| 2005 |
ApoER2 is present in postsynaptic densities of excitatory synapses where it forms a functional complex with NMDA receptors. Reelin signaling through ApoER2 enhances LTP through a mechanism requiring amino acids encoded by an alternatively spliced exon (exon 19) in the intracellular domain, which is required for Reelin-induced tyrosine phosphorylation of NMDA receptor subunits. |
Co-immunoprecipitation, postsynaptic density fractionation, alternative splicing analysis, LTP electrophysiology, behavioral learning/memory tasks in knock-in mice |
Neuron |
High |
16102539
|
| 2000 |
ApoER2, but not VLDLR, binds JNK-interacting proteins (JIP-1 and JIP-2), which act as molecular scaffolds for the JNK signaling pathway. The ApoER2 binding domain on JIP-2 does not overlap with binding sites for MLK3, MKK7, and JNK, allowing ApoER2 to assemble a multiprotein complex containing Disabled-1 and JIPs at the neuronal cell surface. |
Co-immunoprecipitation, yeast two-hybrid, domain mapping |
The Journal of biological chemistry |
Medium |
10827199
|
| 2003 |
Purified Reelin binds directly to ApoER2 and VLDLR to induce tyrosine phosphorylation of Disabled-1 (Dab1). ApoER2 shows greater Reelin-binding affinity than VLDLR. Complete absence of both receptors abolishes Reelin-induced Dab1 phosphorylation in cortical neurons. |
Purified Reelin binding assay, Dab1 phosphorylation immunoblot, genetic knockout mice, cortical neuron cultures |
Brain research. Molecular brain research |
High |
12670700
|
| 2007 |
PCSK9 induces degradation of ApoER2 (as well as LDLR and VLDLR) either via cellular co-expression or re-internalization of secreted PCSK9. This degradation does not require PCSK9 catalytic activity and is directed to late endosomes/lysosomes. Membrane-bound PCSK9 chimeras are more efficient at degrading ApoER2 than secreted PCSK9. |
Cell co-expression, secreted protein re-internalization, lysosomal targeting assays, catalytically inactive mutant PCSK9, immunoblotting |
The Journal of biological chemistry |
High |
18039658
|
| 2007 |
ApoER2 mediates selenium uptake from selenoprotein P (Sepp1) in the mouse testis. Sertoli cells express ApoER2 as the Sepp1 receptor; apoER2-deficient males show sharply reduced testis selenium and identical sperm defects to Sepp1-deficient males. Co-immunoprecipitation confirmed ApoER2-Sepp1 interaction. |
Sepp1 affinity chromatography, mass spectrometry, co-immunoprecipitation, ApoER2 knockout mice, in situ hybridization, immunocytochemistry, selenium measurement |
The Journal of biological chemistry |
High |
17314095
|
| 2008 |
ApoER2 and Dab1 are required for postnatal chain migration of neuronal precursors from the subventricular zone to the olfactory bulb in a Reelin-independent manner. Mice lacking both ApoER2 and VLDLR, or Dab1, showed severely compromised chain formation and virtual absence of the rostral migratory stream. |
Genetic knockout mice, organotypic migration assay, immunohistochemistry, neuroanatomical analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
17494763
|
| 2008 |
Thrombospondin-1 (THBS-1) is a novel physiological ligand for ApoER2 and VLDLR. THBS-1 binds ApoER2 and VLDLR and induces phosphorylation of Dab1 but, unlike Reelin, does not induce Dab1 degradation or Akt phosphorylation. THBS-1 stabilizes neuronal precursor chains in the rostral migratory stream. |
Ligand binding assay, Dab1 phosphorylation immunoblot, THBS-1 knockout mice, subventricular zone explant cultures |
The EMBO journal |
High |
18946489
|
| 2005 |
F-spondin interacts with ApoER2 through its thrombospondin domain binding to the ApoER2 ligand-binding domain. Full-length F-spondin increases ApoER2-APP co-immunoprecipitation, increases surface expression of both, promotes cleavage of APP and ApoER2, and decreases Aβ production in a RAP-inhibitable manner. |
Co-immunoprecipitation, surface biotinylation, RAP-inhibition assay, cell transfection, primary neuron cultures |
Molecular and cellular biology |
Medium |
16227578
|
| 2008 |
Activated protein C (APC) binds directly and with high affinity (Kd ~30 nM) to ApoER2 (but not VLDLR) via a surface plasmon resonance-measured interaction. APC ligation of ApoER2 induces rapid phosphorylation of Dab1 Tyr-220 and Akt Ser-473, with downstream GSK3β Ser-9 phosphorylation via PI3K. siRNA knockdown of ApoER2 abolishes APC-induced Dab1 phosphorylation. |
Surface plasmon resonance, siRNA knockdown, phospho-specific immunoblotting, PI3K inhibitor, RAP blocking |
Proceedings of the National Academy of Sciences of the United States of America |
High |
19116273
|
| 2010 |
The E3 ubiquitin ligase IDOL induces ubiquitination of ApoER2 and VLDLR on their cytoplasmic tails, leading to their degradation. LXR activation increases IDOL expression and decreases VLDLR levels in vivo. LXR activation reduces Reelin binding to VLDLR and Dab1 phosphorylation, functionally linking LXR and Reelin signaling. |
Ubiquitination assay, cell overexpression, siRNA knockdown, pharmacological LXR activation in mice, Dab1 phosphorylation immunoblot |
The Journal of biological chemistry |
High |
20427281
|
| 2010 |
Antiphospholipid antibodies (aPL) promote leukocyte-endothelial adhesion and thrombosis through ApoER2-dependent antagonism of eNOS. The mechanism involves β2GPI dimerization leading to attenuated eNOS Ser1179 phosphorylation via protein phosphatase 2A. ApoER2-/- mice are protected from aPL inhibition of eNOS, leukocyte adhesion, and thrombus formation in vivo. |
ApoER2 knockout mice, in vivo carotid conductance assay, eNOS phosphorylation immunoblot, PP2A activity assay, monocyte adhesion assay |
The Journal of clinical investigation |
High |
21123944
|
| 2012 |
ApoER2 (LRP8) on endothelial cells serves as the receptor for cancer-secreted ApoE to suppress metastatic endothelial recruitment (MER) and angiogenesis. ApoE engagement of endothelial LRP8 (not LRP1) suppresses angiogenesis, and miRNAs that suppress ApoE promote metastasis via this pathway. |
In vivo selection, siRNA knockdown, locked nucleic acid miRNA inhibition, endothelial recruitment assays, xenograft metastasis models |
Cell |
Medium |
23142051
|
| 2012 |
PCSK9 potentiates neuronal apoptosis by reducing ApoER2 protein levels. RNAi-mediated knockdown of PCSK9 increases ApoER2 levels and reduces neuronal apoptosis; knockdown of ApoER2 (but not VLDLR) reverses this protection. PCSK9 regulates neuronal apoptosis via ApoER2-associated ERK and JNK signaling independently of NMDA receptor function. |
RNAi knockdown, apoptosis assays (caspase-3, p-c-Jun), pharmacological signaling pathway inhibition, cerebellar granule neuron culture |
Cellular and molecular life sciences : CMLS |
Medium |
22481440
|
| 2005 |
ApoER2 undergoes endocytosis via a clathrin-mediated pathway dependent on its cytoplasmic FxNPXY motif, which mediates binding to the adaptor protein Dab2. Dominant-negative eps15 and Dab2 decrease ApoER2 internalization. Lipid raft association of ApoER2 does not determine its endocytic pathway. |
Dominant-negative expression, nystatin treatment, clathrin inhibition, receptor internalization assay, co-immunoprecipitation with Dab2 |
Traffic (Copenhagen, Denmark) |
Medium |
16101684
|
| 2009 |
ApoER2 and VLDLR have divergent receptor fates upon Reelin stimulation linked to their differential sorting to raft vs. non-raft membrane domains. VLDLR (non-raft) endocytoses and degrades Reelin via clathrin/endosome pathway without receptor degradation. ApoER2 (raft-resident) generates specific receptor fragments and is degraded via lysosomes, contributing to negative feedback loops. |
Chimeric receptor constructs, lipid raft fractionation, Reelin endocytosis assay, lysosomal degradation assay, immunoblotting |
The Journal of biological chemistry |
Medium |
19948739
|
| 2009 |
Coagulation factor XI (FXI) is a ligand for platelet ApoER2. Platelet adhesion to FXI is abrogated by soluble recombinant ApoER2, RAP, or LDL-binding domain 1 or 2 of ApoER2. ApoER2-deficient murine platelets fail to adhere to FXI. Soluble FXI binds immobilized ApoER2 with an affinity of 61 nM. |
Platelet adhesion assay, ApoER2-deficient mice, surface plasmon resonance binding measurement, RAP inhibition, recombinant domain deletion mutants |
Arteriosclerosis, thrombosis, and vascular biology |
High |
19661487
|
| 2005 |
β2-Glycoprotein I (β2GPI) binds platelet ApoER2 via domain V of dimeric β2GPI. Domain V deletion mutants lacking the phospholipid-insertion loop fail to bind ApoER2 or increase platelet adhesion to collagen, while domain I and II deletion mutants retain ApoER2 binding. |
Domain deletion mutants of β2GPI, immunoprecipitation, platelet adhesion assay in whole blood |
The Journal of biological chemistry |
Medium |
16091370
|
| 2012 |
ApoER2 (LRP8) mediates Wnt/β-catenin signaling and controls osteoblast differentiation. LRP8 knockdown decreases β-catenin levels and suppresses Wnt-induced Axin2 transcription and osteoblast mineralization; LRP8 ectopic expression promotes Wnt-induced β-catenin accumulation and osteoblast differentiation. |
siRNA knockdown, ectopic overexpression, Wnt reporter assay, immunoblotting for β-catenin, osteoblast differentiation assay, KS483 osteoprogenitor cells |
Journal of bone and mineral research |
Medium |
22589174
|
| 2015 |
Reelin binding to LRP8 triggers activation of a cohort of neuronal enhancers (LRN enhancers) via a synapse-to-nucleus pathway. This requires γ-secretase-dependent cleavage of LRP8 releasing its intracellular domain (ICD), which regulates synaptically generated signals. LRP8 ICD participates in transcriptional regulation of synaptic plasticity genes underlying memory formation. |
In vivo ChIP-seq enhancer mapping, γ-secretase inhibition, LRP8 ICD nuclear fractionation, mouse learning/memory behavioral assays, NMDA-receptor signaling assays |
Neuron |
High |
25892301
|
| 2014 |
Sorting nexin 17 (SNX17) interacts with the NPxY endocytosis motif of ApoER2 via its FERM domain and stimulates ApoER2 recycling from early to recycling endosomes without affecting endocytic rate. SNX17 knockdown increases Reelin-induced ApoER2 degradation and reduces dendritic tree development and Reelin signaling in hippocampal neurons. |
GST pull-down, co-immunoprecipitation, ApoER2 recycling assay, siRNA knockdown, neuronal culture morphology, Dab1 phosphorylation assay |
PloS one |
Medium |
24705369
|
| 2013 |
Clusterin binds directly to ApoER2 and VLDLR and is internalized by cells expressing either receptor. Clusterin binding triggers a Reelin-like signal, inducing Dab1 phosphorylation and PI3K/Akt and n-cofilin activation. Blocking clusterin in SVZ explants compromises cell proliferation and neuroblast chain formation. |
Ligand binding/internalization assay, Dab1 phosphorylation immunoblot, PI3K/Akt immunoblot, SVZ explant culture, clusterin blocking antibody |
The Journal of biological chemistry |
Medium |
24381170
|
| 2014 |
Apoer2 lacking exon 16 (O-linked sugar domain) shows reduced extracellular cleavage and consequently impaired γ-secretase-dependent release of the ApoER2 intracellular domain. Mice expressing this variant show increased ApoER2 abundance, altered hippocampal spine density, glutamate receptor abundance, and synaptic efficacy. |
Knock-in mice, proteolytic cleavage assay, spine density quantification, glutamate receptor immunoblot, hippocampal LTP electrophysiology, behavioral tests |
Science signaling |
High |
25429077
|
| 2013 |
Presenilin 1 (PS1)/γ-secretase processes ApoER2 to generate an intracellular C-terminal fragment (CTF). The ApoER2 CTF binds to the RELN promoter region and suppresses reelin transcription at the transcriptional level. PS1 conditional knockout mice show increased ApoER2 and reelin protein levels. |
PS1 conditional knockout mice, luciferase reporter assay, nuclear fractionation, chromatin immunoprecipitation (ChIP), pharmacological γ-secretase inhibition |
FASEB journal |
High |
24344333
|
| 2017 |
ApoER2 ectodomain adopts an intermediate contracted-open conformation when complexed with the signaling-competent Reelin fragment at neutral pH, different from LDLR. Crystallographic analysis identifies an auxiliary low-affinity binding interface; pH shift during endocytosis weakens this auxiliary interface and destabilizes the ligand-receptor complex, priming ligand release prior to internalization. |
X-ray crystallography of full-length ApoER2 ectodomain-Reelin fragment complex, mutational analysis, pH-dependent binding assays |
EMBO reports |
High |
28446613
|
| 2018 |
The apoER2 cytoplasmic tail serves as a scaffold for aPL-induced assembly and activation of heterotrimeric PP2A in endothelial cells. Dab2 recruitment to the apoER2 NPXY motif promotes activating L309 methylation of the PP2A catalytic subunit by leucine methyl transferase-1. SHC1 recruits PP2A scaffolding subunit to the proline-rich apoER2 C-terminus, mediating inhibitory dephosphorylation of Akt and eNOS. This apoER2-Dab2-SHC1 complex underlies aPL-invoked thrombosis in mice. |
Co-immunoprecipitation, endothelial cell PP2A activity assay, site-specific mutational analysis of apoER2 domains, mouse thrombosis model, apoER2 knockout mice |
Blood |
High |
29500169
|
| 2019 |
ApoER2 participates in APC (anaphase-promoting complex)/CDC20 complex formation during mitosis. In apoER2-deficient smooth muscle cells, PP2A-C fails to interact with CDC20, resulting in inactive APC and impaired cytokinesis abscission, leading to cell cycle arrest at metaphase/anaphase and premature cell senescence. |
Co-immunoprecipitation of apoER2 with PP2A catalytic subunit and CDC20, cell cycle protein immunoblotting, β-galactosidase senescence assay, p16INK4a immunofluorescence, Lrp8 knockout mice |
Arteriosclerosis, thrombosis, and vascular biology |
Medium |
31412739
|
| 2009 |
The signaling motifs in the Apoer2 cytoplasmic domain are functionally dissociable from Sepp1 (selenoprotein P) uptake. Knock-in mice with signaling-impaired Apoer2 cytoplasmic domain mutations have normal brain and testis selenium concentrations, demonstrating that neurological defects in these mice result from disrupted Reelin signaling, not impaired selenium uptake. |
Knock-in mice with cytoplasmic domain mutations, selenium concentration measurement in tissues, neurological phenotyping, sperm motility analysis |
Biological chemistry |
High |
19007311
|
| 2012 |
Long isoform selenoprotein P (Sepp1) is taken up by L8 myoblast cells via an apoER2-mediated mechanism requiring binding to heparin sulfate proteoglycans. siRNA knockdown of apoER2 (but not Lrp1) inhibits 75Se uptake from Sepp1. Lysosomal acidification is required for Sepp1 digestion and selenium utilization but not for Sepp1 uptake itself. |
siRNA knockdown, 75Se radiolabeled uptake assay, affinity chromatography with mass spectrometry, protamine/chlorate treatment, lysosomal acidification inhibition |
The Journal of biological chemistry |
High |
22761431
|
| 2006 |
FE65 interacts with ApoER2 via its N-terminal PTB domain, acting as an intracellular bridge between ApoER2 and APP. Full-length FE65 increases surface expression of ApoER2, increases secreted APP and ApoER2 forms, and decreases Aβ production. Both PTB domains of FE65 must be present simultaneously for effects on APP/ApoER2 processing. |
Co-immunoprecipitation, surface protein biotinylation, live cell staining, COS7 cell transfection, Aβ ELISA |
The Journal of biological chemistry |
Medium |
16638748
|
| 2007 |
ApoER2 expression increases APP association with lipid rafts, promotes gamma-secretase activity, and increases Aβ production while decreasing APP internalization. The increased Aβ production is dependent on the integrity of the NPxY endocytosis motif of ApoER2. ApoER2 physically interacts and co-localizes with APP. |
Co-immunoprecipitation, APP internalization rate assay, lipid raft fractionation, gamma-secretase activity assay, Aβ ELISA, NPxY motif mutagenesis |
Molecular neurodegeneration |
Medium |
17620134
|
| 2014 |
ApoE3 binding to ApoER2 stimulates eNOS, promotes endothelial cell migration, and attenuates monocyte-endothelial adhesion in endothelial cells. ApoE4 does not stimulate eNOS or migration and selectively antagonizes ApoE3/ApoER2 actions, requiring the N-terminal to C-terminal interaction that distinguishes ApoE4 from ApoE3. The LRP8 R952Q variant is a loss-of-function variant of ApoER2 in endothelium; ApoER2-/- mice show decreased carotid reendothelialization and exaggerated neointima formation. |
eNOS activity assay, endothelial cell migration assay, monocyte adhesion assay, ApoER2 knockout mouse carotid reendothelialization, neointima formation model, adenoviral apoE expression |
Proceedings of the National Academy of Sciences of the United States of America |
High |
25197062
|
| 2017 |
The E3 ubiquitin ligase IDOL determines synaptic ApoER2 protein levels in response to neuronal activation and regulates dendritic spine morphogenesis. IDOL-dependent ApoER2 ubiquitination modulates filopodia initiation and synapse maturation. IDOL knockout in neurons causes ApoER2 overexpression, impaired activity-dependent spine remodeling, and defective LTP. |
IDOL knockout neurons, ApoER2 protein level immunoblot, dendritic spine imaging, hippocampal LTP electrophysiology, experience-dependent barrel cortex plasticity assay, learning/memory behavioral tests |
eLife |
High |
28891791
|
| 2017 |
GRIP1 binds ApoER2 and bridges a complex including ApoER2, ephrinB2, and AMPA receptors at the postsynapse. Neuronal activity induces ApoER2-ephrinB2 association; phosphorylation of ephrinB2 Ser-9 is essential for complex stability. In vivo mutation of ephrinB2 Ser-9 disrupts the complex, eliminates ApoER2 downstream signaling, and impairs activity-induced AMPA receptor insertion and LTP. |
Co-immunoprecipitation, knock-in ephrinB2 Ser-9 mutant mice, AMPA receptor surface insertion assay, hippocampal LTP electrophysiology, compound genetics |
Cell reports |
High |
28978486
|
| 2016 |
Antisense oligonucleotide (ASO)-mediated correction of ApoER2 exon 19 splicing in Alzheimer's disease mice improves synaptic function and learning/memory. The balance of ApoER2 exon 19 splicing is deregulated in AD patient postmortem brain tissue. Exon 19 is required for ApoER2 signaling. |
ASO treatment in AD transgenic mice, splice variant analysis in human postmortem brain, synaptic function electrophysiology, Morris water maze behavioral testing |
EMBO molecular medicine |
Medium |
26902204
|
| 2016 |
Presenilin-1 (PS1) mutations alter ApoER2 processing and trafficking. PS1 mutation R278I impairs γ-secretase cleavage of ApoER2 at baseline and after Reelin treatment. PS1 L282V mutation reduces cell-surface levels of ApoER2 without affecting total levels, indicating a trafficking defect. PS1 M146V permits accumulation of ApoER2 CTFs after Reelin treatment. |
PS1 mutant cell lines, ApoER2 CTF immunoblot, cell-surface protein biotinylation, γ-secretase inhibitor treatment, Reelin stimulation |
Neurobiology of aging |
Medium |
27810638
|
| 2015 |
ApoER2 and Reelin are expressed in regenerating peripheral nerves and regulate Schwann cell migration. Reelin activates Rac1 at the leading edge of Schwann cells (detected by FRET). ApoER2 exon-19-containing splice variant (with proline-rich insert) binds PAR3. Tiam1, a Rac1-specific GEF, is required for Reelin-induced Schwann cell migration, and PAR3 associates with Tiam1 and ApoER2. |
FRET experiments for Rac1 activation, co-immunoprecipitation of ApoER2-PAR3, siRNA knockdown of Tiam1/PAR3/ApoER2, Schwann cell migration assay, peripheral nerve injury model |
Molecular and cellular neurosciences |
Medium |
26386179
|
| 2019 |
ApoER2 homo- and hetero-oligomers are formed in the absence of Reelin. Full-length Reelin binding rearranges ApoER2 homo-oligomers into higher-order receptor clusters, which leads to Dab1 phosphorylation. Binding of the central Reelin fragment does not increase cluster size and does not induce Dab1 phosphorylation, but can induce ApoER2 hetero-oligomerization with VLDLR without triggering the canonical signal. |
Time-resolved fluorescence anisotropy, fluorescence lifetime imaging microscopy (FLIM), FRET, HEK293 cells expressing tagged receptors |
Frontiers in molecular neuroscience |
Medium |
30873003
|
| 2021 |
VLDLR and ApoER2 (LRP8) are functional entry receptors for multiple alphaviruses including Semliki forest virus, eastern equine encephalitis virus, and Sindbis virus. The alphavirus E2-E1 glycoproteins interact with the ligand-binding domains of VLDLR and ApoER2. VLDLR LBD-Fc fusion protein blocks virus infection in cell culture and protects mice from lethal challenge. |
Ectopic receptor expression facilitating viral entry, virus-like particle internalization assay, LBD-Fc blocking experiments, mouse lethal challenge model |
Nature |
High |
34929721
|
| 2023 |
LRP8 is a key determinant protecting MYCN-amplified neuroblastoma cells from ferroptosis by mediating selenoprotein P (SELENOP) uptake to supply selenocysteine required for GPX4 translation. Genetic deletion of LRP8 causes ferroptosis due to insufficient selenocysteine supply; this dependency is specific to cells with low expression of alternative selenium uptake pathways (system Xc-). |
CRISPR activation screen, LRP8 knockout (constitutive and inducible) in orthotopic xenografts, ferroptosis assays, GPX4 immunoblot, selenium uptake assay |
EMBO molecular medicine |
High |
37435859
|
| 2009 |
Splice variants of ApoER2 with different numbers of ligand-binding type A (LA) repeats (LA1237 vs. LA12378) differ in Reelin-binding affinity. LA8 and Reelin repeat 8 (RR8) interfere with the interaction between the central Reelin fragment and ApoER2. Proteolytic cleavage of Reelin and alternative splicing of ApoER2 contribute to fine regulation of Reelin signaling. |
Quantitative binding assay between Reelin isoforms/fragments and ApoER2 splice variants, monoclonal antibody specificity, primary cortical neuron signaling assays |
Neuroscience research |
Medium |
19167437
|
| 2025 |
LRP8 is a receptor for tick-borne encephalitis virus (TBEV). LRP8 downregulation reduces TBEV infection in human cells and overexpression enhances it. LRP8 binds directly to the TBEV E glycoprotein and mediates viral attachment and internalization. An LRP8-based soluble decoy blocked TBEV infection in human cell lines and neuronal cells and protected mice from lethal challenge. |
Genome-scale CRISPR-Cas9 screen, LRP8 overexpression/knockdown, direct LRP8-E glycoprotein binding assay, viral attachment/internalization assay, LRP8 soluble decoy in cell culture and mouse lethal challenge |
Nature |
High |
40993380
|
| 2014 |
NGF-induced TrkA activation in PC12 cells induces ApoER2 proteolytic processing via metalloproteinase activity, independently of MAPK and PI3K. In primary cortical neurons, BDNF (TrkB ligand) also regulates ApoER2 proteolysis. Reelin regulates proteolysis of its own receptor ApoER2 but does not affect p75NTR processing. |
TrkA/TrkB activation in cell lines and primary neurons, metalloproteinase inhibitors, MAPK/PI3K pharmacological inhibition, ApoER2 shedding/CTF immunoblot |
BMC neuroscience |
Medium |
25233900
|
| 2022 |
Human APOER2 isoforms lacking different numbers of ligand-binding repeats generate differential amounts of C-terminal fragments (CTFs) in response to ApoE peptide. Isoform Δex5-8 generates the highest CTF; Δex4-6 generates the lowest. Differential CTF generation correlates with proteolytic release of the transcriptionally active ICD (mediated via Mint1 adaptor). Loss of mouse Apoer2 decreases miniature excitatory event frequency; rescue with human APOER2-FL or Δex4-6 (but not Δex5-8) restores this frequency. |
Identification of 25 human APOER2 isoforms by gene-specific PCR sequencing, CTF immunoblot, ICD nuclear fractionation, Mint1 interaction assay, Apoer2 knockout neurons with lentiviral rescue, miniature EPSC recordings |
The Journal of neuroscience |
Medium |
35414534
|
| 2023 |
An ApoER2 variant with a highly glycosylated O-linked sugar domain has a high affinity for SeP (Kd = 0.67 nM) in Jurkat cells. This high-affinity variant mediates selenium transport via SeP through a selenocysteine lyase-independent pathway, in contrast to the Sec lyase-dependent degradation pathway in low-affinity cells. Acidification of intracellular vesicles is necessary for selenium transport via SeP in both cell types. |
ApoER2 variant characterization, SeP binding affinity measurement, siRNA knockdown, 75Se uptake assay, selenocysteine lyase inhibition, lysosomal acidification inhibition |
The Journal of biological chemistry |
Medium |
37406814
|
| 2013 |
Dab1 mediates colocalization of multi-adaptor CIN85 with ApoER2 in neurons. Stimulation with active Reelin fragment recruits CIN85 to plasma membrane domains where it colocalizes with ApoER2 and Dab1, then moves to EEA1-labeled early endosomes. Tyrosine phosphorylation of Dab1 strengthens its binding to CIN85. |
Co-immunoprecipitation, immunofluorescence colocalization, Reelin stimulation, endosome marker co-localization, phospho-Dab1 binding assay |
Genes to cells |
Medium |
23506116
|
| 2021 |
ApoER2 (apoER2) activation by PP2A in trophoblasts driven by antiphospholipid antibodies promotes preeclampsia in a mouse model of antiphospholipid syndrome, demonstrating ApoER2-PP2A signaling in trophoblasts as a mechanistic driver of preeclampsia pathogenesis. |
Mouse model of antiphospholipid syndrome, trophoblast-specific genetic approaches, PP2A activity assays, preeclampsia phenotypic readouts |
Circulation research |
Medium |
34404233
|