International Union of Pharmacology. XLIX. Nomenclature and Structure-Function Relationships of Transient Receptor Potential Channels

@article{Clapham2005InternationalUO,
  title={International Union of Pharmacology. XLIX. Nomenclature and Structure-Function Relationships of Transient Receptor Potential Channels},
  author={David E. Clapham and David Julius and Craig Montell and Günter Schultz},
  journal={Pharmacological Reviews},
  year={2005},
  volume={57},
  pages={427 - 450}
}
include a 25-amino acid (aa) motif in some subfamilies (the TRP domain) containing a TRP box (EWKFAR) just C-terminal to S6. The TRP domain and box, as well as slight variations of these motifs, are present in all TRPC and TRPM channel genes, but not in other TRP channels. The N-terminal cytoplasmic domains of TRPC, TRPV, and TRPA channels contain ankyrin repeats, whereas those of the TRPC and TRPM channels contain proline-rich sequences in the region just C-terminal portion of the TRP domain… Expand
Structure of the mouse TRPC4 ion channel
TLDR
An electron cryo-microscopy structure of TRPC4 in its apo state to an overall resolution of 3.3 Å reveals an unusually complex architecture with a long pore loop stabilized by a disulfide bond that provides molecular insights intoTRPC4 ion selectivity and extends the knowledge of the diversity and evolution of the TRP channels. Expand
Structure of the mouse TRPC4 ion channel
Members of the transient receptor potential (TRP) ion channels conduct cations into cells. They mediate functions ranging from neuronally-mediated hot and cold sensation to intracellular organellarExpand
Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels.
TLDR
Structural and biochemical data on the role of the ankyrin repeats in different TRPV channels are discussed and conserved structural elements unique to the ARDs of TRpV proteins are revealed. Expand
Transient Receptor Potential (TRP) Channels.
TLDR
This superfamily of channels is involved in a vast array of physiological and pathophysiological processes making the study of these channels imperative to the understanding of subcellular biochemistry. Expand
Structure of the mouse TRPC4 ion channel
TLDR
The cryo-EM structure of TRPC4 in its unliganded (apo) state is presented, which provides molecular insights intoTRPC4's ion selectivity and TPR channel evolution and extends the knowledge of the diversity and evolution of the TRP channels. Expand
Identification of Two Domains Involved in the Assembly of Transient Receptor Potential Canonical Channels*
TLDR
Overexpression in HEK293T cells of chimeras that contained an N terminus and a C terminus from different subfamily groups increased intracellular calcium entry subsequent to stimulation of Gq protein-coupled receptors, suggesting that two types of interactions are involved in the assembly of the four subunits of the TRPC channel. Expand
TRPC1 Ca(2+)-permeable channels in animal cells.
TLDR
It is concluded that TRPC1 is a most interesting protein because of the apparent wide variety of its roles and functions and the challenges posed to those attempting to elucidate its primary intracellular functions and mechanisms of action. Expand
The characterization of a novel S100A1 binding site in the N-terminus of TRPM1.
TLDR
It is shown that formation of the TRPM1/S100A1 complex is calcium-dependent and the structural model of the complex explained data obtained from fluorescence spectroscopy measurements revealing that the complex formation is facilitated through interactions of clusters positively charged and hydrophobic residues at the N-terminus of TR PM1. Expand
Classical Transient Receptor Potential 1 (TRPC1): Channel or Channel Regulator?
TLDR
This review will focus on the current status of research on TRPC1 function obtained in primary cells and aTRPC1-deficient mouse model. Expand
Glycosylation of TRPM4 and TRPM5 channels: molecular determinants and functional aspects
TLDR
Evidence is provided that TRPM4 and TRPM5 are each N-linked glycosylated at a unique residue, Asn992 and Asn932, respectively, and it is suggested thatTRPM4/5 gly cosylation seems not to be involved in channel trafficking, but mainly in their functional regulation. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 203 REFERENCES
N-Linked Protein Glycosylation Is a Major Determinant for Basal TRPC3 and TRPC6 Channel Activity*
TLDR
The glycosylation pattern plays a pivotal role for the tight regulation of TRPC6 through phospholipase C-activating receptors and shows that TRPC3 displays considerable constitutive activity, while TRPC 6 is a tightly regulated channel. Expand
Molecular and Functional Characterization of the Melastatin-related Cation Channel TRPM3*
TLDR
From its function and expression in human kidney, a role of TRPM3 is proposed in renal Ca2+ homeostasis, suggesting volume-regulated activity of TRP3. Expand
The TRP Superfamily of Cation Channels
TLDR
Members of the TRP superfamily function in various processes, although their roles are best established in sensory modalities ranging from vision to hearing, taste, pheromone detection, pain perception, and osmosensation, which have relevance for human health. Expand
The TRPC3/6/7 subfamily of cation channels.
TLDR
This review summarizes the current knowledge about the mechanism of activation of the TRPC3/6/7 subfamily, as well as the potential role of these proteins as components of native Ca2+-permeant channels. Expand
Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform
TLDR
It is revealed that TRPM4 and MLSN each mediate Ca2+ entry when expressed in HEK293 cells and it is proposed that control of translocation through interaction between MLSN-S and MLSn-L represents a mode for regulating ion channel activity. Expand
TRP channel proteins and signal transduction.
TLDR
Members of the TRP family are "special assignment" channels, which are recruited to diverse signaling pathways, although, in general, they are classified as nonselective cationic channels. Expand
TRPC1 and TRPC5 Form a Novel Cation Channel in Mammalian Brain
TLDR
It is demonstrated here that TRPC1 and TRPC5 are subunits of a heteromeric neuronal channel, and proposed that many TRPC heteromers form diverse receptor-regulated nonselective cation channels in the mammalian brain. Expand
A unified nomenclature for the superfamily of TRP cation channels.
TLDR
The current effort to unify the TRP nomenclature focuses on three subfamilies that bear significant similarities to the founding member of this superfamily, Drosophila TRP, and which include highly related members in worms, flies, mice, and humans. Expand
Expression and Characterization of Human Transient Receptor Potential Melastatin 3 (hTRPM3)*
TLDR
Results are consistent with the hypothesis that hTRPM3 mediates a Ca2- entry pathway that apparently is distinct from the endogenous Ca2+ entry pathways present in HEK 293 cells. Expand
The Membrane Topology of Human Transient Receptor Potential 3 as Inferred from Glycosylation-scanning Mutagenesis and Epitope Immunocytochemistry*
TLDR
The first hydrophobic region of Trp rather than being a transmembrane segment is intracellular and available for protein-protein interactions, suggesting that this region may have been luminal and was reinserted into the membrane at a late stage of channel assembly. Expand
...
1
2
3
4
5
...