AFM imaging reveals the tetrameric structure of the TRPC1 channel.
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.
Barrera
Nelson P
NP
Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, UK.
Shaifta
Yasin
Y
McFadzean
Ian
I
Ward
Jeremy P T
JP
Henderson
Robert M
RM
Edwardson
J Michael
JM
D019281:Dimerization; D018625:Microscopy, Atomic Force; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D011487:Protein Conformation; D050052:TRPC Cation Channels / Q000648:ultrastructure*
D046912:Multiprotein Complexes; D050052:TRPC Cation Channels; C096351:transient receptor potential cation channel, subfamily C, member 1