Affinage

EPB41L2

Band 4.1-like protein 2 · UniProt O43491

Length
1005 aa
Mass
112.6 kDa
Annotated
2026-04-28
34 papers in source corpus 25 papers cited in narrative 25 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EPB41L2 (protein 4.1G) is a membrane-skeletal adaptor that couples diverse transmembrane proteins to the cortical cytoskeleton, thereby controlling their surface expression, subcellular distribution, and downstream signaling in neural, immune, reproductive, and skeletal tissues. Its FERM domain anchors the protein to the plasma membrane and directly binds adenylyl cyclase 6 to suppress cAMP production, while its C-terminal domain engages the cytoplasmic tails of GPCRs (A1AR, mGlu1α, PTHR, SREBs), immune receptors (FcγRI, CD226), and adhesion molecules (β1 integrin, NECL4), modulating receptor-mediated ERK, calcium, and Hedgehog signaling (PMID:21482674, PMID:31383768, PMID:26644476, PMID:16029167). Ca²⁺/calmodulin binding to the N-terminal headpiece induces a disorder-to-compact conformational switch that sterically inhibits FERM domain interactions, providing a calcium-dependent regulatory mechanism (PMID:23354586). In vivo, 4.1G knockout mice display disorganized internodal protein distribution in peripheral myelin, male infertility from impaired Sertoli–spermatid contacts, mislocalized photoreceptor synaptic terminals with reduced visual acuity, and defective primary ciliogenesis in preosteoblasts (PMID:22291039, PMID:21482674, PMID:25660028, PMID:35216233).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1998 Medium

    Identification of EPB41L2 as a new 4.1 family member established that the membrane-binding, spectrin-actin binding, and C-terminal domains are conserved, and that alternative splicing generates isoforms with distinct subcellular distributions.

    Evidence cDNA cloning, sequence analysis, and isoform-specific localization

    PMID:9598318

    Open questions at the time
    • No functional assays performed
    • Interacting partners unknown
    • Tissue-specific isoform functions uncharacterized
  2. 2004 High

    Discovery that 4.1G binds cytoplasmic tails of GPCRs (A1AR, mGlu1α) and the immune co-receptor CD226 revealed a general role as a GPCR/receptor scaffolding adaptor, with functional consequences for receptor surface expression and cAMP/calcium signaling.

    Evidence Yeast two-hybrid, Co-IP from brain tissue and transfected cells, domain truncation, cAMP and calcium functional assays, T cell activation and cytoskeleton fractionation

    PMID:12974671 PMID:15138281 PMID:15372499

    Open questions at the time
    • Stoichiometry and affinity of GPCR interactions unknown
    • In vivo relevance of GPCR scaffolding not tested
  3. 2005 High

    Demonstration that 4.1G promotes PTHR surface localization and enhances downstream ERK and calcium signaling — blocked by a dominant-negative CTD fragment — established it as a positive regulator of receptor trafficking and signaling output.

    Evidence Y2H, cell-surface biotinylation, ERK phosphorylation and calcium assays with dominant-negative construct in COS-7 cells

    PMID:16029167

    Open questions at the time
    • Mechanism of trafficking enhancement (recycling vs. degradation) unresolved
    • Dominant-negative effect not tested in vivo
  4. 2006 Medium

    Localization of 4.1G to specific Schwann cell membrane domains (paranodal loops, Schmidt-Lanterman incisures, periaxonal/abaxonal membranes) with developmental redistribution established it as a myelination-associated scaffold.

    Evidence Immunoelectron microscopy, double immunolabeling, and developmental Northern/Western blot analysis in rodent sciatic nerve

    PMID:16752423

    Open questions at the time
    • No loss-of-function data at this stage
    • Binding partners in Schwann cell membranes unidentified
  5. 2010 Medium

    Biochemical reconstitution of FERM domain interactions with erythroid membrane proteins and demonstration that Ca²⁺/calmodulin modulates these interactions established 4.1G as a calcium-regulated membrane adaptor.

    Evidence In vitro binding assays with purified proteins, calmodulin-affinity binding, domain truncation analysis

    PMID:20812914

    Open questions at the time
    • All data in vitro; in-cell calcium regulation not demonstrated
    • Relative affinities vs. 4.1R not functionally tested in cells
  6. 2011 High

    4.1G knockout mice revealed essential in vivo roles: NECL4-dependent Sertoli-spermatid adhesion for male fertility, and MPP6 targeting to Schmidt-Lanterman incisures for myelinated nerve organization, directly linking the adaptor function to tissue-level phenotypes.

    Evidence 4.1G knockout mouse with histology, ultrastructural EM, Co-IP, immunolocalization in testis and sciatic nerve

    PMID:21482674 PMID:22025680

    Open questions at the time
    • Whether fertility phenotype is strain-dependent remains uncertain
    • Direct vs. indirect role in MPP6 targeting not resolved
  7. 2012 High

    Multiple studies converged to show that 4.1G organizes internodal protein distribution in peripheral nerves, promotes tight junction assembly via its FERM domain, and suppresses adenylyl cyclase-mediated cAMP production at the plasma membrane, broadening its known functions beyond receptor scaffolding.

    Evidence 4.1G KO sciatic nerve confocal microscopy (juxtaparanodal protein mislocalization), overexpression/siRNA with cAMP assays and FERM-deletion mutants, calcium switch tight junction assay in OLN-93 cells

    PMID:21898413 PMID:22291039 PMID:23201780

    Open questions at the time
    • Identity of the adenylyl cyclase isoform targeted was unknown at this point
    • Tight junction function not validated in vivo
  8. 2013 High

    Structural biophysics revealed that Ca²⁺/calmodulin binding to the N-terminal headpiece induces a disorder-to-compact conformational transition that sterically occludes the FERM domain, providing a defined molecular switch mechanism for regulating 4.1G interactions.

    Evidence SAXS, NMR spectroscopy, and circular dichroism on purified headpiece and FERM domain constructs

    PMID:23354586

    Open questions at the time
    • No in-cell validation of conformational switch
    • Physiological calcium concentrations triggering the switch not determined
  9. 2015 High

    Identification of β1 integrin as a direct FERM domain ligand, with KO MEFs showing reduced integrin surface expression and impaired adhesion/migration, and identification of AP3B2-dependent neurite extension with retinal synapse mislocalization in KO mice, extended 4.1G's roles to cell adhesion and neuronal morphogenesis.

    Evidence In vitro binding, Co-IP, surface biotinylation, FAK phosphorylation in KO MEFs; Co-IP with AP3B2, optokinetic response and retinal immunofluorescence in KO mice

    PMID:25660028 PMID:26644476

    Open questions at the time
    • Whether integrin phenotype contributes to nerve or testis KO phenotypes untested
    • AP3B2 binding domain on 4.1G not mapped
  10. 2019 High

    Direct binding of the FERM domain to the N-terminus of adenylyl cyclase 6 was identified as the molecular basis for 4.1G-mediated cAMP suppression; mutagenesis of AC6 disrupted both binding and plasma membrane distribution, linking scaffold function to enzyme regulation.

    Evidence GST pulldown, Co-IP, AC6-N-3A mutagenesis, cAMP assay with 4.1G knockdown and dominant-negative AC6-N overexpression

    PMID:31383768

    Open questions at the time
    • In vivo consequences of AC6 regulation by 4.1G not examined
    • Whether other AC isoforms are similarly regulated is unknown
  11. 2022 Medium

    Discovery that 4.1G is required for primary ciliogenesis and Hedgehog signaling in preosteoblasts, with KO mice showing bone mineralization defects, revealed an unexpected role in cilium-dependent developmental signaling.

    Evidence 4.1G KO mouse bone phenotype, siRNA in MC3T3-E1 cells with cilium markers and Hedgehog pathway readouts, Alizarin Red staining

    PMID:35216233

    Open questions at the time
    • Mechanism by which 4.1G promotes ciliogenesis is unknown
    • Whether ciliary defects extend to other tissues not examined
    • Single lab finding
  12. 2025 Medium

    Biophysical characterization showed that the intrinsically disordered CTD forms a fuzzy complex with NuMA, with macromolecular crowding enhancing binding, suggesting that cellular crowding conditions tune 4.1G scaffold interactions.

    Evidence NMR, SAXS, circular dichroism, and binding kinetics under crowding conditions with purified proteins

    PMID:40726410

    Open questions at the time
    • No in-cell or functional validation of 4.1G-NuMA interaction
    • Physiological relevance of NuMA binding unknown
    • Whether crowding effects apply to other CTD partners untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include the structural basis and selectivity rules governing how 4.1G discriminates among its many transmembrane partners, whether the Ca²⁺/calmodulin conformational switch operates in physiological signaling contexts in vivo, the mechanism by which 4.1G promotes primary ciliogenesis, and whether human disease phenotypes arise from EPB41L2 loss-of-function.
  • No human genetic disease linked to EPB41L2 mutations
  • No atomic-resolution structure of full-length 4.1G or FERM–partner complexes
  • In vivo calcium regulation of 4.1G conformational state untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 8 GO:0008092 cytoskeletal protein binding 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005886 plasma membrane 4 GO:0005856 cytoskeleton 2 GO:0005829 cytosol 1
Pathway
R-HSA-112316 Neuronal System 7 R-HSA-162582 Signal Transduction 6 R-HSA-1500931 Cell-Cell communication 3 R-HSA-168256 Immune System 3
Partners
A1ARAC6CD226ITGB1MPP6NECL4NUMAPTHR

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 EPB41L2 (4.1G) encodes a 113-kDa protein with three conserved domains shared with 4.1R: a membrane-binding domain, a spectrin-actin binding domain, and a C-terminal domain. Different isoforms exhibit differential subcellular localizations, arising from both alternative splicing and distinct gene expression. cDNA cloning, sequence analysis, subcellular localization by isoform-specific expression Genomics Medium 9598318
2004 4.1G binds the carboxyl-terminal domain of CD226 (PTA-1) and forms a dynamic molecular complex with human discs large (hDlg) in T cells; T cell stimulation induces PTA-1 and 4.1G to associate tightly with the cytoskeleton, and the PTA-1 C-terminal peptide influences which isoform of 4.1G is bound. Co-immunoprecipitation, cytoskeleton fractionation, domain truncation binding assays, T cell activation experiments The Journal of biological chemistry Medium 15138281
2004 4.1G binds via its C-terminal domain to the third intracellular loop of the A1 adenosine receptor (A1AR), inhibiting A1AR-mediated cAMP inhibition and intracellular calcium release, and altering cell-surface A1AR expression. Yeast two-hybrid screen, truncation binding studies, co-immunoprecipitation from brain tissue, functional cAMP and calcium assays in HEK-293 and CHO cells The Biochemical journal High 12974671
2004 4.1G binds directly to the C-terminal tail of metabotropic glutamate receptor subtype 1α (mGlu1α), co-localizes with it in hippocampal neurons, increases mGlu1α ligand-binding ability, alters its cellular distribution, and influences mGlu1α-mediated cAMP accumulation. Co-immunoprecipitation from HEK293 cells and rat brain, domain truncation, immunofluorescence in hippocampal neurons, ligand binding assay, cAMP functional assay Journal of neuroscience research High 15372499
2005 4.1G interacts with the C-terminus of the PTH/PTH-related protein receptor (PTHR) and facilitates its cell-surface localization; full-length 4.1G (but not a dominant-negative C-terminal domain fragment) enhances PTHR-mediated ERK1/2 phosphorylation and intracellular calcium elevation. Yeast two-hybrid, co-localization by immunohistochemistry in COS-7 cells, cell-surface biotinylation assay, ERK phosphorylation assay, calcium measurement The Biochemical journal High 16029167
2006 4.1G localizes to paranodal loops, Schmidt-Lanterman incisures (SLI), periaxonal, mesaxonal, and abaxonal membranes of Schwann cells in rodent sciatic nerve, with distribution shifting from diffuse in immature cells to discrete membrane domains during maturation. Immunohistochemistry, double immunolabeling, immunoelectron microscopy, Northern/Western blot analysis Journal of neuroscience research Medium 16752423
2007 The C-terminal domain of 4.1G binds to the cytoplasmic tail of FcγRI (CD64); binding requires a membrane-proximal core motif HxxBxxxBB in FcγRI followed by hydrophobic and negatively charged residues, with an alternatively spliced 4.1G product showing increased binding. Yeast two-hybrid, alanine-scanning mutagenesis of FcγRI cytoplasmic tail Molecular immunology Medium 18023480
2010 4.1G binds to erythroid membrane proteins band 3, glycophorin C, CD44, p55, and calmodulin via its FERM/membrane-binding domain; Ca2+/calmodulin modulates these interactions, with the N-terminal headpiece region of 4.1G differentially affecting binding affinities for band 3 and glycophorin C compared to 4.1R135. In vitro binding assays, calmodulin-affinity binding, domain truncation analysis The Biochemical journal Medium 20812914
2011 4.1G interacts with nectin-like 4 (NECL4) in testis Sertoli cells; deletion of 4.1G in mice leads to decreased NECL4 expression and altered NECL4 localization, impaired Sertoli-spermatogenic cell contact, and male infertility in B6-129 hybrid mice. 4.1G knockout mouse generation, co-immunoprecipitation, immunolocalization, histology, ultrastructural electron microscopy Molecular and cellular biology High 21482674
2011 4.1G is required to target MPP6 (membrane protein palmitoylated 6) to Schmidt-Lanterman incisures (SLI) in myelinated peripheral nerves; in 4.1G knockout mice MPP6 is mislocalized to cytoplasm near Schwann cell nuclei, and SLI shape is altered in aged knockouts. Co-immunoprecipitation, immunofluorescence in 4.1G knockout mice, immunoelectron microscopy Molecular and cellular biology High 22025680
2011 Serine phosphorylation of the FcγRI cytoplasmic domain (by CK2) promotes its interaction with protein 4.1G and targets FcγRI to lipid rafts; a non-phosphorylatable FcγRI mutant is excluded from lipid rafts. Yeast two-hybrid, co-immunoprecipitation from human PBMC, in vitro CK2 phosphorylation assay, immunostaining, lipid raft fractionation Journal of leukocyte biology Medium 22003208
2012 4.1G is required for normal organization of internodal proteins in peripheral myelinated nerves; deletion of 4.1G in Schwann cells leads to aberrant distribution of juxtaparanodal proteins (Kv1 channels, Caspr2, TAG-1) that pile up at juxtaparanodes rather than forming a double strand along internodes. 4.1G knockout mouse, immunofluorescence, confocal microscopy of sciatic nerve The Journal of cell biology High 22291039
2012 4.1G co-immunoprecipitates with spectrin and SERCA2 in cardiac muscle, with 4.1G localizing to intracellular structures coincident with sarcoplasmic reticulum. Co-immunoprecipitation, immunofluorescence, subcellular fractionation Experimental cell research Medium 22429617
2012 Plasma membrane-associated 4.1G suppresses adenylyl cyclase-mediated cAMP production; this suppression requires the FERM domain for plasma membrane targeting, and is observed in membrane preparations of 4.1G-overexpressing cells. Overexpression, siRNA knockdown, FERM-domain deletion mutant, cAMP assays in HEK293 cells, membrane preparations Cellular signalling Medium 23201780
2012 4.1G FERM domain is essential for cellular arborization of oligodendrocyte cell line OLN-93; 4.1G promotes tight junction reassembly and its knockdown inhibits tight junction formation, with 4.1G clustering at cell periphery with ZO-1. Overexpression of domain-deleted constructs, siRNA knockdown, calcium switch tight junction assay, immunoprecipitation, immunofluorescence Journal of cellular physiology Medium 21898413
2013 4.1G interacts with a subset of CNG (cyclic-nucleotide gated) channels in rod outer segments (ROS) via its FERM and CTD domains; a smaller splice variant of 4.1G selectively binds CNG channels not associated with the peripherin-2-CNG channel complex. Immunoprecipitation, mass spectrometry, cDNA cloning, domain truncation binding assays, immunofluorescence Journal of cell science Medium 24144699
2013 Src kinase is present in SLIs of sciatic nerves in a complex with MPP6 and 4.1G; in 4.1G-deficient nerves (lacking both 4.1G and MPP6 in SLIs), activated P418-Src immunoreactivity in SLIs is increased, and MPP6 co-immunoprecipitates with Src. Immunofluorescence with phospho-specific Src antibodies, co-immunoprecipitation, 4.1G knockout mouse comparison Histochemistry and cell biology Medium 23306908
2013 Ca2+/calmodulin binding to the N-terminal headpiece region (GHP) of 4.1G — specifically to the peptide S71RGISRFIPPWLKKQKS — induces a conformational change from intrinsically disordered coiled structure to a compact structure, which sterically inhibits FERM domain interactions with membrane proteins. Small-angle X-ray scattering, NMR spectroscopy, circular dichroism, peptide binding assays Cell biochemistry and biophysics High 23354586
2015 4.1G directly binds β1 integrin via its membrane-binding domain; in 4.1G knockout MEFs, surface expression of β1 integrin and its active form are reduced, focal adhesion kinase phosphorylation is suppressed, and cell adhesion, spreading, and migration are impaired. Co-immunoprecipitation, in vitro binding assay with domain-deleted constructs, cell-surface biotinylation, FAK phosphorylation assay, migration assay in 4.1G KO MEFs The Journal of biological chemistry High 26644476
2015 4.1G binds to AP3B2 (adaptor protein 3 subunit β2, involved in neuronal membrane trafficking) and promotes neurite extension in an AP3B2-dependent manner; 4.1G-deficient retina shows mislocalization of photoreceptor terminals and impaired visual acuity. Co-immunoprecipitation, 4.1G knockout mouse, optokinetic response assay, immunofluorescence Cell reports Medium 25660028
2017 4.1G is required for proper sorting of scaffold protein Lin7 (Lin7c and Lin7a) in sciatic nerves; 4.1G-deficient mice show loss of Lin7 immunolocalization and reduced Lin7 protein, and MPP6 co-immunoprecipitates with Lin7. Loss of 4.1G also causes myelin thickening and paranodal attachment defects. 4.1G knockout mouse, immunofluorescence, co-immunoprecipitation, electron microscopy, motor conduction velocity measurement Histochemistry and cell biology Medium 28755316
2019 4.1G directly binds adenylyl cyclase type 6 (AC6) via its FERM domain interacting with the N-terminus of AC6; this interaction suppresses AC6 activity at the plasma membrane, attenuating PTHR-mediated Gs/AC6/cAMP signaling. An AC6-N arginine-to-alanine mutant (AC6-N-3A) disrupts both 4.1G binding and plasma membrane distribution. Co-immunoprecipitation, in vitro GST pulldown binding assay, mutagenesis (AC6-N-3A), cAMP functional assay, 4.1G knockdown, dominant-negative AC6-N overexpression Molecular pharmacology High 31383768
2022 4.1G is required for primary ciliogenesis in preosteoblasts; 4.1G knockout mice show suppressed primary cilium formation and calcium deposits in trabecular bone, and 4.1G knockdown in MC3T3-E1 cells suppresses cilia elongation, Hedgehog signaling induction, and osteoblast differentiation. 4.1G knockout mouse, siRNA knockdown, immunofluorescence (primary cilium markers), Hedgehog signaling assay, Alizarin Red calcium staining International journal of molecular sciences Medium 35216233
2023 EPB41L2 (4.1G) interacts physically with Super-Conserved Receptors Expressed in the Brain (SREBs, orphan GPCRs); EPB41L2 co-localizes with SREB1 at the plasma membrane and its knockdown reduces plasma membrane localization of SREB1 and alters its detergent solubility, suggesting EPB41L2 regulates membrane microenvironment of these receptors. BioID2 proximity labeling, streptavidin pulldown with mass spectrometry, co-immunoprecipitation, immunofluorescence, siRNA knockdown Cells Medium 37998360
2025 The C-terminal domain (CTD) of 4.1G is intrinsically disordered and forms a fuzzy complex with the disordered C-terminus of NuMA (nuclear mitotic apparatus protein); macromolecular crowding induces structural compaction of 4.1G-CTD while preserving its disordered character and enhances binding affinity and association kinetics with NuMA. NMR spectroscopy, small-angle X-ray scattering, circular dichroism, biophysical binding kinetics under crowding conditions Physical chemistry chemical physics Medium 40726410

Source papers

Stage 0 corpus · 34 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1998 Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics 97 9598318
2004 The LFA-1-associated molecule PTA-1 (CD226) on T cells forms a dynamic molecular complex with protein 4.1G and human discs large. The Journal of biological chemistry 59 15138281
2004 Cytoskeletal protein 4.1G binds to the third intracellular loop of the A1 adenosine receptor and inhibits receptor action. The Biochemical journal 44 12974671
2012 The cytoskeletal adapter protein 4.1G organizes the internodes in peripheral myelinated nerves. The Journal of cell biology 43 22291039
2004 Cytoskeletal protein 4.1G is a binding partner of the metabotropic glutamate receptor subtype 1 alpha. Journal of neuroscience research 41 15372499
2011 Lack of protein 4.1G causes altered expression and localization of the cell adhesion molecule nectin-like 4 in testis and can cause male infertility. Molecular and cellular biology 30 21482674
2005 Increase in cell-surface localization of parathyroid hormone receptor by cytoskeletal protein 4.1G. The Biochemical journal 30 16029167
2006 Expression of protein 4.1G in Schwann cells of the peripheral nervous system. Journal of neuroscience research 29 16752423
2011 Essential function of protein 4.1G in targeting of membrane protein palmitoylated 6 into Schmidt-Lanterman incisures in myelinated nerves. Molecular and cellular biology 26 22025680
2015 Protein-4.1G-Mediated Membrane Trafficking Is Essential for Correct Rod Synaptic Location in the Retina and for Normal Visual Function. Cell reports 23 25660028
2009 The function of glutamatergic synapses is not perturbed by severe knockdown of 4.1N and 4.1G expression. Journal of cell science 22 19225127
2017 Deficiency of a membrane skeletal protein, 4.1G, results in myelin abnormalities in the peripheral nervous system. Histochemistry and cell biology 18 28755316
2010 Involvement of a membrane skeletal protein, 4.1G, for Sertoli/germ cell interaction. Reproduction (Cambridge, England) 18 20200204
2005 Immunohistochemical study of a membrane skeletal molecule, protein 4.1G, in mouse seminiferous tubules. Histochemistry and cell biology 18 16041627
2005 Protein 4.1 G localizes in rodent microglia. Histochemistry and cell biology 17 16184385
2013 Involvement of Src in the membrane skeletal complex, MPP6-4.1G, in Schmidt-Lanterman incisures of mouse myelinated nerve fibers in PNS. Histochemistry and cell biology 16 23306908
2020 CircRNA EPB41L2 inhibits tumorigenicity of lung adenocarcinoma through regulating CDH4 by miR-211-5p. European review for medical and pharmacological sciences 15 32329852
2012 Isoforms of protein 4.1 are differentially distributed in heart muscle cells: relation of 4.1R and 4.1G to components of the Ca2+ homeostasis system. Experimental cell research 13 22429617
2015 Protein 4.1G Regulates Cell Adhesion, Spreading, and Migration of Mouse Embryonic Fibroblasts through the β1 Integrin Pathway. The Journal of biological chemistry 12 26644476
2013 Interaction of 4.1G and cGMP-gated channels in rod photoreceptor outer segments. Journal of cell science 12 24144699
2011 Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis. International journal of cell biology 12 21904552
2007 Protein 4.1G binds to a unique motif within the Fc gamma RI cytoplasmic tail. Molecular immunology 12 18023480
2012 Suppression of adenylyl cyclase-mediated cAMP production by plasma membrane associated cytoskeletal protein 4.1G. Cellular signalling 10 23201780
2011 Serine phosphorylation of FcγRI cytoplasmic domain directs lipid raft localization and interaction with protein 4.1G. Journal of leukocyte biology 10 22003208
2010 Similarities and differences in the structure and function of 4.1G and 4.1R135, two protein 4.1 paralogues expressed in erythroid cells. The Biochemical journal 9 20812914
2019 Activity of Adenylyl Cyclase Type 6 Is Suppressed by Direct Binding of the Cytoskeletal Protein 4.1G. Molecular pharmacology 8 31383768
2022 Cytoskeletal Protein 4.1G Is Essential for the Primary Ciliogenesis and Osteoblast Differentiation in Bone Formation. International journal of molecular sciences 7 35216233
2020 Anti-Osteoarthritic Effects of a Mixture of Dried Pomegranate Concentrate Powder, Eucommiae Cortex, and Achyranthis Radix 5:4:1 (g/g) in a Surgically Induced Osteoarthritic Rabbit Model. Nutrients 6 32235804
2013 Novel mechanism of regulation of protein 4.1G binding properties through Ca2+/calmodulin-mediated structural changes. Cell biochemistry and biophysics 5 23354586
2010 Immunolocalization of membrane skeletal protein, 4.1G, in enteric glial cells in the mouse large intestine. Neuroscience letters 5 21093541
2012 4.1G promotes arborization and tight junction formation of oligodendrocyte cell line OLN-93. Journal of cellular physiology 4 21898413
2023 Proximity Interactome Analysis of Super Conserved Receptors Expressed in the Brain Identifies EPB41L2, SLC3A2, and LRBA as Main Partners. Cells 2 37998360
2025 Exploring the effects of macromolecular crowding on the conformation and NuMA binding of 4.1G-CTD. Physical chemistry chemical physics : PCCP 1 40726410
2022 [Novel BRAF::EPB41L2 gene fusion in posterior fossa pilocytic astrocytoma. Brief communication]. Arkhiv patologii 1 36178221