Abstract
The transient receptor potential vanilloid family includes four ion channels–TRPV1, TRPV2, TRPV3 and TRPV4–that are represented within the vertebrate subphylum and involved in several sensory and physiological processes. These channels are related to adaptation to the environment, and probably under strong evolutionary pressure. Using multiple sequence alignments as source for evolutionary, bioinformatics and statistical analysis, we have analyzed the evolutionary profiles for TRPV1, TRPV2, TRPV3 and TRPV4. The evolutionary pressure exerted over vertebrate TRPV2 sequences compared to the other channels argues for a positive selection profile for TRPV2 compared to TRPV1, TRPV3 and TRPV4. We have analyzed the selective pressure on specific protein domains, observing a common selective pressure trend for the common TRPV scaffold, consisting of the ankyrin repeat domain, the membrane proximal domain, the transmembrane domain, and the TRP domain. Through a more detailed analysis we have identified evolutionary constraints involved in the subunit contact at the transmembrane domain level. Performing evolutionary comparison, we have translated specific channel structural information such as the transmembrane topology, and the interaction between the membrane proximal domain and the TRP box. We have also identified potential common regulatory domains among all TRPV1-4 members, such as protein-protein, lipid-protein and vesicle trafficking domains.
Highlights
TRP channel superfamily consists of a set polymodal nonselective oligomeric membrane cationic channels, with large cytoplasmic regulatory domains [1,2]
This hypothesis fits with the chromosome location of TRPV1, TRPV2 and TRPV3 in human (Chr17) and mouse (Chr11) for example, that indicates that a TRPV gene duplicated first originating TRPV2, and a more recent gene duplication generated the ancestor of TRPV1 and TRPV3 genes [29]
Concerning TRPV1-4, we find that TRPV2 is under positive selection
Summary
TRP channel superfamily consists of a set polymodal nonselective oligomeric membrane cationic channels, with large cytoplasmic regulatory domains [1,2] These channels are predicted to share a common tetrameric membrane topology around the formation of a pore in the membrane to allow the flux of cations, but there are several differential regulatory domains that allow/block the cation flux through the membrane [2]. These domains are very specialized, and follow an evolutionary pattern that has been reflected in the subfamily classification of the large TRP superfamily. Another classification identifies the TRPV1-4 subgroup as thermosensors in mammals: TRPV1 and TRPV2 act as noxious heat sensors (T.43uC), and TRPV3 and TRPV4 as physiological temperature sensors
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