AFM imaging reveals the tetrameric structure of the TRPC1 channel

N P Barrera, Y Shaifta, I McFadzean, J P T Ward, R M Henderson, J M Edwardson

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)

Abstract

We have determined the subunit stoichiometry of the transient receptor potential C1 (TRPC1) channel by imaging isolated channels using atomic force microscopy (AFM). A frequency distribution of the molecular volumes of individual channel particles had two peaks, at 170 and 720 nm(3), corresponding with the expected sizes of TRPC1 monomers and tetramers, respectively. Complexes were formed between TRPC1 channels and antibodies against a V5 epitope tag present on each subunit. The frequency distribution of angles between pairs of bound antibodies had two peaks, at 88 degrees and 178 degrees. This result again indicates that the channel assembles as a tetramer. (C) 2007 Elsevier Inc. All rights reserved
Original languageEnglish
Pages (from-to)1086 - 1090
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume358
Issue number4
DOIs
Publication statusPublished - 13 Jul 2007

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