Stomatin encapsulates aquaporin-1 and urea transporter–B in the erythrocyte membrane
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 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.
Fields of Study & Subjects
Erythrocyte Function and Pathophysiology
Ion Transport and Channel Regulation
Ion channel regulation and function
Publication details
- Journal / source
- Science Advances
- Publisher
- American Association for the Advancement of Science (AAAS)
- Volume
- 12
- Issue
- 14
- Pages
- eaec1721–eaec1721
- Publication date
- 1 April 2026
- Language
- EN