ArticleBiochimica et biophysica acta2013
Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains.
Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 84 citations in OpenAlex.
- Deciphering Membrane Protein Complexes in Plasmodium falciparum Gametocytes via Integrative Structural Systems Biology.Molecular & cellular proteomics : MCP · 2026Article
- Stomatin encapsulates aquaporin-1 and urea transporter-B in the erythrocyte membrane.Science advances · 2026Article
- Role of channels in the ObioRxiv : the preprint server for biology · 2025Article
- Mechanical Stimulation of Red Blood Cells Aging: Focusing on the Microfluidics Application.Micromachines · 2025Review
- EphA-Mediated Regulation of Stomatin Expression in Prostate Cancer Cells.Cancer medicine · 2024Article
- Mutations in linker-2 of KLF1 impair expression of membrane transporters and cytoskeletal proteins causing hemolysis.Nature communications · 2024Article
- Erythrocyte Oxidative Status in People with Obesity: Relation to Tissue Losses, Glucose Levels, and Weight Reduction.Antioxidants (Basel, Switzerland) · 2024Article
- Sphingosine-1-phosphate suppresses GLUT activity through PP2A and counteracts hyperglycemia in diabetic red blood cells.Nature communications · 2023Article
- Potential Theranostic Roles of SLC4 Molecules in Human Diseases.International journal of molecular sciences · 2023Review
- Red Blood Cell Deformability Is Expressed by a Set of Interrelated Membrane Proteins.International journal of molecular sciences · 2023Article
- Proteomic analysis of sialoliths from calcified, lipid and mixed groups as a source of potential biomarkers of deposit formation in the salivary glands.Clinical proteomics · 2023Article
- Identification of Structural Determinants of the Transport of the Dehydroascorbic Acid Mediated by Glucose Transport GLUT1.Molecules (Basel, Switzerland) · 2023Article
- Structural and mutational studies suggest key residues to determine whether stomatin SPFH domains form dimers or trimers.Biochemistry and biophysics reports · 2022Article
- Mechanosensitive Pannexin 1 Activity Is Modulated by Stomatin in Human Red Blood Cells.International journal of molecular sciences · 2022Article
- Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth.Nature communications · 2022Article
- Structural organization of erythrocyte membrane microdomains and their relation with malaria susceptibility.Communications biology · 2021Article
- The SPFH Protein Superfamily in Fungi: Impact on Mitochondrial Function and Implications in Virulence.Microorganisms · 2021Review
- Cell-to-cell contact-mediated regulation of tumor behavior in the tumor microenvironment.Cancer science · 2021Review
- Proteome of Stored RBC Membrane and Vesicles from Heterozygous Beta Thalassemia Donors.International journal of molecular sciences · 2021Article
- Aging-associated changes in CD47 arrangement and interaction with thrombospondin-1 on red blood cells visualized by super-resolution imaging.Aging cell · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The widely expressed, homo-oligomeric, lipid raft-associated, monotopic integral membrane protein stomatin and its homologues are known to interact with and modulate various ion channels and transporters. Stomatin is a major protein of the human erythrocyte membrane, where it associates with and modifies the glucose transporter GLUT1; however, previous attempts to purify hetero-oligomeric stomatin complexes for biochemical analysis have failed. Because lateral interactions of membrane proteins may be short-lived and unstable, we have used in situ chemical cross-linking of erythrocyte membranes to fix the stomatin complexes for subsequent purification by immunoaffinity chromatography. To further enrich stomatin, we prepared detergent-resistant membranes either before or after cross-linking. Mass spectrometry of the isolated, high molecular, cross-linked stomatin complexes revealed the major interaction partners as glucose transporter-1 (GLUT1), anion exchanger (band 3), and water channel (aquaporin-1). Moreover, ferroportin-1 (SLC40A1), urea transporter-1 (SLC14A1), nucleoside transporter (SLC29A1), the calcium-pump (Ca-ATPase-4), CD47, and flotillins were identified as stomatin-interacting proteins. These findings are in line with the hypothesis that stomatin plays a role as membrane-bound scaffolding protein modulating transport proteins.
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