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

  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},
  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… 

Structure of the mouse TRPC 4 ion channel 1 2

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 knowledge of the diversity and evolution of the TRP channels.

Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels.

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.

Structure of the mouse TRPC4 ion channel

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.

Identification of Two Domains Involved in the Assembly of Transient Receptor Potential Canonical Channels*

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.

TRPC1 Ca(2+)-permeable channels in animal cells.

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.

The characterization of a novel S100A1 binding site in the N-terminus of TRPM1.

Classical Transient Receptor Potential 1 (TRPC1): Channel or Channel Regulator?

This review will focus on the current status of research on TRPC1 function obtained in primary cells and aTRPC1-deficient mouse model.

Glycosylation of TRPM4 and TRPM5 channels: molecular determinants and functional aspects

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.

The versatile nature of the calcium‐permeable cation channel TRPP2

This review summarizes the most pertinent evidence about the properties of TR PP2 channels, focusing on the compartment‐specific functions of mammalian TRPP2.

TRP Channels: Their Function and Potentiality as Drug Targets

The molecular pharmacology of TRP modulators is described and their modulatory mechanisms and pharmacological actions are discussed and proposed that this subtype selectivity is conferred through synergistic effects of electrophilic cysteine transnitrosylation and molecular recognition of the non-electrophilic moiety on the N-nitrosamine.



N-Linked Protein Glycosylation Is a Major Determinant for Basal TRPC3 and TRPC6 Channel Activity*

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.

Molecular and Functional Characterization of the Melastatin-related Cation Channel TRPM3*

From its function and expression in human kidney, a role of TRPM3 is proposed in renal Ca2+ homeostasis, suggesting volume-regulated activity of TRP3.

The TRP Superfamily of Cation Channels

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.

The TRPC3/6/7 subfamily of cation channels.

Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform

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.

TRP channel proteins and signal transduction.

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.

A unified nomenclature for the superfamily of TRP cation channels.

Expression and Characterization of Human Transient Receptor Potential Melastatin 3 (hTRPM3)*

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.

The Membrane Topology of Human Transient Receptor Potential 3 as Inferred from Glycosylation-scanning Mutagenesis and Epitope Immunocytochemistry*

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.