STOM Gene (Human Stomatin) – Structure, Function, and Localization OpenAI o3-deep-research-2025-06-26 94 citations 2025-11-04T03:15:12.723243

STOM Gene (Human Stomatin) – Structure, Function, and Localization

Overview of Stomatin (STOM)

Stomatin is a widely expressed membrane protein encoded by the human STOM gene (UniProt P27105). It belongs to the stomatin/prohibitin/flotillin/HflK/C (SPFH) superfamily (also called the band-7 family) of membrane proteins, which are known for organizing lipid microdomains (pubmed.ncbi.nlm.nih.gov). Stomatin is a ~31 kDa integral membrane protein that attaches to the cytosolic side of the plasma membrane via a hydrophobic segment (residues 26–54) in a hairpin-like insertion (pmc.ncbi.nlm.nih.gov). Both its N- and C-termini face the cytoplasm, consistent with a monotopic membrane topology (pmc.ncbi.nlm.nih.gov). Stomatin was first identified in human red blood cell (RBC) membranes (historically termed band 7.2b), and it was named for its absence in overhydrated hereditary stomatocytosis (OHSt), a condition where stomatin-deficient RBCs exhibit abnormal “stomatocyte” morphology (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The protein is highly conserved across species, with homologs like MEC-2 in C. elegans and podocin in kidney cells, reflecting its fundamental role in membrane biology (pmc.ncbi.nlm.nih.gov).

Oligomerization and lipid rafts: A hallmark of stomatin is its tendency to form homo-oligomers and associate with cholesterol-rich lipid rafts in the membrane (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In RBCs and other cells, stomatin molecules assemble into large complexes that are resistant to detergent, indicating raft association (pmc.ncbi.nlm.nih.gov). Breakthrough structural studies in 2025 resolved the cryo-EM structure of human stomatin in membranes, revealing a 16-subunit ring-shaped complex ~12 nm in diameter (pmc.ncbi.nlm.nih.gov). This ring forms a cage-like microdomain in the membrane that is mechanically distinct and resistant to curvature (pmc.ncbi.nlm.nih.gov). Such an arrangement suggests stomatin can stiffen the local membrane area, consistent with the idea that stomatin-rich rafts act as mechanotransduction platforms (pmc.ncbi.nlm.nih.gov). (Notably, other stomatin-family proteins like podocin and STOML3 similarly oligomerize and influence membrane stiffness in mechanosensory cells (pmc.ncbi.nlm.nih.gov).) Early biochemical work also indicated that stomatin is palmitoylated and partitions into raft fractions along with other major raft proteins (such as flotillins) (pmc.ncbi.nlm.nih.gov), although the recent structural data did not find a permanent cholesterol-binding pocket in stomatin’s structure (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Together, these features classify stomatin as a membrane scaffolding protein that organizes specialized lipid domains.

Localization: Stomatin is primarily localized to the plasma membrane, on the cytoplasmic side, where it clusters into discrete patches corresponding to lipid rafts (pmc.ncbi.nlm.nih.gov). In human RBCs, it is one of the major membrane proteins (~2–5% of total membrane protein) and is especially enriched in raft regions (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Stomatin has also been observed in intracellular vesicles and is notably enriched in exosomes. In fact, stomatin’s consistent presence in exosomes from many cell types (including blood cells and cancer cells) has led to proposals of using it as an exosomal marker (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). This enrichment likely ties to its raft-partitioning property, since several raft-organizing proteins (e.g., flotillin-1/2, caveolin-1) tend to be packaged into exosomes (pubmed.ncbi.nlm.nih.gov). Stomatin can also interact with other SPFH-family members to traffic within the cell; for example, stomatin-like protein 1 (STOML1) binds stomatin and targets to late endosomes (pmc.ncbi.nlm.nih.gov), though stomatin itself predominantly resides at the cell surface under steady-state conditions.

Membrane Scaffold and Protein Interactions

One of stomatin’s primary functions is to serve as a membrane scaffold or adaptor, organizing and modulating the activity of various membrane proteins. Stomatin exists as homo-oligomers in the membrane and can form complexes with a range of ion channels and transporters (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). A 2013 proteomic analysis of chemically cross-linked RBC membranes provided a clear picture of stomatin’s interactome in erythrocytes. The study identified GLUT1 (glucose transporter 1), band 3 anion exchanger (AE1), and aquaporin-1 as the major proteins cross-linked to stomatin, alongside several others such as the urea transporter (UT-B/SLC14A1), nucleoside transporter (ENT1/SLC29A1), plasma membrane Ca²⁺-ATPase (PMCA4), ferroportin (SLC40A1), CD47, and flotillin-1/2 (pmc.ncbi.nlm.nih.gov). These findings strongly support the idea that stomatin organizes multi-protein complexes in lipid rafts and influences the function of transport proteins in its vicinity (pmc.ncbi.nlm.nih.gov). Stomatin itself does not have known enzymatic activity – instead, it modulates other proteins’ activities through direct or indirect interactions, likely by affecting their localization, stability, or conformational state.

Regulation of transporter function: In erythrocytes, stomatin’s interaction with GLUT1 has a remarkable effect on substrate flux. Stomatin binding appears to alter GLUT1’s substrate specificity, diverting it from transporting glucose to transporting dehydroascorbic acid (DHA) – the oxidized form of vitamin C (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). This was shown in species (like humans) that cannot synthesize vitamin C: stomatin helps convert GLUT1 into a high-affinity DHA importer, enabling efficient vitamin C uptake and recycling in RBCs (pmc.ncbi.nlm.nih.gov). As a result, stomatin-rich RBCs take up oxidized vitamin C from plasma and reduce it internally, a critical process for antioxidant maintenance in humans (pmc.ncbi.nlm.nih.gov). Concomitantly, stomatin presence was found to repress glucose uptake through GLUT1 in RBCs while enhancing DHA uptake (pmc.ncbi.nlm.nih.gov). The molecular mechanism is still under investigation, but this functional switch has been documented and links stomatin to metabolic adaptation in erythrocytes (pmc.ncbi.nlm.nih.gov).

Stomatin also modulates transporter activity in other cell types. In hepatocytes, stomatin has been shown to interact with the sodium taurocholate cotransporting polypeptide (NTCP/SLC10A1) – the bile acid uptake transporter – within raft microdomains (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). Co-immunoprecipitation experiments confirmed stomatin–NTCP binding, and functional assays demonstrated that knocking down stomatin leads to increased bile salt uptake via NTCP (pubmed.ncbi.nlm.nih.gov). Interestingly, stomatin depletion raised NTCP levels at the cell surface, suggesting that stomatin normally limits NTCP’s plasma membrane abundance or activity (pubmed.ncbi.nlm.nih.gov). This indicates a negative regulatory role where stomatin keeps bile acid import in check, possibly by organizing NTCP in specific membrane domains or affecting its endocytic recycling. Such regulatory interactions underscore stomatin’s broader role as a modulator of solute transport across membranes.

Ion channel modulation and mechanosensation: Stomatin and its homologs are well known to influence ion channel function, particularly mechanosensitive and acid-sensing channels. In sensory neurons, stomatin is part of a protein complex (including stomatin-like proteins) that associates with acid-sensing ion channels (ASICs) and other degenerin/ENaC family channels (pmc.ncbi.nlm.nih.gov). Mammalian stomatin can bind ASIC subunits; notably, experiments have shown that stomatin must form dimers or higher-order oligomers to exert an inhibitory effect on ASIC currents (pmc.ncbi.nlm.nih.gov). For example, co-expression of stomatin was found to reduce ASIC3-mediated cation currents, and mutational studies revealed that stomatin monomers alone bind ASICs but dimerization is required for channel gating modulation (pmc.ncbi.nlm.nih.gov). These findings align with a 2012 study where a stomatin dimer was seen to modulate ASIC activity in vitro (pmc.ncbi.nlm.nih.gov). Beyond ASICs, stomatin-family proteins are integral to mechanosensory apparatus: Stomatin-like protein 3 (STOML3) is essential for touch sensation in mice, as it modulates mechanotransducer channels in dorsal root ganglion neurons (pmc.ncbi.nlm.nih.gov). In C. elegans, the stomatin homolog MEC-2 is required for mechanosensitive channel function in touch receptor neurons (pmc.ncbi.nlm.nih.gov). Recent research (2023) in worm neurons showed that MEC-2 forms dynamic protein condensates at the membrane that transition from liquid-like to a more solid state, a change that correlates with switching the complex’s function from cargo transport to mechanical signal transduction (phys.org) (phys.org). This highlights a general mechanism whereby stomatin proteins oligomerize to tune membrane mechanics and ion channel activity, impacting how cells sense mechanical forces. While stomatin (STOM) in humans is not the only player in touch sensation (redundant family members like STOML3 take on specialized roles), it clearly participates in ion channel regulation in various contexts.

A striking example in mechanosensation is in red blood cells themselves. RBCs experience shear stress in circulation and rely on mechanosensitive channels for volume regulation. Pannexin 1 (PANX1), a mechanosensitive membrane channel, was recently found to associate with stomatin in RBCs (www.mdpi.com). Proximity ligation assays showed that stomatin and PANX1 lie in close nanometer proximity on the erythrocyte membrane (www.mdpi.com). When stomatin is absent – as in RBCs from OHSt patients – PANX1 channel activity is dysregulated, supporting the idea that stomatin normally restrains or organizes PANX1 function (www.mdpi.com). Indeed, stomatin-deficient OHSt red cells exhibit a pathological leak of Na^+ and K^+ ions (pubmed.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The loss of stomatin causes an unregulated cation flux and osmotic fragility in these cells (pmc.ncbi.nlm.nih.gov). Thus, stomatin is thought to stabilize ion channels or transporters in a closed/inactive state under resting conditions, preventing detrimental leaks. The pathophysiology of hereditary stomatocytosis underscores stomatin’s role: in the OHSt subtype, mutations in the Rh-associated glycoprotein (RhAG) lead to mis-trafficking of stomatin, its absence from RBC membranes, and consequent Na^+/K^+ leakage (pmc.ncbi.nlm.nih.gov). Another rare variant called stomatin-deficient cryohydrocytosis (sdCHC) is caused by GLUT1 mutations and likewise results in RBCs with no stomatin and extreme cation permeability, alongside neurological symptoms (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). These disease connections illustrate that stomatin is crucial for maintaining membrane permeability barriers and ion homeostasis in red cells, likely through its interactions with transporters and channels.

Biological Roles and Pathways

Erythrocyte physiology: In human erythrocytes, stomatin constitutes ~2–3% of the membrane protein and is a key structural element of the membrane skeleton and raft domains (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). Although stomatin is not required for RBC viability in mice (Stom knockout mice are viable and do not show obvious stomatocytosis (pmc.ncbi.nlm.nih.gov)), human RBCs lacking stomatin (in OHSt or sdCHC patients) have significant defects in volume regulation and membrane stability (pmc.ncbi.nlm.nih.gov). Stomatin is thought to organize a sub-membranous network by linking to the actin-spectrin cytoskeleton – early microscopy showed stomatin co-localizes with cortical actin filaments in some cells (pmc.ncbi.nlm.nih.gov). However, no direct actin-binding sequence has been confirmed in stomatin, and this remains an area of investigation (pmc.ncbi.nlm.nih.gov). The prevailing model is that stomatin-rich lipid rafts provide platforms to concentrate and regulate membrane transporters (like band 3, GLUT1, aquaporin, etc.) and to possibly sequester ion channels. By doing so, stomatin helps the RBC adapt to stresses: for instance, during oxidative stress, the stomatin-GLUT1 switch to vitamin C uptake helps protect RBCs (pmc.ncbi.nlm.nih.gov); during mechanical stress, stomatin may modulate stretch-activated channels (such as PANX1 or Piezo-type channels) to prevent undue ion leakage (www.mdpi.com). Stomatin also leaves reticulocytes via exosomes during RBC maturation in some species, in parallel with other membrane proteins (pmc.ncbi.nlm.nih.gov) – this regulated removal may fine-tune the final content of the mature red cell membrane. Overall, stomatin’s primary role in RBCs is structural and regulatory, ensuring proper membrane composition, fluidity, and transporter function for a durable, biconcave cell (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov).

Signal transduction and metabolic pathways: Beyond RBCs, stomatin has emerging roles in cell signaling and metabolism. A recent Nature Communications (2022) study demonstrated that stomatin influences adipogenesis (fat cell differentiation) through the ERK/MAPK signaling pathway (pmc.ncbi.nlm.nih.gov). Stomatin is highly expressed in adipocyte lipid rafts, and its expression increases when pre-adipocytes are induced to differentiate or when mice are fed a high-fat diet (pmc.ncbi.nlm.nih.gov). Functional assays showed that overexpression of stomatin enhances lipid droplet growth (by promoting droplet fusion) and fatty acid uptake in maturing adipocytes (pmc.ncbi.nlm.nih.gov). Conversely, stomatin knockdown impaired the normal induction of key adipogenic transcription factors (such as C/EBPβ and PPARγ) and led to smaller adipocytes with less lipid storage (pmc.ncbi.nlm.nih.gov). Mechanistically, stomatin was found to modulate the activity of the ERK pathway during differentiation – loss of stomatin resulted in altered phosphorylation dynamics of ERK1/2, which are crucial for adipogenesis (pubmed.ncbi.nlm.nih.gov). These findings position stomatin as a positive regulator of adipocyte maturation, linking membrane microdomain organization to intracellular signaling cascades. It appears that by scaffolding certain raft proteins (possibly insulin or growth factor receptors, or downstream effectors), stomatin can influence the ERK pathway and thereby the gene expression program of differentiation (pmc.ncbi.nlm.nih.gov).

Stomatin’s impact on signaling is also evident in other contexts. In the liver, as noted, stomatin modulates bile acid signaling by regulating NTCP-mediated bile uptake – which could have downstream effects on metabolic homeostasis and even viral entry (since NTCP is the entry receptor for hepatitis B/D viruses) (pubmed.ncbi.nlm.nih.gov) (pubmed.ncbi.nlm.nih.gov). There is also evidence that stomatin can interact with signaling molecules or adaptors. A proteomic study in macrophages (2023) found that stomatin binds to peroxiredoxin-1 (Prdx1), a redox-regulating enzyme, and targets it for lysosomal degradation (pubmed.ncbi.nlm.nih.gov). By promoting Prdx1 turnover, stomatin caused an increase in cellular reactive oxygen species (ROS) levels, which in turn enhanced NF-κB signaling and osteoclast differentiation (pubmed.ncbi.nlm.nih.gov). This was shown in the context of bone metabolism: stomatin expression was upregulated in osteoclast precursors from osteoporotic bone, and mice lacking stomatin had increased bone mass due to reduced osteoclast activity (pubmed.ncbi.nlm.nih.gov). Importantly, inhibiting stomatin in macrophage/osteoclast-lineage cells blunted osteoclastogenesis and protected mice from estrogen-withdrawal bone loss (pubmed.ncbi.nlm.nih.gov). These results reveal a novel role for stomatin in a ROS-mediated signaling pathway that drives cell differentiation (osteoclast formation). It reinforces the concept that stomatin’s scaffold function is not limited to ion transporters – it can extend to organizing signal-regulatory complexes (in this case, a Prdx1 degradation complex) at the membrane or cytosolic face, thereby influencing pathways like oxidative signaling and NF-κB.

Pathophysiological and clinical significance: While stomatin is ubiquitously expressed, its dysregulation can have tissue-specific consequences. In the hematological realm, stomatin levels serve as a diagnostic marker for certain hereditary anemias (OHSt and cryohydrocytosis) (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). In those disorders, absence of stomatin in RBC membranes is a hallmark finding, used to distinguish them from other hemolytic anemias. Interestingly, the causative mutations in these conditions lie in other genes (ion channels or transporters), suggesting stomatin loss is a downstream effect that exacerbates the membrane leak phenotype (pmc.ncbi.nlm.nih.gov). The “stomatin-deficient” phenotype in anemic patients highlights how crucial stomatin is for normal RBC function.

Emerging evidence links stomatin to cancer and other diseases, mostly through its regulatory effects on signaling pathways. For instance, low stomatin expression has been correlated with increased metastasis in some cancers such as non-small cell lung cancer, implying a tumor suppressor function (possibly by restraining pro-migratory signaling at the membrane) (www.spandidos-publications.com). In contrast, high stomatin levels in certain lymphoma subtypes were associated with worse prognosis, suggesting context-dependent effects (pmc.ncbi.nlm.nih.gov). Experimentally, overexpressing stomatin in cancer cell lines was reported to inhibit the Akt signaling axis and slow tumor growth, supporting a role in modulating growth factor signaling at lipid rafts (pubmed.ncbi.nlm.nih.gov). These findings are still preliminary, but they dovetail with the idea that stomatin-rich microdomains influence signaling pathways like Akt and ERK that are central to proliferation and survival. Given its involvement in multiple pathways, stomatin (and its binding partners) could be explored as therapeutic targets. The osteoporosis study mentioned above is a prime example – by targeting stomatin in certain cells, researchers achieved a beneficial modulation of cell function (reducing osteoclast activity) (pubmed.ncbi.nlm.nih.gov). Similarly, manipulating stomatin levels could potentially alter metabolic outcomes in obesity or modulate viral entry in hepatitis (via NTCP interaction), though such applications remain to be tested.

Conclusion

Stomatin (STOM) is now recognized as a multifaceted membrane organizer that influences cell physiology by shaping the lipid microenvironment and regulating membrane protein function. Its primary role is structural and regulatory: forming membrane microdomains (rafts) and scaffolding select channels and transporters, thereby tuning their activity. In human cells, stomatin helps control substrate transport (glucose, vitamin C, bile acids), ion flux (Na^+, K^+, etc.), and mechanosensitive signaling, all dependent on context. These specific functions are carried out at the cytoplasmic face of the plasma membrane, often in cholesterol-rich domains where stomatin oligomers reside (pmc.ncbi.nlm.nih.gov) (www.mdpi.com). From red blood cells ensuring osmotic stability, to neurons modulating mechano‐transducers, to adipocytes expanding lipid stores, stomatin’s influence is widespread but consistently centers on organizing membrane components to facilitate the appropriate physiological response.

Mechanistically, stomatin does not act as an enzyme or classic receptor; rather, it is an adaptor protein – it binds to proteins like GLUT1, ASIC channels, or NTCP and alters their localization or function through direct interaction or by altering the local membrane properties (pmc.ncbi.nlm.nih.gov) (pmc.ncbi.nlm.nih.gov). The biological significance of stomatin is evident from both evolutionary conservation and disease associations. Loss of stomatin from the membrane can lead to dramatic phenotypes (ion-leaky, fragile RBCs (pmc.ncbi.nlm.nih.gov), impaired mechanosensation (pmc.ncbi.nlm.nih.gov), or altered cell differentiation (pubmed.ncbi.nlm.nih.gov)), whereas proper stomatin function contributes to homeostasis (e.g. vitamin C recycling in humans via RBCs (pmc.ncbi.nlm.nih.gov)). Ongoing research (2022–2024) continues to uncover new roles, such as stomatin’s control of MAPK signaling in adipogenesis (pmc.ncbi.nlm.nih.gov) and its impact on osteoclast biology through ROS signaling (pubmed.ncbi.nlm.nih.gov). These studies not only deepen our understanding of how stomatin works at the molecular level, but also point to potential translational avenues – for example, targeting stomatin-rich lipid raft complexes could modulate immune cell activity or metabolic processes in disease. In summary, stomatin serves as a key structural regulator of cell membranes, orchestrating the interplay between membrane structure and function to support proper cellular physiology.

References: (Key references from recent literature are cited in-line above, with publication year and source when available)

Citations

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  26. AnnotationURLCitation(end_index=8475, start_index=8313, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=molecular%2C%20cross,scaffolding%20protein%20modulating%20transport%20proteins')
  27. AnnotationURLCitation(end_index=8813, start_index=8651, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=molecular%2C%20cross,scaffolding%20protein%20modulating%20transport%20proteins')
  28. AnnotationURLCitation(end_index=9530, start_index=9361, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Apparently%2C%20stomatin%20modulates%20GLUT1%20to,is%20implicated%20that%20the%20high')
  29. AnnotationURLCitation(end_index=9673, start_index=9531, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=match%20at%20L620%20unable%20to,Hagen%20et%20al.%2C%202008')
  30. AnnotationURLCitation(end_index=10013, start_index=9871, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=match%20at%20L620%20unable%20to,Hagen%20et%20al.%2C%202008')
  31. AnnotationURLCitation(end_index=10338, start_index=10169, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Apparently%2C%20stomatin%20modulates%20GLUT1%20to,is%20implicated%20that%20the%20high')
  32. AnnotationURLCitation(end_index=10631, start_index=10462, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Apparently%2C%20stomatin%20modulates%20GLUT1%20to,is%20implicated%20that%20the%20high')
  33. AnnotationURLCitation(end_index=10962, start_index=10793, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Apparently%2C%20stomatin%20modulates%20GLUT1%20to,is%20implicated%20that%20the%20high')
  34. AnnotationURLCitation(end_index=11396, start_index=11221, title='The Lipid Raft Component Stomatin Interacts with the Na+ Taurocholate Cotransporting Polypeptide (NTCP) and Modulates Bile Salt Uptake - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/32316189/#:~:text=The%20sodium%20taurocholate%20cotransporting%20polypeptide,rafts%2C%20as%20demonstrated%20by%20a')
  35. AnnotationURLCitation(end_index=11549, start_index=11397, title='The Lipid Raft Component Stomatin Interacts with the Na+ Taurocholate Cotransporting Polypeptide (NTCP) and Modulates Bile Salt Uptake - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/32316189/#:~:text=play%20a%20role%20in%20the,CLCC1%20overexpression%20nor%20its%20knockdown')
  36. AnnotationURLCitation(end_index=11888, start_index=11731, title='The Lipid Raft Component Stomatin Interacts with the Na+ Taurocholate Cotransporting Polypeptide (NTCP) and Modulates Bile Salt Uptake - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/32316189/#:~:text=knockdown%20increased%20NTCP,interaction%20modulates%20bile%20salt%20transport')
  37. AnnotationURLCitation(end_index=12207, start_index=12050, title='The Lipid Raft Component Stomatin Interacts with the Na+ Taurocholate Cotransporting Polypeptide (NTCP) and Modulates Bile Salt Uptake - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/32316189/#:~:text=knockdown%20increased%20NTCP,interaction%20modulates%20bile%20salt%20transport')
  38. AnnotationURLCitation(end_index=13072, start_index=12891, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Mammalian%20stomatin%20modulates%20ENaC,mediated%20currents%20%5B23%5D.%20Similarly%2C%20stomatin')
  39. AnnotationURLCitation(end_index=13438, start_index=13257, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Mammalian%20stomatin%20modulates%20ENaC,mediated%20currents%20%5B23%5D.%20Similarly%2C%20stomatin')
  40. AnnotationURLCitation(end_index=13847, start_index=13666, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Mammalian%20stomatin%20modulates%20ENaC,mediated%20currents%20%5B23%5D.%20Similarly%2C%20stomatin')
  41. AnnotationURLCitation(end_index=14069, start_index=13955, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Kozlenkov%20A,Google%20Scholar')
  42. AnnotationURLCitation(end_index=14473, start_index=14306, title='Structural basis for membrane microdomain formation by a human Stomatin complex - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12344292/#:~:text=Several%20members%20of%20the%20stomatin,analysis%20of%20human%20Stomatin%20reveals')
  43. AnnotationURLCitation(end_index=14766, start_index=14599, title='Structural basis for membrane microdomain formation by a human Stomatin complex - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12344292/#:~:text=Several%20members%20of%20the%20stomatin,analysis%20of%20human%20Stomatin%20reveals')
  44. AnnotationURLCitation(end_index=15238, start_index=15053, title='A change in rigidity switches the function of protein condensates involved in sensing touch', type='url_citation', url='https://phys.org/news/2023-10-rigidity-function-protein-condensates-involved.html#:~:text=The%20focus%20of%20the%20study,Caenorhabditis%20elegans%2C%20a%20model%20organism')
  45. AnnotationURLCitation(end_index=15409, start_index=15239, title='A change in rigidity switches the function of protein condensates involved in sensing touch', type='url_citation', url='https://phys.org/news/2023-10-rigidity-function-protein-condensates-involved.html#:~:text=promoting%20MEC,of%20mechanical%20cues%20during%20mechanosensation')
  46. AnnotationURLCitation(end_index=16245, start_index=16100, title='Mechanosensitive Pannexin 1 Activity Is Modulated by Stomatin in Human Red Blood Cells', type='url_citation', url='https://www.mdpi.com/1422-0067/23/16/9401#:~:text=modulate%20bile%20salt%20uptake%20,lipid%20rafts%2C%20with%20connections%20to')
  47. AnnotationURLCitation(end_index=16498, start_index=16365, title='Mechanosensitive Pannexin 1 Activity Is Modulated by Stomatin in Human Red Blood Cells', type='url_citation', url='https://www.mdpi.com/1422-0067/23/16/9401#:~:text=Proximity%20Ligation%20Assay%20,Finally%2C%20we%20confirmed%20our')
  48. AnnotationURLCitation(end_index=16824, start_index=16679, title='Mechanosensitive Pannexin 1 Activity Is Modulated by Stomatin in Human Red Blood Cells', type='url_citation', url='https://www.mdpi.com/1422-0067/23/16/9401#:~:text=modulate%20bile%20salt%20uptake%20,lipid%20rafts%2C%20with%20connections%20to')
  49. AnnotationURLCitation(end_index=17104, start_index=16917, title='Hereditary dehydrated and overhydrated stomatocytosis: recent advances - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/10088641/#:~:text=The%20hereditary%20stomatocytoses%20and%20allied,stomatocytosis%20and%20familial%20pseudohyperkalemia%2C%20a')
  50. AnnotationURLCitation(end_index=17263, start_index=17105, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=the%20very%20rare%20condition%2C%20stomatin,spanning%20membrane%20proteins')
  51. AnnotationURLCitation(end_index=17490, start_index=17361, title='Erythrocyte adducin: A structural regulator of the red blood cell membrane - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3385930/#:~:text=,increased%20cation%20fluxes%20and%20elevated')
  52. AnnotationURLCitation(end_index=18060, start_index=17898, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=investigation%20revealed%20that%20stomatin%20deficiency,sdCHC%2C%20see%20below')
  53. AnnotationURLCitation(end_index=18432, start_index=18274, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=the%20very%20rare%20condition%2C%20stomatin,spanning%20membrane%20proteins')
  54. AnnotationURLCitation(end_index=18568, start_index=18433, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=Stomatin,hematological%20symptoms%20that%20do%20not')
  55. AnnotationURLCitation(end_index=19175, start_index=18992, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=The%20widely%20expressed%2C%20homo,subsequent%20purification%20by%20immunoaffinity%20chromatography')
  56. AnnotationURLCitation(end_index=19304, start_index=19176, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=Cross,probably%20acts%20as%20a%20scaffolding')
  57. AnnotationURLCitation(end_index=19596, start_index=19436, title='Structure-function analysis of human stomatin: A mutation study - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5456319/#:~:text=of%20this%20protein%20in%20red,due%20to%20mistrafficking%20during%20terminal')
  58. AnnotationURLCitation(end_index=19853, start_index=19724, title='Erythrocyte adducin: A structural regulator of the red blood cell membrane - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3385930/#:~:text=,increased%20cation%20fluxes%20and%20elevated')
  59. AnnotationURLCitation(end_index=20199, start_index=20050, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=human%20erythrocyte%20membrane%20domains%20,binding%20domain%20of')
  60. AnnotationURLCitation(end_index=20450, start_index=20317, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=The%20precise%20role%20of%20stomatin,In%20species')
  61. AnnotationURLCitation(end_index=20954, start_index=20812, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=match%20at%20L620%20unable%20to,Hagen%20et%20al.%2C%202008')
  62. AnnotationURLCitation(end_index=21244, start_index=21099, title='Mechanosensitive Pannexin 1 Activity Is Modulated by Stomatin in Human Red Blood Cells', type='url_citation', url='https://www.mdpi.com/1422-0067/23/16/9401#:~:text=modulate%20bile%20salt%20uptake%20,lipid%20rafts%2C%20with%20connections%20to')
  63. AnnotationURLCitation(end_index=21474, start_index=21374, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=al,0030%20%5BDOI')
  64. AnnotationURLCitation(end_index=21876, start_index=21743, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=The%20precise%20role%20of%20stomatin,In%20species')
  65. AnnotationURLCitation(end_index=22005, start_index=21877, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=Cross,probably%20acts%20as%20a%20scaffolding')
  66. AnnotationURLCitation(end_index=22440, start_index=22300, title='Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9296665/#:~:text=hypertrophy%20and%20obesity,It%20also%20promotes%20fatty')
  67. AnnotationURLCitation(end_index=22714, start_index=22612, title='Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9296665/#:~:text=assay%20%28Fig,BAT')
  68. AnnotationURLCitation(end_index=23022, start_index=22882, title='Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9296665/#:~:text=hypertrophy%20and%20obesity,It%20also%20promotes%20fatty')
  69. AnnotationURLCitation(end_index=23328, start_index=23206, title='Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9296665/#:~:text=match%20at%20L601%20respectively%29,7c')
  70. AnnotationURLCitation(end_index=23680, start_index=23543, title='Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/35854007/#:~:text=acid%20uptake%20and%20lipid%20droplet,PR%29%2C%20and%20BAT')
  71. AnnotationURLCitation(end_index=24210, start_index=24070, title='Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9296665/#:~:text=hypertrophy%20and%20obesity,It%20also%20promotes%20fatty')
  72. AnnotationURLCitation(end_index=24703, start_index=24528, title='The Lipid Raft Component Stomatin Interacts with the Na+ Taurocholate Cotransporting Polypeptide (NTCP) and Modulates Bile Salt Uptake - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/32316189/#:~:text=The%20sodium%20taurocholate%20cotransporting%20polypeptide,rafts%2C%20as%20demonstrated%20by%20a')
  73. AnnotationURLCitation(end_index=24861, start_index=24704, title='The Lipid Raft Component Stomatin Interacts with the Na+ Taurocholate Cotransporting Polypeptide (NTCP) and Modulates Bile Salt Uptake - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/32316189/#:~:text=knockdown%20increased%20NTCP,interaction%20modulates%20bile%20salt%20transport')
  74. AnnotationURLCitation(end_index=25284, start_index=25117, title='Targeting lipid raft-related stomatin to ameliorate osteoporosis in preclinical models - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/40595453/#:~:text=Mechanistically%2C%20STOM%20interacts%20with%20Prdx1%2C,induced%20bone%20loss.%20Overall')
  75. AnnotationURLCitation(end_index=25634, start_index=25467, title='Targeting lipid raft-related stomatin to ameliorate osteoporosis in preclinical models - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/40595453/#:~:text=Mechanistically%2C%20STOM%20interacts%20with%20Prdx1%2C,induced%20bone%20loss.%20Overall')
  76. AnnotationURLCitation(end_index=26027, start_index=25860, title='Targeting lipid raft-related stomatin to ameliorate osteoporosis in preclinical models - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/40595453/#:~:text=Osteoporosis%20is%20a%20metabolic%20bone,normal%20conditions%20and%20after%20ovariectomy')
  77. AnnotationURLCitation(end_index=26349, start_index=26182, title='Targeting lipid raft-related stomatin to ameliorate osteoporosis in preclinical models - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/40595453/#:~:text=Mechanistically%2C%20STOM%20interacts%20with%20Prdx1%2C,induced%20bone%20loss.%20Overall')
  78. AnnotationURLCitation(end_index=27246, start_index=27079, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=Stomatin%20first%20attracted%20attention%20when,was%20named%20after%20the%20disease')
  79. AnnotationURLCitation(end_index=27409, start_index=27247, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=investigation%20revealed%20that%20stomatin%20deficiency,sdCHC%2C%20see%20below')
  80. AnnotationURLCitation(end_index=27913, start_index=27751, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=investigation%20revealed%20that%20stomatin%20deficiency,sdCHC%2C%20see%20below')
  81. AnnotationURLCitation(end_index=28548, start_index=28398, title='Experimental and Therapeutic Medicine', type='url_citation', url='https://www.spandidos-publications.com/10.3892/etm.2021.10992#:~:text=7%20,activity%20of%20the%20anion%20exchanger')
  82. AnnotationURLCitation(end_index=28836, start_index=28688, title='Upregulation of stomatin is associated with poor prognosis and promotes tumor progression of orbital diffuse large B-cell lymphoma - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12141002/#:~:text=Upregulation%20of%20stomatin%20is%20associated,Google%20Scholar')
  83. AnnotationURLCitation(end_index=29158, start_index=29040, title='Stomatin-Mediated Inhibition of the Akt Signaling Axis Suppresses Tumor Growth - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/33757977/#:~:text=Stomatin,Cancer%20Chemother%20Pharmacol')
  84. AnnotationURLCitation(end_index=29842, start_index=29675, title='Targeting lipid raft-related stomatin to ameliorate osteoporosis in preclinical models - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/40595453/#:~:text=Mechanistically%2C%20STOM%20interacts%20with%20Prdx1%2C,induced%20bone%20loss.%20Overall')
  85. AnnotationURLCitation(end_index=30946, start_index=30763, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=The%20widely%20expressed%2C%20homo,subsequent%20purification%20by%20immunoaffinity%20chromatography')
  86. AnnotationURLCitation(end_index=31092, start_index=30947, title='Mechanosensitive Pannexin 1 Activity Is Modulated by Stomatin in Human Red Blood Cells', type='url_citation', url='https://www.mdpi.com/1422-0067/23/16/9401#:~:text=modulate%20bile%20salt%20uptake%20,lipid%20rafts%2C%20with%20connections%20to')
  87. AnnotationURLCitation(end_index=31818, start_index=31656, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=molecular%2C%20cross,scaffolding%20protein%20modulating%20transport%20proteins')
  88. AnnotationURLCitation(end_index=32000, start_index=31819, title='Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3790964/#:~:text=Mammalian%20stomatin%20modulates%20ENaC,mediated%20currents%20%5B23%5D.%20Similarly%2C%20stomatin')
  89. AnnotationURLCitation(end_index=32340, start_index=32211, title='Erythrocyte adducin: A structural regulator of the red blood cell membrane - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC3385930/#:~:text=,increased%20cation%20fluxes%20and%20elevated')
  90. AnnotationURLCitation(end_index=32535, start_index=32368, title='Structural basis for membrane microdomain formation by a human Stomatin complex - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC12344292/#:~:text=Several%20members%20of%20the%20stomatin,analysis%20of%20human%20Stomatin%20reveals')
  91. AnnotationURLCitation(end_index=32736, start_index=32569, title='Targeting lipid raft-related stomatin to ameliorate osteoporosis in preclinical models - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/40595453/#:~:text=Osteoporosis%20is%20a%20metabolic%20bone,normal%20conditions%20and%20after%20ovariectomy')
  92. AnnotationURLCitation(end_index=32986, start_index=32844, title='The Molecular Basis for Altered Cation Permeability in Hereditary Stomatocytic Human Red Blood Cells - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC5911802/#:~:text=match%20at%20L620%20unable%20to,Hagen%20et%20al.%2C%202008')
  93. AnnotationURLCitation(end_index=33251, start_index=33111, title='Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth - PMC', type='url_citation', url='https://pmc.ncbi.nlm.nih.gov/articles/PMC9296665/#:~:text=hypertrophy%20and%20obesity,It%20also%20promotes%20fatty')
  94. AnnotationURLCitation(end_index=33478, start_index=33311, title='Targeting lipid raft-related stomatin to ameliorate osteoporosis in preclinical models - PubMed', type='url_citation', url='https://pubmed.ncbi.nlm.nih.gov/40595453/#:~:text=Mechanistically%2C%20STOM%20interacts%20with%20Prdx1%2C,induced%20bone%20loss.%20Overall')