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| Title | The cryo-EM structure of the SNX-BAR Mvp1 tetramer. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 1506, Year 2020 |
| Publish date | Mar 20, 2020 |
 Authors | Dapeng Sun / Natalia V Varlakhanova / Bryan A Tornabene / Rajesh Ramachandran / Peijun Zhang / Marijn G J Ford /   |
| PubMed Abstract | Sorting nexins (SNX) are a family of PX domain-containing proteins with pivotal roles in trafficking and signaling. SNX-BARs, which also have a curvature-generating Bin/Amphiphysin/Rvs (BAR) domain, ...Sorting nexins (SNX) are a family of PX domain-containing proteins with pivotal roles in trafficking and signaling. SNX-BARs, which also have a curvature-generating Bin/Amphiphysin/Rvs (BAR) domain, have membrane-remodeling functions, particularly at the endosome. The minimal PX-BAR module is a dimer mediated by BAR-BAR interactions. Many SNX-BAR proteins, however, additionally have low-complexity N-terminal regions of unknown function. Here, we present the cryo-EM structure of the full-length SNX-BAR Mvp1, which is an autoinhibited tetramer. The tetramer is a dimer of dimers, wherein the membrane-interacting BAR surfaces are sequestered and the PX lipid-binding sites are occluded. The N-terminal low-complexity region of Mvp1 is essential for tetramerization. Mvp1 lacking its N-terminus is dimeric and exhibits enhanced membrane association. Membrane binding and remodeling by Mvp1 therefore requires unmasking of the PX and BAR domain lipid-interacting surfaces. This work reveals a tetrameric configuration of a SNX-BAR protein that provides critical insight into SNX-BAR function and regulation. |
 External links | Nat Commun / PubMed:32198400 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.2 Å |
| Structure data | EMDB-20555, PDB-6q0x: |
| Source |
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 Keywords | LIPID BINDING PROTEIN / Mvp1 /  sorting nexin / SNX / PX / BAR / SNX-BAR |
