Title | TRP channels |
Publication Type | Journal Article |
Year of Publication | 2007 |
Authors | Venkatachalam K, Montell C |
Journal | Annu Rev Biochem |
Volume | 76 |
Pagination | 387-417 |
Date Published | 2007 |
ISSN | 0066-4154 |
Keywords | Amino Acid Sequence, Animals, Genetic Diseases, Inborn, Humans, Models, Molecular, Molecular Sequence Data, Multiprotein Complexes, Phylogeny, Protein Isoforms, Protein Structure, Quaternary, Sensation, Sequence Alignment, TRPC Cation Channels |
Abstract | The TRP (Transient Receptor Potential) superfamily of cation channels is remarkable in that it displays greater diversity in activation mechanisms and selectivities than any other group of ion channels. The domain organizations of some TRP proteins are also unusual, as they consist of linked channel and enzyme domains. A unifying theme in this group is that TRP proteins play critical roles in sensory physiology, which include contributions to vision, taste, olfaction, hearing, touch, and thermo- and osmosensation. In addition, TRP channels enable individual cells to sense changes in their local environment. Many TRP channels are activated by a variety of different stimuli and function as signal integrators. The TRP superfamily is divided into seven subfamilies: the five group 1 TRPs (TRPC, TRPV, TRPM, TRPN, and TRPA) and two group 2 subfamilies (TRPP and TRPML). TRP channels are important for human health as mutations in at least four TRP channels underlie disease. |
DOI | 10.1146/annurev.biochem.75.103004.142819 |
Alternate Journal | Annu. Rev. Biochem. |
PubMed ID | 17579562 |
Grant List | R01 EY010852-17 / EY / NEI NIH HHS / United States |