TRPM4b channel suppresses store-operated Ca2+ entry by a novel protein-protein interaction with the TRPC3 channel

Jae Yong Park, Eun Mi Hwang, Oleg Yarishkin, Jin Ho Seo, Eunju Kim, Jiyun Yoo, Gwan Su Yi, Dong Gyu Kim, Nammi Park, Chang Man Ha, Jun ho La, Dawon Kang, Jaehee Han, Uhtaek Oh, Seong Geun Hong

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)


We identified human TRPC3 protein by yeast two-hybrid screening of a human brain cDNA library with human TRPM4b as a bait. Immunoprecipitation and confocal microscopic analyses confirmed the protein-protein interaction between TRPM4b and TRPC3, and these two TRPs were found to be highly colocalized at the plasma membrane of HEK293T cells. Overexpression of TRPM4b suppressed TRPC3-mediated whole cell currents by more than 90% compared to those in TRPC3-expressed HEK293T cells. Furthermore, HEK293T cells stably overexpressing red fluorescent protein (RFP)-TRPM4b exhibited an almost complete abolition of UTP-induced store-operated Ca2+ entry, which is known to take place via endogenous TRPC channels in HEK293T cells. This study is believed to provide the first clear evidence that TRPM4b interacts physically with TRPC3, a member of a different TRP subfamily, and regulates negatively the channel activity, in turn suppressing store-operated Ca2+ entry through the TRPC3 channel.

Original languageEnglish
Pages (from-to)677-683
Number of pages7
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - 2008 Apr 11
Externally publishedYes


  • Store-operated Ca entry
  • TRPC3
  • TRPM4b
  • Yeast two-hybrid

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'TRPM4b channel suppresses store-operated Ca<sup>2+</sup> entry by a novel protein-protein interaction with the TRPC3 channel'. Together they form a unique fingerprint.

Cite this