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Related Concept Videos

Thermosensation01:43

Thermosensation

Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...
Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
LTR Retrotransposons03:08

LTR Retrotransposons

LTR retrotransposons are class I transposable elements with long terminal repeats flanking an internal coding region. These elements are less abundant in mammals compared to other class I transposable elements. About 8 percent of human genomic DNA comprises LTR retrotransposons. Some of the common examples of LTR retrotransposons are Ty elements in yeast and Copia elements in Drosophila.
The internal coding region of LTR retrotransposons and their mechanism of transposition closely resembles a...

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Articles linked to this work by shared authors, journal, and citation graph.

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Structural requirements of steroidal agonists of transient receptor potential melastatin 3 (TRPM3) cation channels.

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Citrus fruit and fabacea secondary metabolites potently and selectively block TRPM3.

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TRPM3, a biophysical enigma?

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Related Experiment Video

Updated: Jul 17, 2026

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice
08:35

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice

Published on: March 17, 2015

TRPM3.

J Oberwinkler1, S E Phillipp

  • 1Institut für klinische und experimentelle Pharmakologie und Toxikologie der Universität des Saarlandes, 66421 Homburg, Germany. johannes.oberwinkler@uniklinikum-saarland.de

Handbook of Experimental Pharmacology
|January 16, 2007
PubMed
Summary

Transient Receptor Potential Melastatin 3 (TRPM3) exhibits numerous variants due to alternative splicing. This review overviews TRPM3 variants and their distinct functional properties, particularly concerning ion selectivity.

Area of Science:

  • Molecular biology
  • Ion channel research
  • Genetics

Background:

  • Transient Receptor Potential Melastatin 3 (TRPM3) is the latest identified member of the TRPM channel subfamily.
  • TRPM3 is closely related to TRPM1.
  • Alternative splicing of the TRPM3 gene leads to a diverse array of channel variants.

Purpose of the Study:

  • To provide a comprehensive overview of the known TRPM3 variants.
  • To compare the functional properties of different TRPM3 splice variants.
  • To highlight how alternative splicing impacts TRPM3 channel function, especially ion selectivity.

Main Methods:

  • Literature review of studies on TRPM3 variants.
  • Comparative analysis of reported functional data for TRPM3 channels.

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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

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  • Examination of splice variants affecting the pore-forming region.
  • Main Results:

    • The TRPM3 gene generates a significant number of splice variants.
    • A specific splice event in the pore-forming region alters divalent cation selectivity.
    • Functional properties vary considerably among identified TRPM3 variants.

    Conclusions:

    • Alternative splicing is a key mechanism generating functional diversity in TRPM3 channels.
    • Understanding TRPM3 variants is crucial for elucidating their physiological roles.
    • The differential ion selectivity of TRPM3 variants suggests specialized functions.