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

Details

Serval ID
serval:BIB_5B6006AC1550
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Direct visualization of the trimeric structure of the ASIC1a channel, using AFM imaging.
Journal
Biochemical and Biophysical Research Communications
Author(s)
Carnally S.M., Dev H.S., Stewart A.P., Barrera N.P., Van Bemmelen M.X., Schild L., Henderson R.M., Edwardson J.M.
ISSN
1090-2104[electronic]
Publication state
Published
Issued date
2008
Volume
372
Number
4
Pages
752-755
Language
english
Abstract
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.
Keywords
Aluminum Silicates/chemistry, Humans, Microscopy, Atomic Force, Nerve Tissue Proteins/chemistry, Nerve Tissue Proteins/ultrastructure, Protein Subunits/chemistry, Sodium Channels/chemistry, Sodium Channels/ultrastructure
Pubmed
Web of science
Create date
30/10/2009 13:35
Last modification date
20/08/2019 15:14
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