ArticlePloS one2017
Structure-function analysis of human stomatin: A mutation study.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- Stomatin encapsulates aquaporin-1 and urea transporter-B in the erythrocyte membrane.Science advances · 2026Article
- Stomatin and Stomatin-Like Proteins Can Regulate Transporter Proteins Activity and Has a Role in Cancer Metastasis.The Journal of membrane biology · 2025Review
- Structural basis for membrane microdomain formation by a human Stomatin complex.Nature communications · 2025Article
- Targeting lipid raft-related stomatin to ameliorate osteoporosis in preclinical models.Nature communications · 2025Article
- ATF6 enables pathogen infection in ticks by inducingProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Red blood cell lipid distribution in the pathophysiology and laboratory evaluation of chorea-acanthocytosis and McLeod syndrome patients.Frontiers in physiology · 2025Article
- EphA-Mediated Regulation of Stomatin Expression in Prostate Cancer Cells.Cancer medicine · 2024Article
- Kinase-catalyzed biotinylation for discovery and validation of substrates to multispecificity kinases NME1 and NME2.The Journal of biological chemistry · 2024Article
- The diverse functions of the DEG/ENaC family: linking genetic and physiological insights.The Journal of physiology · 2023Article
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- Cyanobacterial membrane dynamics in the light of eukaryotic principles.Bioscience reports · 2023Article
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- Proteomic analysis identifies Stomatin as a biological marker for psychological stress.Neurobiology of stress · 2023Article
- Lipid Polarization during Cytokinesis.Cells · 2022Review
- Structural and mutational studies suggest key residues to determine whether stomatin SPFH domains form dimers or trimers.Biochemistry and biophysics reports · 2022Article
- Removal of Stomatin, a Membrane-Associated Cell Division Protein, Results in Specific Cellular Lipid Changes.Journal of the American Chemical Society · 2022Article
- Female Germ Cell Development in Chickens and Humans: The Chicken Oocyte Enriched Genes Convergent and Divergent with the Human Oocyte.International journal of molecular sciences · 2022Review
- Distinct Impairments Characterizing Different ADNP Mutants Reveal Aberrant Cytoplasmic-Nuclear Crosstalk.Cells · 2022Article
- Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth.Nature communications · 2022Article
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Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stomatin is an ancient, widely expressed, oligomeric, monotopic membrane protein that is associated with cholesterol-rich membranes/lipid rafts. It is part of the SPFH superfamily including stomatin-like proteins, prohibitins, flotillin/reggie proteins, bacterial HflK/C proteins and erlins. Biochemical features such as palmitoylation, oligomerization, and hydrophobic "hairpin" structure show similarity to caveolins and other integral scaffolding proteins. Recent structure analyses of the conserved PHB/SPFH domain revealed amino acid residues and subdomains that appear essential for the structure and function of stomatin. To test the significance of these residues and domains, we exchanged or deleted them, expressed respective GFP-tagged mutants, and studied their subcellular localization, molecular dynamics and biochemical properties. We show that stomatin is a cholesterol binding protein and that at least two domains are important for the association with cholesterol-rich membranes. The conserved, prominent coiled-coil domain is necessary for oligomerization, while association with cholesterol-rich membranes is also involved in oligomer formation. FRAP analyses indicate that the C-terminus is the dominant entity for lateral mobility and binding site for the cortical actin cytoskeleton.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.