Structure–functional intimacies of transient receptor potential channels

• Published in: Quarterly reviews of biophysics Vol. 42; no. 3; pp. 201 - 246
• Main Authors: Latorre, Ramon, Zaelzer, Cristián, Brauchi, Sebastian
• Format: Journal Article
• Language: English
• Published: New York, USA Cambridge University Press 01.08.2009
• Subjects: Amino acids; Animals; Biophysics; Humans; Models, Biological; Mutagenesis; Permeability; Proteins; TRPC Cation Channels - chemistry; TRPC Cation Channels - genetics; TRPC Cation Channels - metabolism
• ISSN: 0033-5835; 1469-8994
• DOI: 10.1017/S0033583509990072

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.