ArticleEMBO reports2017
Structural basis for ligand capture and release by the endocytic receptor ApoER2.
Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- LRP8 is a functional receptor for yellow fever virus.Nature microbiology · 2026Article
- Self-assembling nanocomposites for smart drug delivery: towards personalized and stimuli-responsive therapeutics.RSC advances · 2026Review
- Structure of Reelin repeat 8 and the adjacent C-terminal region.Biophysical journal · 2022Article
- Lipid Peroxidation Induced ApoE Receptor-Ligand Disruption as a Unifying Hypothesis Underlying Sporadic Alzheimer's Disease in Humans.Journal of Alzheimer's disease : JAD · 2022Article
- Purification of a heterodimeric Reelin construct to investigate binding stoichiometry.European biophysics journal : EBJ · 2020Article
- A substitution mutation in LRP8 gene is significantly associated with susceptibility to familial myocardial infarction.ARYA atherosclerosis · 2020Article
- Dynamics, nanomechanics and signal transduction in reelin repeats.Scientific reports · 2019Article
- Differential Action of Reelin on Oligomerization of ApoER2 and VLDL Receptor in HEK293 Cells Assessed by Time-Resolved Anisotropy and Fluorescence Lifetime Imaging Microscopy.Frontiers in molecular neuroscience · 2019Article
- The Reelin Receptors Apolipoprotein E receptor 2 (ApoER2) and VLDL Receptor.International journal of molecular sciences · 2018Review
- How multi-scale structural biology elucidated context-dependent variability in ectodomain conformation along with the ligand capture and release cycle for LDLR family members.Biophysical reviews · 2018Review
- Structural basis for ligand capture and release by the endocytic receptor ApoER2.EMBO reports · 2017Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apolipoprotein E receptor 2 (ApoER2) is a close homologue of low-density lipoprotein receptor (LDLR) that mediates the endocytosis of ligands, including LDL particles. LDLR family members have been presumed to explore a large conformational space to capture ligands in the extended conformation at the cell surface. Ligands are subsequently released through a pH-titrated structural transition to a self-docked, contracted-closed conformation. In addition to lipoprotein uptake, ApoER2 is implicated in signal transduction during brain development through capture of the extracellular protein reelin. From crystallographic analysis, we determine that the full-length ApoER2 ectodomain adopts an intermediate contracted-open conformation when complexed with the signaling-competent reelin fragment, and we identify a previously unappreciated auxiliary low-affinity binding interface. Based on mutational analyses, we propose that the pH shift during endocytosis weakens the affinity of the auxiliary interface and destabilizes the ligand-receptor complex. Furthermore, this study elucidates that the contracted-open conformation of ligand-bound ApoER2 at neutral pH resembles the contracted-closed conformation of ligand-unbound LDLR at acidic pH in a manner suggestive of being primed for ligand release even prior to internalization.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.