Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Two-State Receptor Model01:29

The Two-State Receptor Model

The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...
Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Structural basis of regioselective double halogenation of the β-carboline tryptoline by the single-component halogenase AetF.

Acta crystallographica. Section D, Structural biology·2026
Same author

Single-Molecule FRET-Tracking of InlB-Activated MET Receptors in Living Cells.

Small (Weinheim an der Bergstrasse, Germany)·2025
Same author

Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein.

Acta crystallographica. Section F, Structural biology communications·2025
Same author

Structural Basis of Regioselective Bromination of Tricyclic Tryptoline by the Tryptophan Halogenase Thal.

Chembiochem : a European journal of chemical biology·2025
Same author

The NADH-dependent flavin reductase ThdF follows an ordered sequential mechanism though crystal structures reveal two FAD molecules in the active site.

The Journal of biological chemistry·2024
Same author

Single-molecule imaging and molecular dynamics simulations reveal early activation of the MET receptor in cells.

Nature communications·2024
Same journal

Fucosylation in cancer and its role in anti-tumor immunity.

European journal of cell biology·2026
Same journal

Ethanol stress-induced vacuole unlobing is mediated via downregulation of phosphatidylinositol-3,5-bisphosphate and Atg18 phospho-regulation.

European journal of cell biology·2026
Same journal

Letter to the Editor: TGF-β drives pulmonary fibrosis through dual dysregulation of TNF pathway transcription and splicing.

European journal of cell biology·2026
Same journal

A new photochromic sterol controls TRPC3 activity by actuating a hub of regulatory lipid coordination.

European journal of cell biology·2026
Same journal

The plaque protein myozap defines unique junction strands in smooth muscle cell bundles.

European journal of cell biology·2026
Same journal

Integrated single-cell RNA sequencing analysis reveals phenotypic differences between blood endothelial cells from oral mucosa and skin.

European journal of cell biology·2026
See all related articles

Related Experiment Video

Updated: Jun 5, 2026

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

Structural insights into Met receptor activation.

Hartmut H Niemann1

  • 1Department of Chemistry, Bielefeld University, Universitätsstrasse 25, 33615 Bielefeld, Germany. Hartmut.Niemann@uni-bielefeld.de

European Journal of Cell Biology
|January 19, 2011
PubMed
Summary
This summary is machine-generated.

The bacterial protein InlB activates the receptor tyrosine kinase Met by mediating dimerization, similar to its natural ligand HGF/SF. This structural insight into Met activation is crucial for understanding its role in development, regeneration, and cancer.

More Related Videos

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins
16:10

A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins

Published on: March 22, 2012

Related Experiment Videos

Last Updated: Jun 5, 2026

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins
16:10

A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins

Published on: March 22, 2012

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Signaling

Background:

  • The receptor tyrosine kinase Met is vital for vertebrate development and tissue repair.
  • Met deregulation is implicated in cancer development.
  • Met is a target during infection by Listeria monocytogenes.

Purpose of the Study:

  • To review the structural basis of Met receptor activation by Listeria monocytogenes InlB.
  • To compare Met activation by InlB with its natural ligand, hepatocyte growth factor/scatter factor (HGF/SF), and its splice variant NK1.

Main Methods:

  • Analysis of crystal structures of Met in complex with L. monocytogenes InlB.
  • Review of existing literature on Met activation by HGF/SF and NK1.

Main Results:

  • Crystal structures reveal that InlB mediates Met dimerization through direct ligand-mediated contacts.
  • This mechanism of dimerization by InlB shares similarities with HGF/SF-induced Met activation.
  • Specific differences in dimerization interfaces are highlighted between InlB and HGF/SF/NK1.

Conclusions:

  • The structural understanding of Met activation by the bacterial protein InlB provides insights into host-pathogen interactions.
  • Comparing InlB-mediated activation with physiological ligands like HGF/SF clarifies conserved and divergent mechanisms of Met signaling.
  • This knowledge is relevant for therapeutic strategies targeting Met in cancer and infectious diseases.