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Related Experiment Video

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Measuring Plasma Membrane Protein Endocytic Rates by Reversible Biotinylation
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Proximal Biotinylation-Based Combinatory Approach for Isolating Integral Plasma Membrane Proteins.

Mehmet Akdag1, Zeynep Sabahat Yunt1, Altug Kamacioglu1

  • 1Department of Molecular Biology and Genetics, Koc University, Istanbul 34450, Turkey.

Journal of Proteome Research
|June 6, 2020
PubMed
Summary

Plasma Membrane-BioID offers a new method for isolating plasma membrane proteins. This technique effectively labels and purifies these proteins for comprehensive proteomic analysis.

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Area of Science:

  • Proteomics
  • Cell Biology
  • Biochemistry

Background:

  • Comprehensive profiling of the cell-surface proteome is difficult.
  • Existing tools lack effective and reproducible methods for isolating plasma membrane proteins from mammalian cells.

Purpose of the Study:

  • To develop an improved method for labeling and isolating plasma membrane proteins.
  • To overcome limitations in identifying integral membrane proteins.

Main Methods:

  • Employed a proximity-dependent biotinylation approach using a lipid-modified BirA* enzyme (MyrPalm BirA*) targeted to the plasma membrane inner leaflet.
  • Developed a method called Plasma Membrane-BioID, eliminating the need for an extra in vitro labeling step.
  • Combined Plasma Membrane-BioID with sucrose density gradient centrifugation for protein isolation and mass spectrometry analysis.

Main Results:

  • Plasma Membrane-BioID effectively biotinylated plasma membrane proteins.
  • The combined method yielded highly pure plasma components.
  • Overcame inherent limitations in identifying integral membrane proteins.

Conclusions:

  • Plasma Membrane-BioID is a valuable tool for cell-surface proteome profiling.
  • The integration of Plasma Membrane-BioID with sucrose density gradient centrifugation provides a robust strategy for proteomic analysis of plasma membrane proteins.