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Murakami, M. et al.

Murakami, Xu, Miyoshi, Sato, Ono, Iijima,

Identification and characterization of the murine TRPM4 channel.

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.[1]

References

Identification and characterization of the murine TRPM4 channel. Murakami, M., Xu, F., Miyoshi, I., Sato, E., Ono, K., Iijima, T. Biochem. Biophys. Res. Commun. (2003) [Pubmed]

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