ArticleNature communications2024
Single-molecule imaging and molecular dynamics simulations reveal early activation of the MET receptor in cells.
Article in Nature communications, 2024. 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.
- Quantitative Mapping of Nanoscale EGFR-Grb2 Assemblies by DNA-PAINT.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Quantitative Stimulated Emission Depletion (STED) Microscopy with DNA-Fluorophore Labels.ACS nano · 2026Article
- Integrating Molecular Dynamics Simulations and Single-molecule FRET Spectroscopy: From Computational FRET Estimation to Experimental Data Interpretation.The journal of physical chemistry. B · 2026Review
- Single-Molecule FRET-Tracking of InlB-Activated MET Receptors in Living Cells.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Recovery of glioblastoma cells derived from patients after a decade of cryopreservation for drug response studies.Scientific reports · 2025Article
- ILVES: Accurate and Efficient Bond Length and Angle Constraints in Molecular Dynamics.Journal of chemical theory and computation · 2025Article
- Article
- Recent Advancements in Imaging Techniques for Individual Extracellular Vesicles.Molecules (Basel, Switzerland) · 2024Review
- Single-molecule imaging and molecular dynamics simulations reveal early activation of the MET receptor in cells.Nature communications · 2024Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Embedding of cell-surface receptors into a membrane defines their dynamics but also complicates experimental characterization of their signaling complexes. The hepatocyte growth factor receptor MET is a receptor tyrosine kinase involved in cellular processes such as proliferation, migration, and survival. It is also targeted by the pathogen Listeria monocytogenes, whose invasion protein, internalin B (InlB), binds to MET, forming a signaling dimer that triggers pathogen internalization. Here we use an integrative structural biology approach, combining molecular dynamics simulations and single-molecule Förster resonance energy transfer (smFRET) in cells, to investigate the early stages of MET activation. Our simulations show that InlB binding stabilizes MET in a conformation that promotes dimer formation. smFRET reveals that the in situ dimer structure closely resembles one of two previously published crystal structures, though with key differences. This study refines our understanding of MET activation and provides a methodological framework for studying other plasma membrane receptors.
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Registered trials
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