ArticleThe Journal of biological chemistry2010
Identification of a linear epitope in sortilin that partakes in pro-neurotrophin binding.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Sortilin is dispensable for secondary injury processes following traumatic brain injury in mice.Heliyon · 2024Article
- PROneurotrophins and CONSequences.Molecular neurobiology · 2018Review
- Sortilin and Its Multiple Roles in Cardiovascular and Metabolic Diseases.Arteriosclerosis, thrombosis, and vascular biology · 2018Review
- Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release.Nature communications · 2017Article
- Sorting receptor sortilin-a culprit in cardiovascular and neurological diseases.Journal of molecular medicine (Berlin, Germany) · 2014Review
- Small-molecule modulation of neurotrophin receptors: a strategy for the treatment of neurological disease.Nature reviews. Drug discovery · 2013Review
- Article
- C-terminus of progranulin interacts with the beta-propeller region of sortilin to regulate progranulin trafficking.PloS one · 2011Article
- Prediction of B-cell linear epitopes with a combination of support vector machine classification and amino acid propensity identification.Journal of biomedicine & biotechnology · 2011Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sortilin acts as a cell surface receptor for pro-neurotrophins (pro-NT) that upon complex formation with the p75 neurotrophin receptor (p75(NTR)) is able to signal neuronal cell death. Here we screened a sortilin peptide library comprising 16-mer overlapping sequences for binding of the pro-domains of nerve growth factor and brain-derived neurotrophic factor. We find that a linear surface-exposed sequence, (163)RIFRSSDFAKNF(174), constitutes an important pro-NT binding epitope in sortilin. Systematic mutational analysis revealed residues Arg(163), Phe(165), Arg(166), and Phe(170) to be critical for the interaction. Expression of a sortilin mutant in which these four amino acids were substituted by alanines disrupted pro-NT binding without affecting receptor heterodimerization with p75(NTR) or binding of ligands that selectively engages the centrally located tunnel in the beta-propeller of sortilin. We furthermore demonstrate that a peptide comprising the ligand-binding epitope can prevent pro-NT-induced apoptosis in RN22 schwannoma cells.
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Registered trials
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.