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Sci. STKE, 10 July 2001
Vol. 2001, Issue 90, p. re1
[DOI: 10.1126/stke.2001.90.re1]

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Physiology, Phylogeny, and Functions of the TRP Superfamily of Cation Channels

Craig Montell

The author is in the Department of Biological Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA. E-mail: cmontell@jhmi.edu

Gloss: The Drosophila transient receptor potential (trp) locus was discovered more than 30 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, recent studies indicate 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 a variety of critical processes such as phototransduction, mechanotransduction, pain perception, osmosensation, and vasorelaxation. In addition, the mechanisms underlying the activation of these cation channels are diverse. Some appear to be receptor-operated channels, whereas others appear to be gated by changes in osmolarity, pH, or temperature. Lastly, investigations into the functions and modes of activation of TRP-related proteins have relevance for human health, because mutations in at least two members of the TRP superfamily are responsible for human diseases.

Citation: C. Montell, Physiology, Phylogeny, and Functions of the TRP Superfamily of Cation Channels. Sci. STKE 2001, re1 (2001).


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