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Sci. STKE, 22 February 2005
Vol. 2005, Issue 272, p. re3
[DOI: 10.1126/stke.2722005re3]

REVIEWS

The TRP Superfamily of Cation Channels

Craig Montell*

Department of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.

Gloss: The Drosophila transient receptor potential (trp) locus was discovered about 35 years ago on the basis of its critical role in visual transduction. For many years, the molecular identity and function of the TRP protein were enigmatic. However, we now know that TRP is the defining member of large superfamily of Ca2+-permeable cation channels that are conserved from worms to humans. Members of the TRP superfamily function in various processes, although their roles are best established in sensory modalities ranging from vision to hearing, taste, pheromone detection, pain perception, and osmosensation. The mechanisms underlying the activation of these cation channels are diverse. Some are receptor-operated channels, whereas others appear to be gated by changes in osmolarity, pH, or temperature. Investigations into the functions and modes of activation of TRP-related proteins have relevance for human health, because mutations in at least three members of the TRP superfamily are responsible for human diseases. This STKE Review includes 4 figures, 5 tables, and 324 citations.

* To whom correspondence should be addressed. E-mail: cmontell{at}jhmi.edu

Citation: C. Montell, The TRP Superfamily of Cation Channels. Sci. STKE 2005, re3 (2005).

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