ArticleProtein science : a publication of the Protein Society2014
Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- Rational Design of Peptide Binders Targeting Prominin‑1 and Sortilin for Molecular Sensing Applications.ACS omega · 2026Article
- Molecular recognition of thyroglobulin by sortilin.Nature communications · 2026Article
- Sortilin-Mediated Rapid, Precise and Sustained Degradation of Membrane Proteins via mRNA-Encoded Lysosome-Targeting Chimera.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Review
- Article
- Computational Identification of Potent Multitarget Natural Ligands for Alzheimer's Disease Therapeutics.Scientifica · 2025Article
- Peptide-Oligonucleotide Conjugation: Chemistry and Therapeutic Applications.Current issues in molecular biology · 2024Review
- Sortilin is dispensable for secondary injury processes following traumatic brain injury in mice.Heliyon · 2024Article
- Sudocetaxel Zendusortide (TH1902) triggers the cGAS/STING pathway and potentiates anti-PD-L1 immune-mediated tumor cell killing.Frontiers in immunology · 2024Article
- Regulation of Human Sortilin Alternative Splicing by Glucagon-like Peptide-1 (GLP1) in Adipocytes.International journal of molecular sciences · 2023Article
- Recent advances in mass spectrometry analysis of neuropeptides.Mass spectrometry reviews · 2023Review
- Identification of Sortilin Alternatively Spliced Variants in Mouse 3T3L1 Adipocytes.International journal of molecular sciences · 2021Article
- An Allosteric Binding Site on Sortilin Regulates the Trafficking of VLDL, PCSK9, and LDLR in Hepatocytes.Biochemistry · 2020Article
- Anti-sortilin1 Antibody Up-Regulates ProgranulinFrontiers in neuroscience · 2020Article
- HSPA12A targets the cytoplasmic domain and affects the trafficking of the Amyloid Precursor Protein receptor SorLA.Scientific reports · 2019Article
- Regional and Cellular Mapping of Sortilin Immunoreactivity in Adult Human Brain.Frontiers in neuroanatomy · 2019Article
- Structural insights into SorCS2-Nerve Growth Factor complex formation.Nature communications · 2018Article
- Sortilin in Glucose Homeostasis: From Accessory Protein to Key Player?Frontiers in pharmacology · 2018Review
- Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release.Nature communications · 2017Article
- Phosphatidylinositol (3,4,5)-trisphosphate binds to sortilin and competes with neurotensin: Implications for very low density lipoprotein binding.Biochemical and biophysical research communications · 2016Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sortilin is a multifunctional receptor involved in sorting and apoptosis. We have previously reported a 2.0-Å structure of the Vps10 ectodomain in complex with one of its ligands, the tridecapeptide neurotensin. Here we set out to further characterize the structural properties of sortilin and its interaction with neurotensin. To this end, we have determined a new 2.7 Å structure using a crystal grown with a 10-fold increased concentration of neurotensin. Here a second peptide fragment was observed within the Vps10 β-propeller, which may in principle either represent a second molecule of neurotensin or the N-terminal part of the molecule bound at the previously identified binding site. However, in vitro binding experiments strongly favor the latter hypothesis. Neurotensin thus appears to bind with a 1:1 stoichiometry, and whereas the N-terminus does not bind on its own, it enhances the affinity in context of full-length neurotensin. We conclude that the N-terminus of neurotensin probably functions as an affinity enhancer for binding to sortilin by engaging the second binding site. Crystal packing differs partly from the previous structure, which may be due to variations in the degree and pattern of glycosylations. Consequently, a notable hydrophobic loop, not modeled previously, could now be traced. A computational analysis suggests that this and a neighboring loop may insert into the membrane and thus restrain movement of the Vps10 domain. We have, furthermore, mapped all N-linked glycosylations of CHO-expressed human sortilin by mass spectrometry and find that their locations are compatible with membrane insertion of the hydrophobic loops.
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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.