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Structure–functional intimacies of transient receptor potential channels

Published online by Cambridge University Press:  22 December 2009

Ramon Latorre ,
Cristián Zaelzer  and
Sebastian Brauchi
Ramon Latorre*
Affiliation:
Centro de Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Gran Bretaña, Valparaíso, Chile
Cristián Zaelzer
Affiliation:
Centro de Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Gran Bretaña, Valparaíso, Chile Escuela de Graduados, Facultad de Ciencias, Universidad Austral de Chile, Valdivia, Chile
Sebastian Brauchi
Affiliation:
Instituto de Fisiología, Facultad de Medicina, Universidad Austral de Chile, Campus Isla Teja, Valdivia, Chile
*
*Author for correspondence: R. Latorre, Centro de Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Gran Bretaña 1111, Valparaíso 2340000, Chile. Email: [email protected]
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Abstract

Although a unifying characteristic common to all transient receptor potential (TRP) channel functions remains elusive, they could be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. TRP channels constitute a large superfamily of ion channels, and can be grouped into seven subfamilies based on their amino acid sequence homology: the canonical or classic TRPs, the vanilloid receptor TRPs, the melastatin or long TRPs, ankyrin (whose only member is the transmembrane protein 1 [TRPA1]), TRPN after the nonmechanoreceptor potential C (nonpC), and the more distant cousins, the polycystins and mucolipins. Because of their role as cellular sensors, polymodal activation and gating properties, many TRP channels are activated by a variety of different stimuli and function as signal integrators. Thus, how TRP channels function and how function relates to given structural determinants contained in the channel-forming protein has attracted the attention of biophysicists as well as molecular and cell biologists. The main purpose of this review is to summarize our present knowledge on the structure of channels of the TRP ion channel family. In the absence of crystal structure information for a complete TRP channel, we will describe important protein domains present in TRP channels, structure–function mutagenesis studies, the few crystal structures available for some TRP channel modules, and the recent determination of some TRP channel structures using electron microscopy.

Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 42 , Issue 3 , August 2009 , pp. 201 - 246
Copyright
Copyright © Cambridge University Press 2009

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