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

Détails

ID Serval
serval:BIB_5B6006AC1550
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Direct visualization of the trimeric structure of the ASIC1a channel, using AFM imaging.
Périodique
Biochemical and Biophysical Research Communications
Auteur⸱e⸱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]
Statut éditorial
Publié
Date de publication
2008
Volume
372
Numéro
4
Pages
752-755
Langue
anglais
Résumé
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.
Mots-clé
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
Création de la notice
30/10/2009 13:35
Dernière modification de la notice
23/11/2020 12:06
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