Identification and characterization of the murine TRPM4 channel

Manabu Murakami, Feng Xu, Ichiro Miyoshi, Eisaku Sato, Kyoichi Ono, Toshihiko Iijima

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)


The transient receptor potential (TRP) channels form a superfamily with six transmembrane structures, which is common in other types of voltage-dependent channels. The TRP-melastatin (TRPM) subfamily includes the putative tumor-suppressor melastatin, which was originally found as a down-regulated protein in melanoma tumor cell lines. Here, we report a novel TRP-related protein that is a murine orthologue of human TRPM4. The function of the novel murine TRPM4 was studied in HEK-293 cells using a fluorescent calcium indicator, fura-2. The removal and re-introduction of extracellular calcium triggered changes in the intracellular calcium only in cells expressing TRPM4a, which suggests that this novel channel plays a role in the calcium entry process. We also isolated a splice variant of TRPM4 that was proven to be non-functional. Both TRPM4 variants integrated into the plasma membrane. Furthermore, FRET analysis revealed that TRPM4a and TRPM4b localized close together, suggesting a multimerization of the two molecules.

Original languageEnglish
Pages (from-to)522-528
Number of pages7
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - 2003 Aug 1


  • Calcium entry
  • Gene structure
  • Melastatin
  • Transient receptor potential
  • cDNA

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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