Affinage

EPB41L1

Band 4.1-like protein 1 · UniProt Q9H4G0

Length
881 aa
Mass
98.5 kDa
Annotated
2026-06-09
32 papers in source corpus 22 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EPB41L1 (4.1N) is a neuron-enriched FERM-domain scaffolding protein that couples transmembrane receptors to the spectrin–actin cytoskeleton and thereby governs receptor surface delivery, lateral membrane diffusion, and synaptic plasticity (PMID:19503082, PMID:15364918). At excitatory synapses it binds the C-terminal domain of the AMPA receptor subunit GluA1 to drive activity-dependent receptor exocytosis and insertion into the plasma membrane, a step required for LTP expression; this interaction is gated by PKC phosphorylation and palmitoylation of GluA1 and by CaMKII phosphorylation of 4.1N itself, which nucleates a p-CaMKII–4.1N–GluA1 complex during LTP (PMID:19503082, PMID:37993087, PMID:37079350). The 4.1N–GluA1 interaction is required for LTP and short-term spatial memory in vivo, and its synaptic role is cell-type-specific, depending on the FERM domain in dentate gyrus granule neurons (PMID:37845032, PMID:41417164). Beyond AMPA receptors, 4.1N scaffolds kainate receptors GluK1/GluK2 (controlling forward trafficking and regulated endocytosis), the α7 acetylcholine receptor, D2/D3 dopamine receptors, and IP3R1, where it tethers the receptor to actin to restrict ER-membrane lateral diffusion, organize basolateral targeting in polarized cells, and shape Ca2+ wave signaling that supports neurite formation (PMID:12181426, PMID:12444087, PMID:15364918, PMID:23400781, PMID:23256752, PMID:21389686). Independently of its membrane scaffolding function, 4.1N undergoes NGF-induced, IP6K2-dependent nuclear translocation, where it inhibits PIKE-mediated nuclear PI3K activation and associates with NuMA to impose G1 arrest (PMID:11136977, PMID:10594058, PMID:30006360). In epithelial and tumor contexts it suppresses progression by recruiting PP1 through its FERM domain to inactivate JNK–c-Jun signaling and by directly binding 14-3-3 to promote its degradation, thereby restraining EMT and anoikis resistance (PMID:26575790, PMID:32448967). 4.1N is also required for lateral membrane assembly in epithelial cells and for the hypothalamus–pituitary–reproductive axis in vivo (PMID:29428502, PMID:33046791).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1999 High

    Established that 4.1N is not solely a membrane scaffold but can act in the nucleus, linking NGF signaling to cell-cycle control.

    Evidence Co-IP, domain mapping, and nuclear-targeting constructs with G1 arrest readout in PC12 cells

    PMID:10594058

    Open questions at the time
    • How NGF triggers nuclear import was not defined
    • Whether NuMA binding is the direct effector of G1 arrest unresolved
  2. 2000 High

    Defined a nuclear signaling function in which 4.1N restrains nuclear PI3K activity, connecting it to the PIKE GTPase pathway.

    Evidence Yeast two-hybrid, Co-IP, and PI3K lipid kinase activity assays with nuclear fractionation

    PMID:11136977

    Open questions at the time
    • Physiological consequence of PIKE inhibition not established in neurons
    • Mechanism of inhibition (sequestration vs. catalytic) unknown
  3. 2002 High

    Showed 4.1N is a general receptor-surface-expression scaffold by mapping direct binding to D2/D3 dopamine receptors and IP3R1 with functional trafficking consequences.

    Evidence Yeast two-hybrid, pulldown, Co-IP, deletion mapping, and immunofluorescence in transfected and polarized cells

    PMID:12181426 PMID:12444087

    Open questions at the time
    • Whether endogenous receptor trafficking depends on 4.1N not tested
    • Binding stoichiometry and regulation unexamined
  4. 2004 High

    Provided the mechanistic principle of 4.1N action — tethering a receptor to actin to restrict its lateral membrane diffusion — using IP3R1 as a model.

    Evidence FRAP of GFP-IP3R1 in live hippocampal neurons with dominant-negative, domain-swap, and actin-depolymerization manipulations

    PMID:15364918

    Open questions at the time
    • Did not address whether diffusion restriction applies to other 4.1N receptor partners
    • Quantitative spectrin contribution not dissected
  5. 2009 High

    Established 4.1N as a required effector of activity-dependent AMPA receptor insertion, tying its scaffold function to synaptic plasticity and identifying PKC/palmitoylation as upstream regulators.

    Evidence Live imaging of GluA1 insertion events, dominant-negative peptide, GluA1 phospho/palmitoylation mutants, and LTP electrophysiology

    PMID:19503082

    Open questions at the time
    • How 4.1N couples GluA1 to exocytic machinery left open
    • In vivo behavioral relevance not addressed in this study
  6. 2013 Medium

    Extended the scaffolding role to kainate and nicotinic receptors, showing a common palmitoylation/PKC-regulated binding logic across receptor families.

    Evidence Co-IP, surface biotinylation, endocytosis and palmitoylation-mutant assays, and acute brain slice biochemistry for GluK2/GluK1 and α7 AChR

    PMID:23256752 PMID:23400781

    Open questions at the time
    • Receptor-specific differences in regulation not reconciled
    • Endogenous knockout validation limited
  7. 2016 Medium

    Defined a tumor-suppressive mechanism in which 4.1N recruits PP1 via its FERM domain to inactivate JNK–c-Jun signaling.

    Evidence Co-IP, PP1 activity assay, FERM-deletion mapping, knockdown/overexpression, and xenograft model in NSCLC

    PMID:26575790

    Open questions at the time
    • Single lab without reciprocal validation across cancer types
    • Direct PP1 dephosphorylation of JNK not biochemically reconstituted
  8. 2018 Medium

    Identified IP6K2 as the determinant of 4.1N nuclear translocation and linked the interaction to cerebellar synapse and locomotor phenotypes in vivo.

    Evidence Co-IP, IP6K2 knockout mice, cerebellar histology, synaptic morphology, and behavioral assays

    PMID:30006360

    Open questions at the time
    • Whether IP6K2 acts catalytically or structurally in nuclear import unknown
    • Connection to PIKE/NuMA nuclear functions not integrated
  9. 2020 Medium

    Revealed an additional anti-tumor mechanism — direct binding and proteasomal degradation of 14-3-3 to block EMT and anoikis resistance — and an in vivo neuroendocrine requirement.

    Evidence Co-IP, ubiquitin-proteasome degradation assays, xenografts in EOC cells, and 4.1N knockout mouse neuroendocrine phenotyping

    PMID:32448967 PMID:33046791

    Open questions at the time
    • Mechanism linking 4.1N to the 14-3-3 degradation machinery undefined
    • Molecular basis of GnRH axonal trafficking defect not resolved
  10. 2023 High

    Resolved the trafficking step controlled by 4.1N (exocytosis basally; both transport and exocytosis during plasticity), showed CaMKII phosphorylation builds the plasticity complex, and uncovered cell-type-specific synaptic dependence.

    Evidence Single-molecule live imaging with siRNA knockdown, phospho-specific Co-IP, interfering peptides, LTP electrophysiology, and cell-type-specific viral knockdown with domain rescue

    PMID:37079350 PMID:37845032 PMID:37993087

    Open questions at the time
    • Why DG vs CA1 neurons differ in 4.1N dependence mechanistically unexplained
    • Functional partition between 4.1N and SAP97 not fully delineated
  11. 2025 Medium

    Demonstrated behavioral relevance, showing the 4.1N–GluA1 interaction is required for LTP and short-term spatial memory in vivo.

    Evidence Viral interfering GluA1 C80 peptide in CA1, LTP electrophysiology, and spatial memory testing

    PMID:41417164

    Open questions at the time
    • Single interfering-peptide approach without genetic confirmation
    • Selective effect on short- but not long-term memory mechanistically unexplained

Open questions

Synthesis pass · forward-looking unresolved questions
  • How 4.1N's distinct functional modes — membrane receptor scaffolding, nuclear cell-cycle/PI3K regulation, and tumor-suppressive PP1/14-3-3 signaling — are partitioned and switched within a single cell remains unresolved.
  • No unified model integrating cytoplasmic, synaptic, and nuclear pools
  • Structural basis for FERM-domain selection among diverse partners undefined
  • Regulation of subcellular partitioning beyond NGF/IP6K2 unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 3 GO:0008092 cytoskeletal protein binding 1
Localization
GO:0005886 plasma membrane 4 GO:0005634 nucleus 3 GO:0005829 cytosol 1 GO:0005856 cytoskeleton 1
Pathway
R-HSA-112316 Neuronal System 4 R-HSA-9609507 Protein localization 4 R-HSA-162582 Signal Transduction 3 R-HSA-1643685 Disease 3
Partners
FLOT1GRIA1GRIK2IP6K2ITPR1NUMA1PP1YWHA (14-3-3)
Complex memberships
IP3R1–4.1N–CASK–syndecan-2 complexp-CaMKII–4.1N–GluA1 complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2009 4.1N is required for activity-dependent GluR1 (GluA1) AMPA receptor insertion into the plasma membrane. PKC phosphorylation of GluR1 at S816 and S818 enhances 4.1N binding to GluR1 and facilitates GluR1 insertion. Palmitoylation of GluR1 C811 modulates PKC phosphorylation and GluR1 insertion. Disrupting 4.1N-dependent GluR1 insertion decreases surface GluR1 expression and impairs LTP expression. Live imaging of individual GluR1 insertion events, dominant-negative peptide disruption, co-immunoprecipitation, site-directed mutagenesis of GluR1 phosphorylation and palmitoylation sites, LTP electrophysiology Nature neuroscience High 19503082
2000 4.1N interacts with PIKE (a nuclear GTPase) and translocates to the nucleus upon NGF treatment, where overexpression of 4.1N abolishes PIKE-mediated enhancement of nuclear PI3K lipid kinase activity. NGF-stimulated nuclear translocation of 4.1N inhibits PIKE activation of nuclear PI3K. Yeast two-hybrid screen, co-immunoprecipitation, PI3K lipid kinase activity assay, dominant-negative overexpression, nuclear fractionation Cell High 11136977
2002 4.1N interacts specifically with D2 and D3 dopamine receptors via the N-terminal segment of their third intracellular domain and the C-terminal domain of 4.1N. Expression of a 4.1N truncation fragment reduces plasma membrane localization of D2 and D3 receptors, indicating 4.1N is required for dopamine receptor surface expression. Yeast two-hybrid, pulldown, co-immunoprecipitation, deletion mapping, immunofluorescence in transfected HEK293 and Neuro2A cells Molecular pharmacology Medium 12181426
2002 4.1N binds to the C-terminal cytoplasmic tail of IP3R1 (inositol 1,4,5-trisphosphate receptor type 1) and is required for translocation of IP3R1 to the basolateral membrane domain in polarized MDCK cells. The 4.1N-binding region of IP3R1 is necessary and sufficient for basolateral targeting, and a fragment of the IP3R1-binding region of 4.1N blocks co-expressed IP3R1 basolateral localization. Yeast two-hybrid, co-immunoprecipitation, dominant-negative fragment expression, immunofluorescence in polarized MDCK cells The Journal of biological chemistry High 12444087
1999 4.1N interacts with the nuclear mitotic apparatus protein NuMA via its C-terminal domain. NGF treatment causes translocation of 4.1N to the nucleus and promotes 4.1N–NuMA association. Nuclear-targeted 4.1N arrests PC12 cells at G1 and produces aberrant nuclear morphology. Inhibition of 4.1N nuclear translocation prevents NGF-mediated cell division arrest, which is reversed by 4.1N overexpression. Co-immunoprecipitation, deletion mapping, targeted nuclear localization constructs, cell cycle analysis (G1 arrest), nuclear morphology imaging in PC12 cells The Journal of neuroscience High 10594058
2003 4.1N binds specifically to the CTDDelta splice form of 4.1N via a 50-amino-acid fragment in the C-terminal tail of IP3R1. The 4.1N–IP3R1 complex is enriched in synaptic locations and can be immunoprecipitated from rat brain synaptosomes. A quaternary complex of IP3R1–4.1N–CASK–syndecan-2 can form in vitro. Yeast two-hybrid, in vitro binding assay, co-immunoprecipitation from rat brain synaptosomes, deletion mapping Molecular and cellular neurosciences Medium 12676536
2004 4.1N acts as a linker between IP3R1 and actin filaments in neuronal dendrites, restricting lateral diffusion of IP3R1 on the ER membrane. Dominant-negative 4.1N or blockade of 4.1N binding to IP3R1 increased IP3R1 diffusion constant. Adding the 4.1N-binding sequence to IP3R3 (which normally lacks it) conferred actin-dependent restriction of its diffusion. FRAP (fluorescence recovery after photobleaching) of GFP-tagged IP3R1 in live hippocampal neurons, dominant-negative overexpression, actin depolymerization, domain swap experiments The Journal of biological chemistry High 15364918
2005 4.1N interacts with nectin-like molecule 1 (NECL1) and NECL1 recruits 4.1N from the cytoplasm to the plasma membrane through its C-terminus, suggesting 4.1N participates in cell-cell junction organization in neurons. In vitro binding assay, co-immunoprecipitation, immunofluorescence localization in transfected cells Biochimica et biophysica acta Low 15893517
2006 Both the C-terminal 14 amino acid segment (CTT14aa) and the middle segment (CTM1) of IP3R1 can bind 4.1N as peptide fragments, but the CTT14aa is the responsible binding site in the context of full-length tetrameric IP3R1. Immunoprecipitation with deletion constructs, FRAP in neuronal dendrites using competing peptides Biochemical and biophysical research communications Medium 16487933
2011 IP3R1 localization via 4.1N is necessary for Ca2+ wave formation, which in turn mediates neurite formation in NGF-differentiated PC12 cells. RNAi knockdown of 4.1N attenuated neurite formation and shifted IP3-evoked Ca2+ signaling from waves to homogeneous patterns. RNAi knockdown, dominant-negative binding-region overexpression, confocal live-cell Ca2+ imaging, neurite morphometry in PC12 cells Neuro-Signals Medium 21389686
2013 4.1N interacts with GluK1 and GluK2 kainate receptor subunits through a membrane-proximal C-terminal domain region. This interaction is required for forward trafficking, plasma membrane distribution, and regulated endocytosis of GluK2a receptors. Palmitoylation of GluK2a promotes 4.1N association and surface expression, while PKC activation decreases 4.1N–GluK2/3 interaction in acute brain slices. Co-immunoprecipitation, surface expression assays, endocytosis assays, palmitoylation-deficient and PKC-activation experiments, acute brain slice biochemistry The Journal of biological chemistry High 23400781
2013 4.1N interacts with the α7 acetylcholine receptor. DCP-LA increases the association of α7 AChR with 4.1N in a PKC-dependent manner (without directly phosphorylating 4.1N). 4.1N knockdown suppresses α7 AChR membrane surface localization, and DCP-LA-enhanced membrane surface expression of α7 AChR is prevented by 4.1N knockdown. Yeast two-hybrid, co-immunoprecipitation from rat hippocampal slices, plasma membrane fractionation, α7 AChR surface fluorescence imaging in PC12 cells, siRNA knockdown The Biochemical journal Medium 23256752
2016 4.1N interacts with PP1 (protein phosphatase 1) via its FERM domain, and ectopic 4.1N expression inactivates the JNK–c-Jun signaling pathway by enhancing PP1 activity and PP1–p-JNK interaction, leading to suppression of downstream metastasis targets (ezrin, MMP9) and cell cycle targets (p53, p21, p19) in NSCLC cells. Co-immunoprecipitation, PP1 activity assay, FERM domain deletion mapping, siRNA knockdown and overexpression, xenograft mouse model Oncotarget Medium 26575790
2016 4.1N directly interacts with flotillin-1 through its FERM and U2 domains in NSCLC cells. 4.1N suppresses cell proliferation and migration through a flotillin-1/β-catenin/Wnt signaling pathway. Co-immunoprecipitation, pulldown, domain deletion mapping, siRNA knockdown and overexpression, proliferation and migration assays Tumour biology Medium 27448302
2018 IP6K2 (inositol hexakisphosphate kinase 2) binds 4.1N with high affinity and specificity. Nuclear translocation of 4.1N is dependent on IP6K2. In cerebellar granule cells, the IP6K2–4.1N interaction regulates Purkinje cell morphology, cerebellar synapses, and locomotor function. Disruption of IP6K2–4.1N interactions impairs cell viability. Co-immunoprecipitation, IP6K2 knockout mice, cerebellar histology, synaptic morphology, locomotor behavioral assays, cell viability assay The Journal of neuroscience Medium 30006360
2018 4.1N localizes to the lateral membrane of human bronchial epithelial cells, where it associates with E-cadherin, β-catenin, and βII spectrin. RNAi depletion of 4.1N reduces lateral membrane height; this is rescued by re-expression of mouse 4.1N. 4.1N is required for full lateral membrane assembly but not the initial phase of lateral membrane biogenesis. RNAi knockdown, rescue by re-expression, co-immunoprecipitation, confocal immunofluorescence, lateral membrane height measurement Biochimica et biophysica acta. Biomembranes Medium 29428502
2020 4.1N directly binds 14-3-3 and promotes its degradation in suspension EOC cells, thereby inhibiting anoikis resistance and EMT. Loss of 4.1N leads to EMT in adherent EOC cells and increased anoikis resistance and entosis-based cell death resistance in suspension cells. Co-immunoprecipitation, ubiquitin-proteasome degradation assay, siRNA knockdown, overexpression, xenograft mouse model, in vitro anoikis/entosis assays Protein & cell Medium 32448967
2020 4.1N knockout mice show defects in GnRH localization to hypothalamic axons (restricted to cell bodies only), decreased pituitary secretory granules, and gonadal atrophy with failed spermatogenesis and follicular development, indicating 4.1N is required for the hypothalamus-pituitary-reproductive axis. 4.1N knockout mouse generation, histopathology, immunofluorescence of GnRH localization in hypothalamus, pituitary granule ultrastructure Scientific reports Medium 33046791
2023 CaMKII phosphorylates 4.1N during TBS-induced LTP in rat hippocampal CA1 neurons, and this phosphorylation facilitates assembly of a p-CaMKII–4.1N–GluA1 complex that drives GluA1 trafficking to postsynaptic densities. Disrupting the 4.1N–GluA1 interaction (Tat-GluA1 MPR peptide) or inhibiting CaMKII (Myr-AIP) both attenuated LTP and reduced postsynaptic GluA1, but neither affected basal mEPSCs. Co-immunoprecipitation, immunoblotting for phospho-proteins, interfering peptides (Tat-GluA1 MPR), CaMKII inhibitor (Myr-AIP), LTP electrophysiology in acute hippocampal slices Neuroscience Medium 37993087
2023 4.1N is required for GluA1 intracellular transport and exocytosis during both basal transmission and cLTP in neurons. SAP97 is essential for GluA1 intracellular transport under basal conditions, while 4.1N controls exocytosis basally and both transport and exocytosis during cLTP. Deletion of the GluA1 C-terminal domain fully suppresses intracellular transport. siRNA knockdown of 4.1N and SAP97, live-cell single-molecule imaging of GluA1 trafficking and exocytosis, cLTP induction, total internal reflection fluorescence microscopy eLife High 37079350
2023 4.1N plays a cell type-specific role in hippocampal glutamatergic synapses: knockdown in dentate gyrus (DG) granule neurons reduces glutamatergic synapse number and function, whereas knockdown in CA1 pyramidal neurons has no effect on basal transmission. The FERM domain of 4.1N (not the CTD) is essential for supporting synaptic AMPAR function in DG granule neurons. In vivo/ex vivo stereotaxic viral knockdown of 4.1N, electrophysiology (mEPSC recording), domain-specific rescue (FERM vs. CTD deletion constructs), immunofluorescence synapse counting The Journal of neuroscience High 37845032
2025 A GluA1 C80 peptide that disrupts GluA1–4.1N binding impairs LTP and short-term spatial memory (but not long-term spatial memory) when expressed bilaterally in hippocampal CA1, demonstrating that the 4.1N–GluA1 interaction is required for synaptic plasticity and short-term memory in vivo. Viral expression of interfering GluA1 C80 peptide in dorsal hippocampus CA1, LTP electrophysiology, spatial memory behavioral testing (Morris water maze variants) Neuroscience bulletin Medium 41417164

Source papers

Stage 0 corpus · 32 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2009 Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation. Nature neuroscience 289 19503082
2000 Pike. A nuclear gtpase that enhances PI3kinase activity and is regulated by protein 4.1N. Cell 147 11136977
2002 D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N. Molecular pharmacology 109 12181426
2004 Lateral diffusion of inositol 1,4,5-trisphosphate receptor type 1 is regulated by actin filaments and 4.1N in neuronal dendrites. The Journal of biological chemistry 76 15364918
2002 Protein 4.1N is required for translocation of inositol 1,4,5-trisphosphate receptor type 1 to the basolateral membrane domain in polarized Madin-Darby canine kidney cells. The Journal of biological chemistry 72 12444087
1999 Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor. The Journal of neuroscience : the official journal of the Society for Neuroscience 60 10594058
2007 Differential neuronal and glial expression of GluR1 AMPA receptor subunit and the scaffolding proteins SAP97 and 4.1N during rat cerebellar development. The Journal of comparative neurology 52 17335044
2003 Association of the type 1 inositol (1,4,5)-trisphosphate receptor with 4.1N protein in neurons. Molecular and cellular neurosciences 49 12676536
2005 Nectin-like molecule 1 is a protein 4.1N associated protein and recruits protein 4.1N from cytoplasm to the plasma membrane. Biochimica et biophysica acta 34 15893517
2013 Kainate receptor post-translational modifications differentially regulate association with 4.1N to control activity-dependent receptor endocytosis. The Journal of biological chemistry 32 23400781
2016 Protein 4.1N acts as a potential tumor suppressor linking PP1 to JNK-c-Jun pathway regulation in NSCLC. Oncotarget 23 26575790
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
2020 Loss of 4.1N in epithelial ovarian cancer results in EMT and matrix-detached cell death resistance. Protein & cell 21 32448967
2006 4.1N binding regions of inositol 1,4,5-trisphosphate receptor type 1. Biochemical and biophysical research communications 20 16487933
2023 Regulation of different phases of AMPA receptor intracellular transport by 4.1N and SAP97. eLife 17 37079350
2013 Defective expression of Protein 4.1N is correlated to tumor progression, aggressive behaviors and chemotherapy resistance in epithelial ovarian cancer. Gynecologic oncology 17 23994105
2018 Inositol Hexakisphosphate Kinase-2 in Cerebellar Granule Cells Regulates Purkinje Cells and Motor Coordination via Protein 4.1N. The Journal of neuroscience : the official journal of the Society for Neuroscience 16 30006360
2012 The membrane-cytoskeletal protein 4.1N is involved in the process of cell adhesion, migration and invasion of breast cancer cells. Experimental and therapeutic medicine 15 23170136
2016 4.1N is involved in a flotillin-1/β-catenin/Wnt pathway and suppresses cell proliferation and migration in non-small cell lung cancer cell lines. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 14 27448302
2011 The type I inositol 1,4,5-trisphosphate receptor interacts with protein 4.1N to mediate neurite formation through intracellular Ca waves. Neuro-Signals 14 21389686
2005 Protein 4.1N does not interact with the inositol 1,4,5-trisphosphate receptor in an epithelial cell line. Cell calcium 10 16122796
2021 4.1N-Mediated Interactions and Functions in Nerve System and Cancer. Frontiers in molecular biosciences 9 34589518
2022 Tumor Suppressor 4.1N/EPB41L1 is Epigenetic Silenced by Promoter Methylation and MiR-454-3p in NSCLC. Frontiers in genetics 8 35795202
2019 Mechanism of microRNA-431-5p-EPB41L1 interaction in glioblastoma multiforme cells. Archives of medical science : AMS 7 31749885
2013 The linoleic acid derivative DCP-LA increases membrane surface localization of the α7 ACh receptor in a protein 4.1N-dependent manner. The Biochemical journal 7 23256752
2018 Protein 4.1N is required for the formation of the lateral membrane domain in human bronchial epithelial cells. Biochimica et biophysica acta. Biomembranes 6 29428502
2015 4.1N suppresses hypoxia-induced epithelial-mesenchymal transition in epithelial ovarian cancer cells. Molecular medicine reports 6 26648170
2023 Phosphorylation of 4.1N by CaMKII Regulates the Trafficking of GluA1-containing AMPA Receptors During Long-term Potentiation in Acute Rat Hippocampal Brain Slices. Neuroscience 4 37993087
2020 Selective effects of protein 4.1N deficiency on neuroendocrine and reproductive systems. Scientific reports 3 33046791
2019 Correction: Protein 4.1N acts as a potential tumor suppressor linking PP1 to JNK-c-Jun pathway regulation in NSCLC. Oncotarget 2 31692885
2025 GluA1 C80 Peptide Impairs Short-Term Spatial Memory in Mice by Interfering with the 4.1N Binding Site. Neuroscience bulletin 1 41417164
2023 Protein 4.1N Plays a Cell Type-Specific Role in Hippocampal Glutamatergic Synapse Regulation. The Journal of neuroscience : the official journal of the Society for Neuroscience 1 37845032

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