title: The interaction domains of transient receptor potential canonical (TRPC)1/4 and TRPC1/5 heteromultimeric channels.
abstract: Transient receptor potential canonical (TRPC) family contains a non-selective cation channel, and four TRPC subunits form a functional tetrameric channel. TRPC4/5 channels form not only the homotetrameric channel but also a heterotetrameric channel with TRPC1. We investigated the interaction domain required for TRPC1/4 or TRPC1/5 heteromultimeric channels using FRET and the patch-clamp technique. TRPC1 only localized at the plasma membrane (PM) when it was coexpressed with TRPC4 or TRPC5. The TRPC1/4 or TRPC1/5 heteromultimeric showed the typical outward rectifying I/V curve. When TRPC1 and TRPC4 form a heteromeric channel, the N-terminal coiled-coil domain (CCD) and C-terminal 725-745 region of TRPC1 interact with the N-terminal CCD and C-terminal 700-728 region of TRPC4. However, when TRPC1 and TRPC5 form a heteromeric channel, the N-terminal CCD and C-terminal 673-725 region of TRPC1 interact with the N-terminal CCD and C-terminal 707-735 region of TRPC5. In conclusion, the N-terminal CCD of TRPC channels is essential for the heteromultimeric structure of TRPC channels, whereas specific C-terminal regions are required for unique heteromerization between subgroups of TRPC channels.
authors.affiliation: Department of Physiology, Seoul National University College of Medicine, Seoul, 110-799, Republic of Korea.
authors.forename: Jongyun
authors.initials: J
authors.lastname: Myeong
authors.affiliation: Department of Physiology, Seoul National University College of Medicine, Seoul, 110-799, Republic of Korea.
authors.forename: Juyeon
authors.initials: J
authors.lastname: Ko
authors.affiliation: Department of Physiology, Seoul National University College of Medicine, Seoul, 110-799, Republic of Korea.
authors.forename: Chansik
authors.initials: C
authors.lastname: Hong
authors.affiliation: Department of Physiology, College of Medicine, Gachon University, Incheon, Republic of Korea.
authors.forename: Dongki
authors.initials: D
authors.lastname: Yang
authors.affiliation: Department of Physiology, College of Veterinary Medicine, Chungnam National University, Daejeon 305-764, Republic of Korea. Electronic address: kplee@cnu.ac.kr.
authors.forename: Kyu Pil
authors.initials: KP
authors.lastname: Lee
authors.affiliation: Department of Physiology, Seoul National University College of Medicine, Seoul, 110-799, Republic of Korea.
authors.forename: Ju-Hong
authors.initials: JH
authors.lastname: Jeon
authors.affiliation: Department of Physiology, Seoul National University College of Medicine, Seoul, 110-799, Republic of Korea. Electronic address: insuk@snu.ac.kr.
authors.forename: Insuk
authors.initials: I
authors.lastname: So
mesh_terms: D001665:Binding Sites; D011485:Protein Binding; D000072417:Protein Domains; D025941:Protein Interaction Mapping / Q000379:methods; D055503:Protein Multimerization / Q000502:physiology; D050052:TRPC Cation Channels / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D050052:TRPC Cation Channels; C489571:TRPC4 ion channel; C491780:TRPC5 protein, human; C096351:transient receptor potential cation channel, subfamily C, member 1
keywords: Förster Resonance Energy Transfer (FRET); TRPC channel; Tetrameric structure