Preview |
PDF (Accepted Manuscript (final draft) incl. Figures)
- Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
3MB |
| Item Type: | Editorial |
|---|---|
| Title: | SPFH protein cage - one ring to rule them all |
| Creators Name: | Daumke, O. and Lewin, G.R. |
| Abstract: | Stomatin/prohibitin/flotillin/HflKC (SPFH) proteins comprise a universally conserved family of membrane-associated scaffolds that compartmentalize membranes, but the detailed molecular mechanism has remained unclear. In a recent paper published in Cell Research, Ma et al. determined the cryo-EM structure of the bacterial SPFH heterodimer HflK/C, which assembles into a giant molecular cage encasing four AAA+ protease hexamers; the structural work elucidates how SPFH proteins confine their client proteins in specialized membrane microdomains. |
| Keywords: | Amino Acid Sequence, Membrane Proteins |
| Source: | Cell Research |
| ISSN: | 1001-0602 |
| Publisher: | Nature Publishing Group |
| Volume: | 32 |
| Number: | 2 |
| Page Range: | 117-118 |
| Date: | February 2022 |
| Additional Information: | Copyright © 2021, Center for Excellence in Molecular Cell Science, CAS |
| Official Publication: | https://doi.org/10.1038/s41422-021-00605-7 |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page


Tools
Tools

