APOE
Gene Ontology Biological Process
- G-protein coupled receptor signaling pathway [IDA]
- N-methyl-D-aspartate receptor clustering [IDA]
- alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering [IDA]
- cGMP-mediated signaling [IDA]
- cholesterol efflux [IDA]
- cholesterol homeostasis [IDA]
- cholesterol metabolic process [IDA, IMP]
- chylomicron remnant clearance [IMP]
- cytoskeleton organization [TAS]
- fatty acid homeostasis [IDA]
- high-density lipoprotein particle assembly [IDA]
- high-density lipoprotein particle clearance [IDA]
- high-density lipoprotein particle remodeling [IGI]
- intracellular transport [TAS]
- lipoprotein metabolic process [TAS]
- long-chain fatty acid transport [IDA]
- negative regulation of MAP kinase activity [IDA]
- negative regulation of beta-amyloid formation [IDA]
- negative regulation of blood coagulation [IDA]
- negative regulation of blood vessel endothelial cell migration [IDA]
- negative regulation of cholesterol biosynthetic process [IDA]
- negative regulation of cholesterol efflux [IDA]
- negative regulation of dendritic spine development [IDA]
- negative regulation of dendritic spine maintenance [IDA]
- negative regulation of endothelial cell proliferation [IDA]
- negative regulation of inflammatory response [IC]
- negative regulation of lipid biosynthetic process [IDA]
- negative regulation of lipid transport across blood brain barrier [IDA]
- negative regulation of neuron death [IDA]
- negative regulation of phospholipid efflux [IDA]
- negative regulation of platelet activation [IDA]
- negative regulation of postsynaptic membrane organization [IDA]
- negative regulation of presynaptic membrane organization [IDA]
- nitric oxide mediated signal transduction [IDA]
- phospholipid efflux [IDA]
- phototransduction, visible light [TAS]
- positive regulation of beta-amyloid formation [IDA]
- positive regulation of cGMP biosynthetic process [IDA]
- positive regulation of cholesterol efflux [IDA, IGI]
- positive regulation of cholesterol esterification [IDA]
- positive regulation of dendritic spine development [IDA]
- positive regulation of dendritic spine maintenance [IDA]
- positive regulation of lipid biosynthetic process [IDA]
- positive regulation of lipid transport across blood brain barrier [IDA]
- positive regulation of low-density lipoprotein particle receptor catabolic process [IDA]
- positive regulation of membrane protein ectodomain proteolysis [IDA]
- positive regulation of neurofibrillary tangle assembly [IDA]
- positive regulation of neuron death [IDA]
- positive regulation of nitric-oxide synthase activity [IDA]
- positive regulation of phospholipid efflux [IDA]
- positive regulation of postsynaptic membrane organization [IDA]
- positive regulation of presynaptic membrane organization [IDA]
- protein import [IDA]
- receptor-mediated endocytosis [IDA]
- regulation of Cdc42 protein signal transduction [IDA]
- regulation of axon extension [TAS]
- regulation of beta-amyloid clearance [IDA]
- regulation of neuron death [IDA]
- regulation of neuronal synaptic plasticity [TAS]
- regulation of tau-protein kinase activity [IDA]
- response to reactive oxygen species [NAS]
- retinoid metabolic process [TAS]
- reverse cholesterol transport [IDA]
- small molecule metabolic process [TAS]
- synaptic transmission, cholinergic [TAS]
- triglyceride metabolic process [IDA, IMP]
- very-low-density lipoprotein particle clearance [IDA, IMP]
- very-low-density lipoprotein particle remodeling [IDA, IGI]
Gene Ontology Molecular Function- antioxidant activity [IDA]
- beta-amyloid binding [IDA]
- heparin binding [IDA]
- identical protein binding [IDA]
- lipid binding [IDA]
- lipid transporter activity [IDA]
- low-density lipoprotein particle receptor binding [IDA, IPI]
- metal chelating activity [IDA]
- phosphatidylcholine-sterol O-acyltransferase activator activity [IDA]
- phospholipid binding [IDA]
- protein binding [IPI]
- protein homodimerization activity [IPI]
- tau protein binding [IPI]
- very-low-density lipoprotein particle receptor binding [IDA, IPI]
- antioxidant activity [IDA]
- beta-amyloid binding [IDA]
- heparin binding [IDA]
- identical protein binding [IDA]
- lipid binding [IDA]
- lipid transporter activity [IDA]
- low-density lipoprotein particle receptor binding [IDA, IPI]
- metal chelating activity [IDA]
- phosphatidylcholine-sterol O-acyltransferase activator activity [IDA]
- phospholipid binding [IDA]
- protein binding [IPI]
- protein homodimerization activity [IPI]
- tau protein binding [IPI]
- very-low-density lipoprotein particle receptor binding [IDA, IPI]
Gene Ontology Cellular Component
- blood microparticle [IDA]
- chylomicron [IDA]
- cytoplasm [NAS, TAS]
- dendrite [NAS]
- early endosome [TAS]
- endocytic vesicle lumen [TAS]
- extracellular matrix [IDA]
- extracellular region [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- high-density lipoprotein particle [IDA]
- intermediate-density lipoprotein particle [IDA]
- low-density lipoprotein particle [IDA]
- membrane [IDA]
- neuronal cell body [NAS]
- nucleus [IDA]
- plasma membrane [TAS]
- very-low-density lipoprotein particle [IDA]
- vesicle [IDA]
LRP8
Gene Ontology Biological Process
- ammon gyrus development [ISS]
- blood coagulation [TAS]
- cytokine-mediated signaling pathway [NAS]
- endocytosis [IDA]
- lipid metabolic process [NAS]
- negative regulation of transcription from RNA polymerase II promoter [ISS]
- phototransduction, visible light [TAS]
- positive regulation of CREB transcription factor activity [ISS]
- positive regulation of dendrite development [ISS]
- positive regulation of dendritic spine morphogenesis [ISS]
- positive regulation of peptidyl-tyrosine phosphorylation [ISS]
- positive regulation of protein tyrosine kinase activity [ISS]
- proteolysis [NAS]
- receptor-mediated endocytosis [IDA]
- reelin-mediated signaling pathway [ISS]
- regulation of synaptic transmission [ISS]
- retinoid metabolic process [TAS]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Domains of apoE required for binding to apoE receptor 2 and to phospholipids: implications for the functions of apoE in the brain.
We have studied the contribution of the carboxy terminal domains of lipid-free apoE isolated from apoE-expressing cell cultures in binding to phospholipids and have determined the affinities of reconstituted POPC-apoE particles for the apoER2. It was found that the initial rate of association of apoE2, apoE3, apoE4, and a mutant form apoE4R158M to multilamellar DMPC vesicles was similar and was ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| LRP8 APOE | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID