Affinage

EPB41L2

Band 4.1-like protein 2 · UniProt O43491

Length
1005 aa
Mass
112.6 kDa
Annotated
2026-06-09
34 papers in source corpus 27 papers cited in narrative 27 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 5/5 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EPB41L2 (4.1G) is a multidomain membrane-skeletal adaptor that organizes the cell surface by linking transmembrane proteins to the underlying cytoskeleton, built from a membrane-binding (FERM) domain, a spectrin-actin binding domain, and a C-terminal domain (CTD) (PMID:9598318). Through its FERM domain it docks directly to diverse membrane partners—β1 integrin (PMID:26644476) and the N-terminus of adenylyl cyclase type 6 (AC6) via a triple-arginine motif (PMID:31383768)—while its CTD engages G-protein-coupled receptors including the A1 adenosine receptor (PMID:12974671), mGlu1α (PMID:15372499), and the parathyroid hormone receptor (PMID:16029167), as well as the immune receptor FcγRI (PMID:18023480) and CNG channels of photoreceptors (PMID:24144699). By controlling the cell-surface delivery and microenvironment of these partners, 4.1G tunes their signaling output: it promotes surface expression of PTHR and β1 integrin (PMID:16029167, PMID:26644476) yet directly suppresses AC6 catalytic activity to dampen Gs/cAMP signaling, an effect requiring FERM-dependent plasma-membrane association (PMID:23201780, PMID:31383768). In Schwann cells 4.1G localizes to paranodes and Schmidt-Lanterman incisures and is required to target the scaffold MPP6 and Lin7 proteins, organize internodal channel distribution, and restrain Src activity, with its loss causing myelin abnormalities and slowed nerve conduction (PMID:22025680, PMID:22291039, PMID:23306908, PMID:28755316). 4.1G also supports spermatogenic cell adhesion through NECL4 (loss causes male infertility) (PMID:21482674, PMID:22025680), positions photoreceptor synaptic terminals via AP3B2-dependent trafficking (PMID:25660028), and promotes primary ciliogenesis and Hedgehog-driven osteoblast differentiation (PMID:35216233). Its scaffolding is allosterically gated: Ca2+/calmodulin binding to the N-terminal headpiece drives a disorder-to-order transition that sterically inhibits FERM-domain interactions, providing Ca2+-dependent regulation (PMID:20812914, PMID:23354586), while the intrinsically disordered CTD forms a fuzzy, crowding-sensitive complex with NuMA (PMID:40726410).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 1998 Medium

    Established 4.1G as a protein 4.1R paralog with a conserved tripartite domain architecture, framing it as a candidate membrane-skeletal adaptor with isoform-specific localization.

    Evidence cDNA cloning, sequence analysis, and subcellular localization of isoforms

    PMID:9598318

    Open questions at the time
    • No binding partners or function identified
    • Isoform-specific roles not assigned
  2. 2004 High

    Demonstrated that 4.1G acts as a receptor-anchoring scaffold by binding GPCR intracellular domains (A1AR, mGlu1α) and the adhesion molecule PTA-1/CD226, modulating receptor surface expression and downstream cAMP/Ca2+ signaling.

    Evidence Yeast two-hybrid, Co-IP in brain tissue and transfected cells, functional cAMP/Ca2+ assays

    PMID:12974671 PMID:15138281 PMID:15372499

    Open questions at the time
    • Domain responsible for receptor binding not fully delineated across partners
    • Whether 4.1G acts in receptor trafficking vs. retention unclear
  3. 2005 High

    Showed 4.1G facilitates cell-surface localization of a GPCR (PTHR) and amplifies its downstream signaling, requiring full-length protein, establishing a positive trafficking/scaffolding role distinct from signal suppression.

    Evidence Yeast two-hybrid, cell-surface biotinylation with CTD dominant-negative, ERK and Ca2+ assays in COS-7

    PMID:16029167

    Open questions at the time
    • Mechanism of surface delivery (trafficking vs. stabilization) not resolved
    • Not validated in native tissue
  4. 2007 Medium

    Mapped a defined membrane-proximal motif (HxxBxxxBB) in FcγRI required for CTD binding, providing a sequence basis for 4.1G recognition of immune-receptor tails.

    Evidence Yeast two-hybrid, truncation and alanine-scanning mutagenesis

    PMID:18023480

    Open questions at the time
    • Interaction not confirmed in primary immune cells at this stage
    • Functional consequence not yet shown
  5. 2009 High

    Genetic loss-of-function established that 4.1G (with 4.1N) is not essential for glutamatergic synaptic transmission or LTP, bounding its in vivo role in the hippocampus despite GluR1 changes.

    Evidence 4.1G KO / 4.1N knockdown mice, electrophysiology, synaptosomal immunoblotting

    PMID:19225127

    Open questions at the time
    • Redundancy with other 4.1 family members not fully excluded
    • Subtle synaptic phenotypes not probed
  6. 2010 High

    Defined 4.1G's membrane-binding domain interactions with classical erythroid skeletal partners and adhesion molecules, and identified a Ca2+-dependent calmodulin site in the headpiece that modulates these interactions—first hint of allosteric regulation.

    Evidence In vitro binding/affinity assays, calmodulin interaction studies; Co-IP and immunolocalization in seminiferous tubules (CADM1)

    PMID:20200204 PMID:20812914

    Open questions at the time
    • Structural basis of CaM regulation not yet defined
    • Physiological context of membrane-protein binding incomplete
  7. 2011 High

    In vivo KO models established 4.1G as essential for organizing membrane specializations: it targets MPP6 to Schmidt-Lanterman incisures in Schwann cells and supports spermatogenic adhesion via NECL4, with loss causing male infertility.

    Evidence 4.1G KO mice, EM ultrastructure, Co-IP, immunolocalization in testis and sciatic nerve; SERCA2/spectrin complex in heart

    PMID:21482674 PMID:22025680 PMID:22429617

    Open questions at the time
    • Mechanism linking MPP6 mislocalization to myelin defects not yet defined
    • SERCA2 complex functional role uncharacterized
  8. 2012 High

    Resolved the mechanistic basis of 4.1G-mediated signal suppression and membrane organization—FERM-dependent plasma-membrane association is required to suppress adenylyl cyclase/cAMP output and to organize internodal channels (Kv1, Caspr2, TAG-1) and tight junctions.

    Evidence Gain/loss of function with FERM-deletion mutants, cAMP assays, KO mouse internodal marker imaging, calcium-switch tight-junction assays

    PMID:21898413 PMID:22291039 PMID:23201780

    Open questions at the time
    • The adenylyl cyclase isoform directly bound not yet identified at this stage
    • Link between membrane scaffolding and channel clustering mechanism unclear
  9. 2013 High

    Extended the partner repertoire to photoreceptor CNG channels and demonstrated phosphoserine-dependent partner selection (CK2-phosphorylated FcγRI) and a role in restraining Src at incisures, revealing post-translational and signaling control of 4.1G scaffolding.

    Evidence IP-MS, domain-binding assays, in vitro CK2-phosphopeptide binding, Co-IP in primary cells, lipid-raft fractionation, KO Src phospho-imaging

    PMID:22003208 PMID:23306908 PMID:24144699

    Open questions at the time
    • How phosphorylation switches partner affinity structurally not resolved
    • Mechanism by which 4.1G-MPP6 restrains Src unknown
  10. 2013 High

    Provided the structural mechanism for Ca2+ regulation: calmodulin binding to a defined headpiece peptide drives a disorder-to-order transition that sterically inhibits FERM-domain membrane interactions.

    Evidence SAXS, NMR, circular dichroism, peptide binding assays

    PMID:23354586

    Open questions at the time
    • Regulation not demonstrated for full-length protein in cells
    • Which membrane partners are most sensitive to CaM gating untested
  11. 2015 High

    KO-based studies established 4.1G as a determinant of β1-integrin surface availability and adhesion/migration, and of photoreceptor terminal positioning through AP3B2-dependent trafficking, linking the adaptor to cytoskeletal-coupled cell behavior and neuronal architecture.

    Evidence 4.1G KO MEFs and mice, in vitro binding, surface FACS, migration and FAK assays, retinal histology, optokinetic testing, neurite assays

    PMID:25660028 PMID:26644476

    Open questions at the time
    • Whether 4.1G stabilizes or traffics surface β1 integrin not distinguished
    • AP3B2-dependent trafficking step molecularly undefined
  12. 2017 High

    Connected 4.1G's Schwann-cell scaffolding role to functional myelin physiology—loss disrupts Lin7 sorting (via MPP6) and produces myelin and nerve-conduction defects.

    Evidence 4.1G KO mice, EM, electrophysiology, Co-IP (MPP6-Lin7), immunofluorescence

    PMID:28755316

    Open questions at the time
    • Causal chain from Lin7 mislocalization to conduction defect incomplete
    • Cell-autonomy not fully dissected
  13. 2019 High

    Pinpointed the direct molecular basis for cAMP suppression: 4.1G-FERM binds a triple-arginine motif in the AC6 N-terminus to control AC6 membrane distribution and inhibit its catalytic activity, attenuating PTHR-Gs signaling.

    Evidence In vitro binding, AC6-N-3A mutagenesis, competitive inhibition, siRNA, cAMP assays, Co-IP

    PMID:31383768

    Open questions at the time
    • Structural detail of the FERM-AC6N interface not solved
    • Whether other AC isoforms are similarly regulated unknown
  14. 2022 Medium

    Identified a developmental signaling role: 4.1G is required for primary ciliogenesis and cilia-dependent Hedgehog signaling driving osteoblast differentiation and bone mineralization.

    Evidence 4.1G KO mice, MC3T3-E1 knockdown, ciliary imaging, calcium-deposition and Hedgehog assays

    PMID:35216233

    Open questions at the time
    • Molecular mechanism linking 4.1G to ciliary assembly not defined
    • Direct ciliary partner not identified
  15. 2023 Medium

    Generalized 4.1G's GPCR-scaffolding role to orphan SREB receptors, showing it promotes SREB1 plasma-membrane localization and alters its membrane microenvironment.

    Evidence BioID2 proximity labeling, MS, Co-IP, siRNA knockdown, immunofluorescence

    PMID:37998360

    Open questions at the time
    • Direct vs. proximity interaction not fully separated
    • Functional consequence for SREB signaling untested
  16. 2025 High

    Characterized the CTD as intrinsically disordered, forming a fuzzy, crowding-enhanced complex with NuMA—extending 4.1G's interaction repertoire to a disorder-driven binding mode sensitive to the cellular environment.

    Evidence SAXS, NMR, in vitro binding kinetics under macromolecular crowding

    PMID:40726410

    Open questions at the time
    • Cellular role of the 4.1G-NuMA interaction not established
    • Whether crowding-dependent binding occurs in vivo untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unknown how the distinct partner repertoires (GPCRs, integrins, adenylyl cyclases, scaffolds, NuMA) are coordinated by a single adaptor across tissues, and whether EPB41L2 dysfunction underlies any human disease.
  • No human disease link established in the corpus
  • No integrated structural model of full-length 4.1G with multiple partners
  • Tissue-specific partner selection mechanism undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 8 GO:0098772 molecular function regulator activity 4 GO:0005198 structural molecule activity 3 GO:0008092 cytoskeletal protein binding 3
Localization
GO:0005886 plasma membrane 5 GO:0005856 cytoskeleton 2 GO:0005783 endoplasmic reticulum 1 GO:0005929 cilium 1
Pathway
R-HSA-162582 Signal Transduction 6 R-HSA-112316 Neuronal System 4 R-HSA-9609507 Protein localization 4 R-HSA-1474244 Extracellular matrix organization 1
Partners
ADCY6AP3B2CADM1FCGR1AITGB1MPP6NECL4NUMA1

Evidence

Reading pass · 27 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 regions of high homology to erythrocyte protein 4.1R: a membrane-binding domain, a spectrin-actin binding domain, and a C-terminal domain. Specific isoforms of 4.1G exhibit differential subcellular localizations, resulting from both alternative splicing and distinct gene expression. cDNA cloning, sequence analysis, subcellular localization studies Genomics Medium 9598318
2004 4.1G binds the carboxyl-terminal domain of the T cell adhesion molecule PTA-1 (CD226) and also associates with human discs large (hDlg). T cell stimulation causes PTA-1 and 4.1G to associate tightly with the cytoskeleton, and activated cells show altered binding of PTA-1 to the amino-terminal region of 4.1G, forming a dynamic molecular complex. Co-immunoprecipitation, membrane raft fractionation, cytoskeletal association assays, domain-binding studies The Journal of biological chemistry Medium 15138281
2004 4.1G binds to the third intracellular loop of the A1 adenosine receptor (A1AR) via its C-terminal domain. This interaction was confirmed in brain tissue and in HEK-293 and CHO cells. 4.1G overexpression reduced A1AR-mediated inhibition of cAMP accumulation, intracellular calcium release, and altered cell-surface A1AR expression. Yeast two-hybrid screening, truncation binding studies, co-immunoprecipitation in brain tissue, functional cAMP and calcium assays in HEK-293 and CHO cells The Biochemical journal High 12974671
2004 4.1G directly interacts with the metabotropic glutamate receptor subtype 1alpha (mGlu1alpha) via the C-terminal tail of mGlu1alpha, co-localizes with mGlu1alpha in hippocampal neurons, and modulates mGlu1alpha-mediated cAMP accumulation, ligand-binding ability, and cellular distribution. Co-localization in hippocampal neurons, co-immunoprecipitation in HEK-293 cells and rat brain tissue, domain truncation analysis, functional cAMP assays Journal of neuroscience research High 15372499
2005 4.1G interacts with the C-terminus of the parathyroid hormone receptor (PTHR) and facilitates cell-surface localization of PTHR, as shown by cell-surface biotinylation. The full-length 4.1G (but not 4.1G-CTD dominant-negative) enhanced PTH-stimulated ERK1/2 phosphorylation and intracellular Ca2+ elevation. Yeast two-hybrid, co-localization in COS-7 cells, cell-surface biotinylation assay, ERK phosphorylation and Ca2+ assays The Biochemical journal High 16029167
2006 4.1G is expressed in Schwann cells of the peripheral nervous system and is specifically localized at paranodal loops, Schmidt-Lanterman incisures, and periaxonal, mesaxonal, and abaxonal membranes. During development, 4.1G transitions from diffuse distribution in immature Schwann cells to discrete localization at these membrane specializations during myelination. Northern blot, Western blot, immunohistochemistry with specific antibody, double immunolabeling, immunoelectron microscopy Journal of neuroscience research Medium 16752423
2007 The C-terminal domain of 4.1G interacts with the cytoplasmic tail of FcγRI (CD64). A specific Fc gamma RI membrane-proximal core motif of HxxBxxxBB followed by hydrophobic and charged residues is central for 4.1G interaction, identified by Fc gamma RI truncation and alanine-substitution mutant analysis. Yeast two-hybrid, domain truncation analysis, alanine substitution mutagenesis Molecular immunology Medium 18023480
2009 Mice with deletion of 4.1G and knockdown of 4.1N to ~22% of wild-type levels (combined ~12% hippocampal expression) showed a moderate reduction in synaptosomal GluR1 at 3 weeks of age, but no change in basic glutamatergic synaptic transmission or long-term potentiation, indicating 4.1G and 4.1N do not have a crucial role in glutamatergic synaptic transmission. Knockout and knockdown mouse model, electrophysiology, synaptosomal fractionation and immunoblotting Journal of cell science High 19225127
2010 4.1G associates with cell adhesion molecule-1 (CADM1) in seminiferous tubule lysates, as shown by co-immunoprecipitation. 4.1G is immunolocalized along cell membranes of Sertoli cells, spermatogonia, and early spermatocytes, and is expressed in spermatogonial stem cells at cell-cell contact regions. Immunolocalization, immunoprecipitation, in vitro spermatogonial stem cell culture, immunoblotting Reproduction (Cambridge, England) Medium 20200204
2010 4.1G binds erythroid membrane proteins including band 3, glycophorin C, CD44, and p55 via its membrane-binding domain. The N-terminal headpiece region of 4.1G differentiates its binding affinities from those of 4.1R135 for band 3 and glycophorin C. The headpiece also contains a high-affinity calcium-dependent calmodulin-binding site that modulates interactions with these membrane proteins. In vitro binding assays, affinity characterization, calmodulin interaction studies The Biochemical journal High 20812914
2011 4.1G deficiency in mice (B6-129 hybrid background) causes male infertility associated with atrophy, impaired cell-cell contact, and sloughing of spermatogenic cells. 4.1G associates with NECL4 (nectin-like 4) in Sertoli cells, and NECL4 expression is decreased and mislocalized in 4.1G-/- testis. Knockout mouse model, histology, ultrastructural analysis (electron microscopy), co-immunoprecipitation, immunolocalization Molecular and cellular biology High 21482674
2011 4.1G co-localizes with MPP6 at Schmidt-Lanterman incisures and paranodes in sciatic nerve. MPP6 co-immunoprecipitates with 4.1G. In 4.1G knockout mice, MPP6 is mislocalized to the cytoplasm near Schwann cell nuclei, demonstrating that 4.1G is required for targeting MPP6 to Schmidt-Lanterman incisures. Immunofluorescence co-localization, co-immunoprecipitation, 4.1G knockout mouse analysis Molecular and cellular biology High 22025680
2011 In heart muscle cells, 4.1G is localized to intracellular structures coincident with sarcoplasmic reticulum and exists in an immunoprecipitable complex with spectrin and SERCA2. Immunofluorescence, immunoprecipitation, subcellular fractionation Experimental cell research Medium 22429617
2011 Serine phosphorylation of the FcγRI cytoplasmic tail by CK2 promotes preferential interaction with protein 4.1G in vitro. 4.1G co-localizes with FcγRI in unstimulated U937 cells where CY is constitutively serine-phosphorylated; FcγRI cross-linking causes uncoupling. A nonphosphorylatable FcγRI mutant is excluded from lipid rafts, implicating 4.1G in phosphoserine-dependent targeting of FcγRI to lipid rafts. Yeast two-hybrid, in vitro binding with CK2-phosphorylated peptides, co-immunoprecipitation in human PBMC, immunostaining, lipid raft fractionation, mutagenesis Journal of leukocyte biology High 22003208
2012 Deletion of 4.1G in Schwann cells causes aberrant distribution of internodal proteins including juxtaparanodal Kv1 channels, Caspr2, and TAG-1, and paranodal junction components. In 4.1G-/- mice, these proteins aggregate at the juxtaparanodal region rather than forming the normal double strand flanking paranodal junction components along internodes. 4.1G knockout mouse, immunofluorescence, confocal microscopy The Journal of cell biology High 22291039
2012 4.1G overexpression suppresses forskolin-induced and PTH-stimulated cAMP production in HEK293 cells; 4.1G knockdown increases cAMP production. A FERM-domain-deleted 4.1G mutant lacking plasma membrane distribution does not alter cAMP production, indicating that plasma membrane association of 4.1G is required for its suppression of adenylyl cyclase activity. Overexpression and siRNA knockdown in HEK293 cells, cAMP assay, membrane fractionation, FERM deletion mutagenesis Cellular signalling High 23201780
2012 4.1G overexpression promotes arborization of oligodendrocyte cell line OLN-93 through its FERM domain, while FERM-domain-deleted 4.1G does not. 4.1G also promotes tight junction reassembly (shown by calcium switch experiment) and its knockdown inhibits tight junction formation, with 4.1G co-clustering with ZO-1 at cell periphery. Overexpression and siRNA knockdown in OLN-93 cells, calcium switch assay, immunoprecipitation, immunofluorescence, domain deletion analysis Journal of cellular physiology Medium 21898413
2013 4.1G interacts with a subset of CNG channels in rod outer segments (ROS) through its FERM and CTD domains, identified by immunoprecipitation/mass spectrometry and confirmed by truncation and domain-binding assays. A smaller splice variant of 4.1G selectively interacted with CNG channels not associated with the peripherin-2-CNG channel complex. Immunoprecipitation and mass spectrometry, domain truncation analysis, domain-binding assays, immunofluorescence Journal of cell science High 24144699
2013 Src kinase is present in Schmidt-Lanterman incisures and forms a complex with MPP6. In 4.1G-deficient nerve fibers (which lack both 4.1G and MPP6 from SLIs), active (P418) Src immunoreactivity in SLIs is enhanced compared to wild-type, implicating the 4.1G-MPP6 complex in restraining Src activity at SLIs. Immunostaining with phospho-specific antibodies, 4.1G knockout mouse analysis, immunoprecipitation Histochemistry and cell biology Medium 23306908
2013 Ca2+/calmodulin binds to the N-terminal headpiece region (GHP) of 4.1G at the peptide SRGISRFIPPWLKKQKS, inducing a conformational switch from intrinsically disordered coiled structure to compact structure. This structural change sterically inhibits 4.1G FERM domain interactions with membrane proteins. Small-angle X-ray scattering, NMR spectroscopy, circular dichroism spectroscopy, peptide binding assays Cell biochemistry and biophysics High 23354586
2015 4.1G binds directly to β1 integrin via its membrane-binding domain (shown by Co-IP and in vitro binding assays). In 4.1G-/- mouse embryonic fibroblasts, cell surface expression of β1 integrin and its active form are decreased, adhesion, spreading, and migration are impaired, and focal adhesion kinase phosphorylation is suppressed. 4.1G knockout MEF cells, co-immunoprecipitation, in vitro binding assay, cell-surface FACS, migration assays, FAK phosphorylation analysis The Journal of biological chemistry High 26644476
2015 4.1G is highly expressed in retinal photoreceptors and binds to AP3B2 (a protein involved in neuronal membrane trafficking). 4.1G-deficient retinas show mislocalization of photoreceptor terminals (without loss of synaptic connections), and 4.1G promotes neurite extension in an AP3B2-dependent manner. 4.1G mutant mice show visual acuity impairment. 4.1G KO mouse, protein interaction (binding assay), immunohistochemistry, optokinetic response test, neurite extension assay Cell reports High 25660028
2017 4.1G deficiency in mice causes myelin abnormalities in the peripheral nervous system (thicker myelin internodes, distorted paranodal tips), slowed motor-conduction velocity, and loss of Lin7c and Lin7a (scaffold proteins) from sciatic nerves. MPP6 interacts with Lin7 by immunoprecipitation, and 4.1G is required for proper Lin7 sorting in Schwann cells. 4.1G-/- mouse model, electron microscopy, electrophysiology, immunoprecipitation, immunofluorescence Histochemistry and cell biology High 28755316
2019 4.1G directly and selectively binds to the N-terminus of adenylyl cyclase type 6 (AC6) via its FERM domain, as shown by in vitro binding assays. Three consecutive arginine residues in AC6-N are required for 4.1G-FERM binding and for proper plasma membrane distribution of AC6. This interaction suppresses AC6 catalytic activity, attenuating PTHR-mediated Gs/AC6/cAMP signaling. Co-immunoprecipitation, in vitro binding assay, site-directed mutagenesis (AC6-N-3A), competitive inhibition with AC6-N overexpression, siRNA knockdown, cAMP assay Molecular pharmacology High 31383768
2022 4.1G is expressed in bone and is required for primary ciliogenesis and osteoblast differentiation. In 4.1G-knockout mice, calcium deposits and primary cilium formation are suppressed in preosteoblast-rich trabecular bone. Knockdown of 4.1G in MC3T3-E1 cells suppresses cilium elongation and inhibits cilia-mediated Hedgehog signaling and subsequent osteoblast differentiation. 4.1G KO mouse, siRNA knockdown in MC3T3-E1 cells, immunofluorescence, calcium deposition assay, Hedgehog signaling assay International journal of molecular sciences Medium 35216233
2023 EPB41L2 (4.1G) is a proximity interactor of Super-Conserved Receptors Expressed in the Brain (SREBs), confirmed by BioID2 proximity labeling and co-immunoprecipitation. EPB41L2 promotes plasma membrane localization of SREB1 and modifies SREB1 membrane microenvironment (increased detergent solubilization) as shown by siRNA knockdown. BioID2 proximity labeling, mass spectrometry, co-immunoprecipitation, siRNA knockdown, immunofluorescence 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 disorder, enhances binding affinity for NuMA, and accelerates association kinetics. Small-angle X-ray scattering, NMR spectroscopy, biophysical binding assays under crowding conditions Physical chemistry chemical physics : PCCP High 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 7 32235804
2010 Immunolocalization of membrane skeletal protein, 4.1G, in enteric glial cells in the mouse large intestine. Neuroscience letters 6 21093541
2013 Novel mechanism of regulation of protein 4.1G binding properties through Ca2+/calmodulin-mediated structural changes. Cell biochemistry and biophysics 5 23354586
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

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