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


Autoria(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.
Data(s)

2008

Resumo

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.

Identificador

http://serval.unil.ch/?id=serval:BIB_5B6006AC1550

isbn:1090-2104[electronic]

pmid:18514062

doi:10.1016/j.bbrc.2008.05.100

isiid:000257419500044

Idioma(s)

en

Fonte

Biochemical and Biophysical Research Communications, vol. 372, no. 4, pp. 752-755

Palavras-Chave #Aluminum Silicates/chemistry; Humans; Microscopy, Atomic Force; Nerve Tissue Proteins/chemistry; Nerve Tissue Proteins/ultrastructure; Protein Subunits/chemistry; Sodium Channels/chemistry; Sodium Channels/ultrastructure
Tipo

info:eu-repo/semantics/article

article