Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
Reelin is a ligand for lipoprotein receptors.
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Reelin directly binds VLDLR and ApoER2 and links receptor engagement to DAB1 signaling.
"A signaling pathway involving the extracellular protein Reelin and the intracellular adaptor protein Disabled-1 (Dab1) controls cell positioning during mammalian brain development."
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Reelin directly binds its canonical lipoprotein-family receptors.
"Here, we demonstrate that Reelin binds directly to lipoprotein receptors, preferably the very low-density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2)."
Functional importance of covalent homodimer of reelin protein linked via its central region.
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Cys2101 links the minimum covalent reelin homodimer and this architecture is required for full signaling.
"Detailed analysis of tryptic fragments produced from the purified reelin proteins revealed that the minimum unit of the multimer is a homodimeric reelin linked via Cys(2101) present in the central region"
The functions of Reelin in membrane trafficking and cytoskeletal dynamics: implications for neuronal migration, polarization and differentiation.
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Canonical reelin signaling is receptor- and DAB1-dependent and branches into cytoskeletal and trafficking pathways.
"Reelin signaling involves a core pathway that activates upon reelin binding to its receptors, particularly ApoER2 (apolipoprotein E receptor 2)/LRP8 (low-density lipoprotein receptor-related protein 8) and very low-density lipoprotein receptor, followed by Src/Fyn-mediated phosphorylation of the adaptor protein Dab1 (Disabled-1)."
MatrisomeDB 2.0: 2023 updates to the ECM-protein knowledge database.
FYN phosphorylates DAB1 in RELN:VLDLR:DAB1:SH3KBP1
RELN:VLDLR:DAB1 binds SH3KBP1
Binding of purified Reelin to ApoER2 and VLDLR mediates tyrosine phosphorylation of Disabled-1.
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ApoER2 and VLDLR are essential canonical receptors for Reelin-induced DAB1 phosphorylation.
"These findings demonstrate that ApoER2 and VLDLR are essential for Reelin signaling and that no other receptor molecules can compensate for their role in mediating tyrosine phosphorylation of Dab1."
Autosomal recessive lissencephaly with cerebellar hypoplasia is associated with human RELN mutations.
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Biallelic human RELN mutations reduce reelin and cause lissencephaly with cerebellar and other brain abnormalities.
"The mutations disrupt splicing of RELN cDNA, resulting in low or undetectable amounts of reelin protein."
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Human reelin is a large secreted receptor-binding protein.
"RELN encodes a large (388 kD) secreted protein that acts on migrating cortical neurons by binding to the very low density lipoprotein receptor (VLDLR), the apolipoprotein E receptor 2 (ApoER2; refs 9-11 ), alpha3beta1 integrin and protocadherins."
Reelin is a serine protease of the extracellular matrix.
Re-evaluation of protease activity of reelin.
Migration, early axonogenesis, and Reelin-dependent layer-forming behavior of early/posterior-born Purkinje cells in the developing mouse lateral cerebellum.
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In mouse lateral cerebellum, Reelin is required for a posture-change step that initiates Purkinje-plate formation in an early/posterior-born subset.
"Previously unknown behaviors are revealed for a subset of Purkinje cells born early in the posteior lateral cerebellum: tangential migration; early axonogenesis; and Reelin-dependent reorientation initiating PP formation."