NompC TRP Channel Required for Vertebrate Sensory Hair Cell Mechanotransduction

Sidi, Samuel; Friedrich, Rainer W.; Nicolson, Teresa

doi:10.1126/science.1084370

Cited by 288 publications

(184 citation statements)

References 20 publications

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“…These neurons express the TRPN channel TRP-4 [48]. The trp-4 gene is an ortholog of the fruitfly and zebrafish nompC genes [74,88]. Because trp-4 mutants do not slow on entering a bacterial lawn [48], TRP-4 may have a role in transducing textural stimuli.…”

Section: Other Mechanosensory Behaviorsmentioning

confidence: 99%

Touch sensitivity in Caenorhabditis elegans

Bounoutas

Chalfie

2007

Pflugers Arch - Eur J Physiol

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The nematode Caenorhabditis elegans was the first organism for which touch insensitive mutants were obtained. The study of the genes defective in these mutants has led to the identification of components of a mechanosensory complex needed for specific cells to sense gentle touch to the body. Multiple approaches using genetics, cell biology, biochemistry, and electrophysiology have characterized a channel complex, containing two DEG/ENaC pore-forming subunits and several other proteins, that transduces the touch response. Other mechanical responses, sensed by other cells using a variety of other components, are less well understood in C. elegans. Many of these other senses may use TRP channels, although DEG/ENaC channels have also been implicated.

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Section: Other Mechanosensory Behaviorsmentioning

confidence: 99%

Touch sensitivity in Caenorhabditis elegans

Bounoutas

Chalfie

2007

Pflugers Arch - Eur J Physiol

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“…TRPA1 channels were initially thought to be the holy grail of auditory transduction channels in mammals (Corey et al 2004), as another member of this superfamily, TRPN1, had been discovered previously in the hair cells of zebrafish (Sidi et al 2003). More recent studies in mammals reported contradictory evidence for TRPA1 (Bautista et al 2006), although a candidate may still be found among this superfamily (see Cuajungco et al 2007 for review).…”

Section: Trp Channelsmentioning

confidence: 99%

Ion Channel Gene Expression in the Inner Ear

Gabashvili

Sokolowski

Morton

et al. 2007

JARO

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The ion channel genome is still being defined despite numerous publications on the subject. The ion channel transcriptome is even more difficult to assess. Using high-throughput computational tools, we surveyed all available inner ear cDNA libraries to identify genes coding for ion channels. We mapped over 100,000 expressed sequence tags (ESTs) derived from human cochlea, mouse organ of Corti, mouse and zebrafish inner ear, and rat vestibular end organs to Homo sapiens, Mus musculus, Danio rerio, and Rattus norvegicus genomes. A survey of EST data alone reveals that at least a third of the ion channel genome is expressed in the inner ear, with highest expression occurring in hair cell-enriched mouse organ of Corti and rat vestibule. Our data and comparisons with other experimental techniques that measure gene expression show that every method has its limitations and does not per se provide a complete coverage of the inner ear ion channelome. In addition, the data show that most genes produce alternative transcripts with the same spectrum across multiple organisms, no ion channel gene variants are unique to the inner ear, and many splice variants have yet to be annotated. Our high-throughput approach offers a qualitative computational and experimental analysis of ion channel genes in inner ear cDNA collections. A lack of data and incomplete gene annotations prevent both rigorous statistical analyses and comparisons of entire ion channelomes derived from different tissues and organisms.

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“…16 Furthermore, C. elegans TRPN1 and Drosophila NOMPC are both found in mechanosensory organs, 16 and TRPN1 is a critical component in hearing and mechanosensation in zebrafish. 28 TRPN proteins all have 29 ankyrin repeat motifs, and the predicted elongated coil shape of their ankyrin repeat domain led to the hypothesis that it acts as a spring that directly senses mechanical stimuli. 29 But mice and humans do not have any TRPN-subfamily channel, and the identity of the mammalian mechanosensitive channel involved in hearing remains unknown.…”

Section: Ankyrin Repeats As Springs?mentioning

confidence: 99%

A primer on ankyrin repeat function in TRP channels and beyond

2008

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Transient Receptor Potential (TRP) channels are rapidly gaining attention as important receptors and transducers of diverse sensory and environmental cues. Recent progress in the field has provided new insights into the structure and function of the ankyrin repeat motifs present in the Nterminal cytosolic domain of many TRP channels. The topics addressed in this review include the structural features of canonical ankyrin repeats, new clues into the functions these repeats perform in cells, and how this information can be applied to develop further experiments on TRP channels and other proteins containing ankyrin repeats.TRP proteins form a large family of ion channels particularly important in animals from worms to man, with more than 30 members in mammals. 1 The founding family member, the Drosophila trp gene -named for the "transient receptor potential" phenotype its mutation causes in light perception by photoreceptors -was first cloned in 1989. 2 The functions assigned to TRP channels in physiology are constantly expanding. They are key transducers of sensory signals, and are generally important in sensing information about the environment in both neuronal and non-neuronal cells (see ref. 3 for comprehensive reviews). Some TRP channels are found in excitable cells of the sensory nervous system, while others are expressed in various other tissues and organs. TRP channels have been implicated in many physiological processes, including calcium and magnesium homeostasis, neuronal growth, temperature sensation and pain perception, to name a few. For example, TRPV1 senses painfully hot temperatures, low extracellular pH and the capsaicin of "hot" chili peppers, while TRPA1 senses many painful chemical stimuli, including the pungent compounds in wasabi and cinnamon. TRPV1 and TRPA1 are expressed in partially overlapping sets of nociceptor neurons that transmit pain signals to the brain.At a molecular level, TRP channels assemble as tetramers through a channel domain that spans the membrane six times and has sequence similarity to voltage-gated ion channels. TRP channels also have large N-and C-terminal cytosolic domains that flank the transmembrane channel domain. These cytosolic domains participate in channel gating and regulation and sense information about the cellular state -ion and metabolite levels, for example. The TRP channel family is divided into seven subfamilies based on sequence similarity 1 : TRPA (ankyrin), TRPC (canonical), TRPM (melastatin), TRPML (mucolipin), TRPP (polycystin), TRPV (vanilloid), and TRPN (NOMPC). Several of these subfamilies -TRPA, TRPC, TRPN and TRPV -have ankyrin repeat sequence motifs in their N-terminal cytosolic domains. Recent work from my lab and others has taken a structural biology approach to elucidate the roles of these ankyrin repeats in TRP channel function. [4][5][6][7][8][9] The emerging structural and functional features of these TRP channel ankyrin repeats are the focus of this short review. NIH Public Access Ankyrin repeats and their structureAnkyrin rep...

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NompC TRP Channel Required for Vertebrate Sensory Hair Cell Mechanotransduction

Cited by 288 publications

References 20 publications

Touch sensitivity in Caenorhabditis elegans

Touch sensitivity in Caenorhabditis elegans

Ion Channel Gene Expression in the Inner Ear

A primer on ankyrin repeat function in TRP channels and beyond

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