ArticleScientific reports2015
Extracellular vimentin interacts with insulin-like growth factor 1 receptor to promote axonal growth.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 66 citations in OpenAlex.
- Review
- Organ-Specific Small Protein Networks in 100 kDa Ultrafiltrates: Functional Analysis and Implications for Neuroregenerative Medicine.International journal of molecular sciences · 2025Article
- Extracellular vimentin amplifies inflammation: Perspectives for immune injury and therapeutics for periodontitis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Review
- Review
- Novel secreted regulators of glucose and lipid metabolism in the development of metabolic diseases.Diabetologia · 2024Review
- Space Flight Enhances Stress Pathways in Human Neural Stem Cells.Biomolecules · 2024Article
- Vimentin takes a hike - Emerging roles of extracellular vimentin in cancer and wound healing.Current opinion in cell biology · 2023Review
- The molecular biophysics of extracellular vimentin and its role in pathogen-host interactions.Current opinion in cell biology · 2023Review
- Vimentin as a potential target for diverse nervous system diseases.Neural regeneration research · 2023Review
- Prevention of Noise-Induced Hearing Loss In Vivo: Continuous Application of Insulin-like Growth Factor 1 and Its Effect on Inner Ear Synapses, Auditory Function and Perilymph Proteins.International journal of molecular sciences · 2022Article
- Cell surface detection of vimentin, ACE2 and SARS-CoV-2 Spike proteins reveals selective colocalization at primary cilia.Scientific reports · 2022Article
- Extracellular Vimentin as a Target Against SARS-CoV-2 Host Cell Invasion.Small (Weinheim an der Bergstrasse, Germany) · 2022Article
- The Pro-fibrotic Response of Mesenchymal Leader Cells to Lens Wounding Involves Hyaluronic Acid, Its Receptor RHAMM, and Vimentin.Frontiers in cell and developmental biology · 2022Article
- Role of Extracellular Vimentin in Cancer-Cell Functionality and Its Influence on Cell Monolayer Permeability Changes Induced by SARS-CoV-2 Receptor Binding Domain.International journal of molecular sciences · 2021Article
- Extracellular vimentin as a target against SARS-CoV-2 host cell invasion.bioRxiv : the preprint server for biology · 2021Article
- Cluster Analysis of Early Postnatal Biochemical Markers May Predict Development of Retinopathy of Prematurity.Translational vision science & technology · 2020Article
- Mechanical and Non-Mechanical Functions of Filamentous and Non-Filamentous Vimentin.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020Review
- MicroRNA-19a-PTEN Axis Is Involved in the Developmental Decline of Axon Regenerative Capacity in Retinal Ganglion Cells.Molecular therapy. Nucleic acids · 2020Article
- Vimentin as a Multifaceted Player and Potential Therapeutic Target in Viral Infections.International journal of molecular sciences · 2020Review
- Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vimentin, an intermediate filament protein, is generally recognised as an intracellular protein. Previously, we reported that vimentin was secreted from astrocytes and promoted axonal growth. The effect of extracellular vimentin in neurons was a new finding, but its signalling pathway was unknown. In this study, we aimed to determine the signalling mechanism of extracellular vimentin that facilitates axonal growth. We first identified insulin-like growth factor 1 receptor (IGF1R) as a receptor that is highly phosphorylated by vimentin stimulation. IGF1R blockades diminished vimentin- or IGF1-induced axonal growth in cultured cortical neurons. IGF1, IGF2 and insulin were not detected in the neuron culture medium after vimentin treatment. The combined drug affinity responsive target stability method and western blotting analysis showed that vimentin and IGF1 interacted with IGF1R directly. In addition, immunoprecipitation and western blotting analyses confirmed that recombinant IGF1R bound to vimentin. The results of a molecular dynamics simulation revealed that C-terminal residues (residue number 330-407) in vimentin are the most appropriate binding sites with IGF1R. Thus, extracellular vimentin may be a novel ligand of IGF1R that promotes axonal growth in a similar manner to IGF1. Our results provide novel findings regarding the role of extracellular vimentin and IGF1R in axonal growth.
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