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Multiple Unbiased Prospective Screens Identify TRP Channels and Their Conserved Gating Elements

Benjamin R. Myers,Y. Saimi,D. Julius,C. Kung

Published 2008 in The Journal of General Physiology

ABSTRACT

It is now clear that transient receptor potential (TRP) channels are sensors of temperature, mechanical force, noxious chemicals, and G protein–coupled receptor–mediated signal transduction. Sequence and topological analyses group TRPs with other tetrameric cation channels (Yu and Catterall, 2004). Each subunit bears extensive N- and C-terminal cytoplasmic domains and an S1-S2-S3-S4-S5-P-S6 motif, where S's are segments of transmembrane α helices and P is the “pore” that houses the ion filter. Although there are no crystal structures of TRPs at this writing, they are expected to be grossly similar to those of K+ channels (Doyle et al., 1998; Long et al., 2007). Indeed, recent electron cryomicroscopy of a TRP channel (TRPV1) at 19-A resolution is consistent with a tetrameric structure having a compact transmembrane core and a large cytoplasmic domain in the form of a “hanging gondola” (Moiseenkova-Bell et al., 2008). Various aspects of TRP channel research have been reviewed elsewhere (Ramsey et al., 2006; Nilius et al., 2007; Venkatachalam and Montell, 2007). These reviews delve deeply into each of the animal TRP subtypes with regard to their expression, activation, regulation, and medical implications. Here, we intend only to complement these reviews, and in so doing we draw attention to the presence of TRPs beyond animal species, the commonalities among TRP subfamilies, the role of prospective searches in founding these subfamilies, and the continued use of prospective methods in dissecting TRP channels. We find especially striking the repeated identifications of a site at which mutations lead to constitutive channel activity in different TRP subtypes and wish to highlight these forward genetic results.

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