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Related Concept Videos

Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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:
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...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...

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Related Experiment Video

Updated: May 12, 2026

BRET-based G Protein Biosensors for Measuring G Protein-Coupled Receptor Activity in Live Cells
09:21

BRET-based G Protein Biosensors for Measuring G Protein-Coupled Receptor Activity in Live Cells

Published on: November 7, 2025

BRET Biosensor Analysis of Receptor Tyrosine Kinase Functionality.

Sana Siddiqui1, Wei-Na Cong, Caitlin M Daimon

  • 1Receptor Pharmacology Unit, National Institute on Aging, National Institutes of Health Baltimore, MD, USA.

Frontiers in Endocrinology
|April 12, 2013
PubMed
Summary

Bioluminescence resonance energy transfer (BRET) offers a powerful method for studying receptor tyrosine kinases (RTKs). This review highlights BRET

Keywords:
RTKcytokine receptorsepidermal growth factor receptorinsulin receptorinsulin-like growth factor receptorneurotrophicprotein–protein interactionreceptor tyrosine kinase

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Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
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Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

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Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays

Published on: September 19, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Bioluminescence resonance energy transfer (BRET) is an advanced technique for analyzing biomolecular protein interactions.
  • While widely used for G protein-coupled receptors (GPCRs), BRET applications for receptor tyrosine kinases (RTKs) are underexplored.
  • RTKs are crucial in diseases like cancer and diabetes, often activated by dimerization.

Purpose of the Study:

  • To review the application of BRET in studying RTK activity and protein-protein signaling interactions.
  • To highlight the potential of BRET for investigating RTK superfamily members and associated receptors.

Main Methods:

  • Literature review of functional BRET studies focusing on RTKs and non-GPCR receptor signaling.
  • Analysis of BRET applications across various RTK subclasses, including neurotrophic, insulinotropic, and growth factor receptors.
  • Examination of BRET studies on tyrosine kinase-associated receptors like cytokine receptors.

Main Results:

  • The review covers BRET studies on diverse RTKs such as Trk, p75NTR, IR, IGFR, EGFR, FGFR, VEGFR, c-kit, PDGFR, OB-R, and GHR.
  • Evidence, though sparse, indicates significant potential for BRET in functional RTK research.
  • BRET facilitates the study of receptor-protein interactions critical for signal transduction.

Conclusions:

  • BRET is a valuable tool for investigating RTK dimerization and signaling pathways.
  • Despite limited current use, BRET holds immense promise for advancing RTK biology research.
  • Further application of BRET can elucidate RTK functions in health and disease.