavioral responses to these drugs were observed. Waterbone application of dl-menthol (0.5 mM) induced surgical anesthesia in 100% of medaka, 90% of goldfish, and 100% of zebrafish. The percentage of response increased dose-dependently from 0.2 mM to 0.5 mM. There were no differences in either percentage or latency of the response in surgical anesthesia among dl-, d-, and l-types of menthol. A high (3.0 mM) concentration of any of the three types of menthol induced rapid movement followed by the anesthetic response. Rapid movement was observed with allyl isothiocyanate, a cold nociceptor agonist, but not with icilin, a cold receptor agonist, in medaka and goldfish. Both allyl isothiocyanate and icilin failed to induce surgical anesthesia. To determine the involvement of -aminobutyric acid (GABA) system in menthol-induced surgical anesthesia, the effect of the receptors antagonist for the GABA A was tested. Pretreatment with a specific GABA A receptor antagonist prolonged the latency of the anesthetic response to menthol, but not to cold-water stimulation, in medaka and goldfish. These results demonstrate that menthol can play a role in the induction of surgical anesthesia in fishes, related at least in part to the activation of GABA A receptors, and of rapid movement possibly via cold nociceptors.

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“…To record microphonic potentials, a recording micropipette was inserted into the otic vesicle (OV) (Corey et al, 2004;Obholzer et al, 2008;Prober et al, 2008). To apply imperative mechanical stimulation to the macular HCs, a piezoelectric probe or micropipette filled with extracellular solution was positioned adjacent to the otoliths.…”

Section: Methodsmentioning

confidence: 99%

Auditory Input to CNS Is Acquired Coincidentally with Development of Inner Ear after Formation of Functional Afferent Pathway in Zebrafish

Tanimoto¹,

Ota²,

Horikawa³

et al. 2009

J. Neurosci.

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Zebrafish TRPA1 Channels Are Required for Chemosensation But Not for Thermosensation or Mechanosensory Hair Cell Function

Cited by 156 publications

References 77 publications

RING finger protein 121 facilitates the degradation and membrane localization of voltage-gated sodium channels

RING finger protein 121 facilitates the degradation and membrane localization of voltage-gated sodium channels

Menthol Induces Surgical Anesthesia and Rapid Movement in Fishes

Auditory Input to CNS Is Acquired Coincidentally with Development of Inner Ear after Formation of Functional Afferent Pathway in Zebrafish

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