CLIC4 interacts with histamine H3 receptor and enhances the receptor cell surface expression

Kay Maeda, Mitsuya Haraguchi, Atsuo Kuramasu, Takeya Sato, Kyohei Ariake, Hiroyuki Sakagami, Hisatake Kondo, Kazuhiko Yanai, Kohji Fukunaga, Teruyuki Yanagisawa, Jun Sukegawa

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17 Citations (Scopus)


Histamine H3 receptor (H3R), one of G protein-coupled receptors (GPCRs), has been known to regulate neurotransmitter release negatively in central and peripheral nervous systems. Recently, a variety of intracellular proteins have been identified to interact with carboxy (C)-termini of GPCRs, and control their intracellular trafficking and signal transduction efficiencies. Screening for such proteins that interact with the C-terminus of H3R resulted in identification of one of the chloride intracellular channel (CLIC) proteins, CLIC4. The association of CLIC4 with H3R was confirmed in in vitro pull-down assays, coimmunoprecipitation from rat brain lysate, and immunofluorescence microscopy of rat cerebellar neurons. The data from flowcytometric analysis, radioligand receptor binding assay, and cell-based ELISA indicated that CLIC4 enhanced cell surface expression of wild-type H3R, but not a mutant form of the receptor that failed to interact with CLIC4. These results indicate that, by binding to the C-terminus of H3R, CLIC4 plays a critical role in regulation of the receptor cell surface expression.

Original languageEnglish
Pages (from-to)603-608
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2008 May 2


  • CLIC4
  • G protein-coupled receptor
  • Histamine H3 receptor
  • Trafficking


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