ArticlebioRxiv : the preprint server for biology2025
Stomatin encapsulates aquaporin-1 and urea transporter-B in the erythrocyte membrane.
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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 (AQP-1) and the urea transporter, UT-B (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.
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