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PMID: 17579562 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

TRP channels.

Annual review of biochemistry ·Vol. 76 ·2007-00-00 ·Pages 387-417

Venkatachalam K, Montell C

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.

MeSH Terms
Amino Acid Sequence Animals Genetic Diseases, Inborn Humans Models, Molecular Molecular Sequence Data Multiprotein Complexes Phylogeny Protein Isoforms/chemistry,classification,genetics,metabolism Protein Structure, Quaternary Sensation/physiology Sequence Alignment TRPC Cation Channels/chemistry,classification,genetics,metabolism
Chemicals
Multiprotein Complexes Protein Isoforms TRPC Cation Channels
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Venkatachalam Kartik
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Montell Craig
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Article Info
Journal
Annual review of biochemistry
Abbr.
Annu Rev Biochem
ISSN
0066-4154
DOI
10.1146/annurev.biochem.75.103004.142819
Published
2007-00-00
Pages
387-417
Language
English
Region
United States
NLM ID
2985150R
PMCID
PMC4196875
Subset
IM
Grants
NEI NIH HHS · R01 EY010852 · United States
NEI NIH HHS · R01 EY010852-17 · United States
External Links
PubMed source DOI: 10.1146/annurev.biochem.75.103004.142819 PMC Full Text View journal details
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