A Unified Nomenclature for the Superfamily of TRP Cation Channels

Montell, Craig; Birnbaumer, Lutz; Flockerzi, Veit; Bindels, René J. M.; Bruford, Elspeth A.; Caterina, Michael J.; Clapham, David E.; Harteneck, Christian; Heller, Stefan; Julius, David; Kojima, Itaru; Mori, Yasuo; Penner, Reinhold; Prawitt, Dirk; Scharenberg, Andrew M.; Schultz, Günter; Shimizu, Nobuyoshi; Zhu, Michael X.

doi:10.1016/s1097-2765(02)00448-3

Cited by 609 publications

(381 citation statements)

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“…This behavior is carried out by 87 neurons exclusive to the male; 42 of these neurons are ciliated neurons in the tail and many of these may be mechanoreceptors [79]. Two TRPP proteins, the polycystinlike proteins LOV-1 and PKD-2, are expressed in a subset of these neurons and required for male mating response and vulva location [4,5,54]. The human polycystins, PC-1 and PC-2, the respective homologs of C. elegans LOV-1 and PKD-2, are defective in inherited polycystic kidney disease [41]; they localize to primary cilium of kidney epithelial cells and sense fluid sheer stress, presumably as a heteromeric channel complex [55].…”

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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“…TRPV5 and TRPV6 constitute a distinct class of highly Ca 2+ -selective channels within the transient receptor potential (TRP) superfamily, which encompasses a diversity of non-voltage operated cation channels (Clapham et al 2001;Harteneck et al 2000;Montell et al 2002b). These two channels belong to the TRPV (vanilloid) subfamily, which is one of the subfamilies comprising this su-perfamily (Hoenderop et al 2005;Montell et al 2002a;Peng et al 2003;Vennekens et al 2002).…”

Section: Molecular Features Of Trpv5 and Trpv6mentioning

confidence: 99%

“…Regulation of TRPV5 and TRPV6 activity TRPV5 and TRPV6 are constitutively active, unlike many other TRP channels that are activated by binding of ligands (Montell et al 2002b). This implies that in order to regulate TRPV5/6 activity, short-term acting mechanisms must exist that control the activity of these channels located on the plasma membrane.…”

Section: Ankyrin Repeatsmentioning

confidence: 99%

“…1), consisting of passive entry of Ca 2+ across the luminal or apical membrane, cytosolic diffusion of Ca 2+ bound to vitamin D 3 -sensitive Ca 2+ -binding proteins (calbindin-D 28K and/or calbindin-D 9K ) and active extrusion of Ca 2+ across the opposite basolateral membrane by the Na + -Ca 2+ -exchanger (NCX1) and/ or Ca 2+ -ATPase (PMCA1b; Bronner 2003;Hoenderop et al 2002b). The molecular identity of the apical Ca 2+ entry pathway remained elusive until the epithelial Ca 2+ channels TRPV5 (previously named ECaC1; Hoenderop et al 1999) and TRPV6 (previously named Ca 2+ transporter 1) were identified (Montell et al 2002b;Peng et al 1999). These channels convey the rate-limiting step in active Ca 2+ transport and play, therefore, a pivotal role in Ca 2+ homeostasis.…”

Section: Introductionmentioning

confidence: 99%

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The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease

Abel

Hoenderop

Bindels

2005

Naunyn-Schmiedeberg's Arch Pharmacol

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The epithelial Ca 2+ channels TRPV5 and TRPV6 represent a new family of Ca 2+ channels that belongs to the superfamily of transient receptor potential channels. TRPV5 and TRPV6 constitute the apical Ca 2+ entry mechanism in active Ca 2+ transport in kidney and intestine. The central role of TRPV5 and TRPV6 in active Ca 2+ (re)absorption makes it a prime target for regulation to maintain Ca 2+ balance. This review covers the hormonal regulation, interaction with accessory proteins and (patho)physiological implications of these epithelial Ca 2+ channels.

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“…They are further divided into TRPC (Canonical), TRPV (Vanilloid), TRPM (Melastatin), TRPA (ANKTM1), TRPP (Polycystin), and TRPML (MucoLipin) subfamilies [1]. Based on their temperature responsiveness, TRPA1, TRPM8, TRPV1, TRPV2, TRPV3, and TRPV4 are also classified as thermal sensitive channels.…”

Section: Introductionmentioning

confidence: 99%

The TRPV3 mutation associated with the hairless phenotype in rodents is constitutively active

Xiao¹,

Tian²,

Tang³

et al. 2008

Cell Calcium

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SummaryTRPV3 is a non-selective cation channel activated by warm to hot temperatures. In rodents, TRPV3 is highly expressed in basal keratinocytes of skin and oral/nasal epithelia. TRPV3 knockout mice showed impaired responses to innocuous and noxious heat but otherwise normal appearance and reactions to many sensory modalities. However, point mutations of TRPV3 at Gly573 to Ser and Cys have recently been linked to autosomal dominant hairless phenotypes and spontaneous dermatitis in mice and rats, implicating an important role for TRPV3 in alopecia and skin diseases. Exactly how the mutations affect TRPV3 function was unexplained. Here we show that both G573S and G573C mutations of murine TRPV3 are constitutively active in heterologous systems. In HEK293 cells, expression of the TRPV3 mutants causes cell death. In Xenopus oocytes, the constitutively active mutant channel is irresponsive to thermal and chemical stimuli but it reduces the temperature threshold and enhances the responses to heat and TRPV3 agonists of the wild type channel when they are co-expressed. We conclude that the G573S and G573C substitutions render the TRPV3 channel spontaneously active under normal physiological conditions, which in turn alters ion homeostasis and membrane potentials of skin keratinocytes, leading to hair loss and dermatitis-like skin diseases.

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A Unified Nomenclature for the Superfamily of TRP Cation Channels

Cited by 609 publications

References 0 publications

Touch sensitivity in Caenorhabditis elegans

Touch sensitivity in Caenorhabditis elegans

The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease

The TRPV3 mutation associated with the hairless phenotype in rodents is constitutively active

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