![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
![[thumbnail of 12500oa.pdf]](https://edoc.mdc-berlin.de/style/images/fileicons/application_pdf.png) |
PDF
- Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
1MB |
| Item Type: | Article |
|---|---|
| Title: | A stomatin dimer modulates the activity of acid-sensing ion channels |
| Creators Name: | Brand, J., Smith, E.S.J., Schwefel, D., Lapatsina, L., Poole, K., Omerbasic, D., Kozlenkov, A., Behlke, J., Lewin, G.R. and Daumke, O. |
| Abstract: | Stomatin proteins oligomerize at membranes and have been implicated in ion channel regulation and membrane trafficking. To obtain mechanistic insights into their function, we determined three crystal structures of the conserved stomatin domain of mouse stomatin that assembles into a banana-shaped dimer. We show that dimerization is crucial for the repression of acid-sensing ion channel 3 (ASIC3) activity. A hydrophobic pocket at the inside of the concave surface is open in the presence of an internal peptide ligand and closes in the absence of this ligand, and we demonstrate a function of this pocket in the inhibition of ASIC3 activity. In one crystal form, stomatin assembles via two conserved surfaces into a cylindrical oligomer, and these oligomerization surfaces are also essential for the inhibition of ASIC3-mediated currents. The assembly mode of stomatin uncovered in this study might serve as a model to understand oligomerization processes of related membrane-remodelling proteins, such as flotillin and prohibitin. |
| Keywords: | ASIC, Ion Channel Regulation, Membrane Trafficking, Protein Structure, Stomatin Family, Animals, Mice, Rats |
| Source: | EMBO Journal |
| ISSN: | 0261-4189 |
| Publisher: | Nature Publishing Group |
| Volume: | 31 |
| Number: | 17 |
| Page Range: | 3635-3646 |
| Date: | 29 August 2012 |
| Official Publication: | https://doi.org/10.1038/emboj.2012.203 |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
