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Biochem Biophys Res Commun. 2016 Jun 3;474(3):476-481. doi: 10.1016/j.bbrc.2016.04.138. Epub 2016 Apr 27.

The interaction domains of transient receptor potential canonical (TRPC)1/4 and TRPC1/5 heteromultimeric channels.

Author information

1
Department of Physiology, Seoul National University College of Medicine, Seoul, 110-799, Republic of Korea.
2
Department of Physiology, College of Medicine, Gachon University, Incheon, Republic of Korea.
3
Department of Physiology, College of Veterinary Medicine, Chungnam National University, Daejeon 305-764, Republic of Korea. Electronic address: kplee@cnu.ac.kr.
4
Department of Physiology, Seoul National University College of Medicine, Seoul, 110-799, Republic of Korea. Electronic address: insuk@snu.ac.kr.

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.

KEYWORDS:

Förster Resonance Energy Transfer (FRET); TRPC channel; Tetrameric structure

PMID:
27131740
DOI:
10.1016/j.bbrc.2016.04.138
[Indexed for MEDLINE]

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