Tags

Type your tag names separated by a space and hit enter

Structure-functional intimacies of transient receptor potential channels.
Q Rev Biophys. 2009 Aug; 42(3):201-46.QR

Abstract

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.

Authors+Show Affiliations

Centro de Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Gran Bretaña, Valparaíso, Chile. ramon.latorre@uv.clNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

20025796

Citation

Latorre, Ramon, et al. "Structure-functional Intimacies of Transient Receptor Potential Channels." Quarterly Reviews of Biophysics, vol. 42, no. 3, 2009, pp. 201-46.
Latorre R, Zaelzer C, Brauchi S. Structure-functional intimacies of transient receptor potential channels. Q Rev Biophys. 2009;42(3):201-46.
Latorre, R., Zaelzer, C., & Brauchi, S. (2009). Structure-functional intimacies of transient receptor potential channels. Quarterly Reviews of Biophysics, 42(3), 201-46. https://doi.org/10.1017/S0033583509990072
Latorre R, Zaelzer C, Brauchi S. Structure-functional Intimacies of Transient Receptor Potential Channels. Q Rev Biophys. 2009;42(3):201-46. PubMed PMID: 20025796.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure-functional intimacies of transient receptor potential channels. AU - Latorre,Ramon, AU - Zaelzer,Cristián, AU - Brauchi,Sebastian, PY - 2009/12/23/entrez PY - 2009/12/23/pubmed PY - 2010/3/2/medline SP - 201 EP - 46 JF - Quarterly reviews of biophysics JO - Q Rev Biophys VL - 42 IS - 3 N2 - 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. SN - 1469-8994 UR - https://www.unboundmedicine.com/medline/citation/20025796/Structure_functional_intimacies_of_transient_receptor_potential_channels_ L2 - https://www.cambridge.org/core/product/identifier/S0033583509990072/type/journal_article DB - PRIME DP - Unbound Medicine ER -
Try the Free App:
Prime PubMed app for iOS iPhone iPad
Prime PubMed app for Android
Prime PubMed is provided
free to individuals by:
Unbound Medicine.