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| Title | Stomatin encapsulates aquaporin-1 and urea transporter-B in the erythrocyte membrane. |
|---|---|
| Journal, issue, pages | Sci Adv, Vol. 12, Issue 14, Page eaec1721, Year 2026 |
| Publish date | Apr 3, 2026 |
Authors | Francesca Vallese / Huan Li / Lucia Barazzuol / Tito Calì / Oliver B Clarke / ![]() |
| PubMed Abstract | Stomatin is a ubiquitous and highly expressed protein in erythrocytes, which associates with cholesterol-rich microdomains in the plasma membrane and is known to regulate the activity of multiple ion ...Stomatin is a ubiquitous and highly expressed protein in erythrocytes, which associates with cholesterol-rich microdomains in the plasma membrane and is known to regulate the activity of multiple ion channels and transporters, but the structural basis of association with stomatin targets remains unknown. Here, we describe high-resolution structures of multiple stomatin complexes with endogenous binding partners isolated from human erythrocyte membranes, revealing that stomatin specifically associates with two membrane proteins involved in water transport and cell volume regulation, aquaporin-1 and the urea transporter SLC14A1. Together, our results reveal the structural basis of stomatin oligomerization, membrane association, and target recruitment and identify a putative role for stomatin in the regulation of osmotic balance in the erythrocyte. |
External links | Sci Adv / PubMed:41921000 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.0 - 3.1 Å |
| Structure data | EMDB-73881, PDB-9z7u: EMDB-74046, PDB-9zcz: EMDB-74047, PDB-9zd0: EMDB-74049, PDB-9zd2: EMDB-74052, PDB-9zd5: |
| Chemicals | ![]() ChemComp-HOH: ![]() ChemComp-CLR: ![]() ChemComp-PLM: ![]() ChemComp-PTY: ![]() ChemComp-PLC: ![]() ChemComp-S1P: |
| Source |
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Keywords | MEMBRANE PROTEIN / Oligomer / C8 symmetry / scaffold / TRANSPORT PROTEIN / aquaporin / SPFH / solute carrier / SLC / intramembrane region |
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homo sapiens (human)
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