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Related Experiment Videos

Cell Surface Protein Detection to Assess Receptor Internalization.

Magdalena Czarnecka1, Joanna Kitlinska1

  • 1Department of Biochemistry and Molecular & Cellular Biology, Georgetown University Medical Center, Washington DC, USA.

Bio-Protocol
|April 18, 2017
PubMed
Summary

Brain-derived neurotrophic factor (BDNF) stimulation triggers the internalization of the neuropeptide Y receptor (Y5R). This suggests cross-talk between TrkB and Y5R signaling pathways, impacting cell responsiveness.

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Area of Science:

  • Cellular biology
  • Neuroscience
  • Molecular signaling

Background:

  • Membrane receptor trafficking, including internalization, is crucial for cellular responses to external stimuli.
  • Receptor internalization modulates ligand accessibility and cellular sensitivity to environmental cues.
  • Internalization serves as a quantifiable indicator of receptor activation.

Purpose of the Study:

  • To investigate potential cross-talk between the neuropeptide Y receptor (Y5R) and the tyrosine kinase receptor for brain-derived neurotrophic factor (TrkB).
  • To quantify Y5R internalization in response to BDNF, a ligand for TrkB.

Main Methods:

  • Utilized receptor internalization as a measure of receptor activation.
  • Stimulated cells with BDNF and assessed Y5R internalization.

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  • Employed cell surface biotinylation with a membrane-impermeable reagent.
  • Purified biotinylated proteins using avidin affinity chromatography.
  • Analyzed receptor levels via Western blot to determine surface expression.

    • Main Results:

    • BDNF stimulation led to a measurable decrease in cell surface Y5R levels.
    • This reduction indicates that BDNF induces the internalization of Y5R.

    Conclusions:

    • The findings demonstrate functional cross-talk between TrkB and Y5R signaling pathways.
    • BDNF-induced Y5R internalization suggests a novel regulatory mechanism in neuronal signaling.