Structure–functional intimacies of transient receptor potential channels

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....

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Published inQuarterly reviews of biophysics Vol. 42; no. 3; pp. 201 - 246
Main Authors Latorre, Ramon, Zaelzer, Cristián, Brauchi, Sebastian
Format Journal Article
LanguageEnglish
Published New York, USA Cambridge University Press 01.08.2009
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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.
AbstractList 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. [PUBLICATION 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.
Author Zaelzer, Cristián
Latorre, Ramon
Brauchi, Sebastian
Author_xml – sequence: 1
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  surname: Latorre
  fullname: Latorre, Ramon
  email: ramon.latorre@uv.cl
  organization: 1Centro de Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Gran Bretaña, Valparaíso, Chile
– sequence: 2
  givenname: Cristián
  surname: Zaelzer
  fullname: Zaelzer, Cristián
  organization: 1Centro de Interdisciplinario de Neurociencias de Valparaíso, Facultad de Ciencias, Universidad de Valparaíso, Gran Bretaña, Valparaíso, Chile
– sequence: 3
  givenname: Sebastian
  surname: Brauchi
  fullname: Brauchi, Sebastian
  organization: 3Instituto de Fisiología, Facultad de Medicina, Universidad Austral de Chile, Campus Isla Teja, Valdivia, Chile
BackLink https://www.ncbi.nlm.nih.gov/pubmed/20025796$$D View this record in MEDLINE/PubMed
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R. Latorre, C. Zaelzer and S. Brauchi
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Snippet Although a unifying characteristic common to all transient receptor potential (TRP) channel functions remains elusive, they could be described as tetramers...
Abstract Although a unifying characteristic common to all transient receptor potential (TRP) channel functions remains elusive, they could be described as...
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SubjectTerms Amino acids
Animals
Biophysics
Humans
Models, Biological
Mutagenesis
Permeability
Proteins
TRPC Cation Channels - chemistry
TRPC Cation Channels - genetics
TRPC Cation Channels - metabolism
Title Structure–functional intimacies of transient receptor potential channels
URI https://www.cambridge.org/core/product/identifier/S0033583509990072/type/journal_article
https://api.istex.fr/ark:/67375/6GQ-HPQCWRM3-K/fulltext.pdf
https://www.ncbi.nlm.nih.gov/pubmed/20025796
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Volume 42
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