Direct visualization of the trimeric structure of the ASIC1a channel, using AFM imaging

Journal Article · Fri Aug 08 00:00:00 EDT 2008 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2008.05.100· OSTI ID:21143804

Carnally, Stewart M; Dev, Harveer S; Stewart, Andrew P ^[1]; Barrera, Nelson P ^[2]; Van Bemmelen, Miguel X; Schild, Laurent ^[3]; Henderson, Robert M ^[1]; Edwardson, J Michael ^[1]

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1. Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD (United Kingdom)
2. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW (United Kingdom)
3. Department of Pharmacology, University of Lausanne, rue du Bugnon 27, 1005 Lausanne (Switzerland)

There has been confusion about the subunit stoichiometry of the degenerin family of ion channels. Recently, a crystal structure of acid-sensing ion channel (ASIC) 1a revealed that it assembles as a trimer. Here, we used atomic force microscopy (AFM) to image unprocessed ASIC1a bound to mica. We detected a mixture of subunit monomers, dimers and trimers. In some cases, triple-subunit clusters were clearly visible, confirming the trimeric structure of the channel, and indicating that the trimer sometimes disaggregated after adhesion to the mica surface. This AFM-based technique will now enable us to determine the subunit arrangement within heteromeric ASICs.

• OSTI ID: 21143804
• Journal Information: Biochemical and Biophysical Research Communications, Vol. 372, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2008.05.100; PII: S0006-291X(08)01031-0; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ATOMIC FORCE MICROSCOPY
CRYSTAL STRUCTURE
DIMERS
IMAGES
MICA
MONOMERS
STOICHIOMETRY