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ER Membrane Protein Interactions Using the Split-Ubiquitin System (SUS).

Lisa Yasmin Asseck1, Niklas Wallmeroth1, Christopher Grefen2

  • 1Centre for Plant Molecular Biology, Developmental Genetics, University of Tübingen, Auf der Morgenstelle 32, 72076, Tübingen, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|October 19, 2017
PubMed
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This study presents a yeast mating-based Split-Ubiquitin System (mbSUS) protocol to analyze protein-protein interactions (PPIs) of endoplasmic reticulum membrane proteins in vivo. The method allows studying full-length proteins in their native context.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular functions.
  • Membrane proteins are vital for cellular processes like signaling and transport.
  • Studying PPIs of membrane proteins in vivo is challenging.

Purpose of the Study:

  • To provide a detailed protocol for the yeast mating-based Split-Ubiquitin System (mbSUS).
  • To enable the study of full-length endoplasmic reticulum membrane protein interactions in vivo.
  • To describe the application of the SUS Bridge assay (SUB) for ternary interactions.

Main Methods:

  • Utilizes the yeast mating-based Split-Ubiquitin System (mbSUS).
  • Leverages the ubiquitin proteasome pathway to activate reporter genes.
Keywords:
GatewayMembrane proteinsProtein–protein interactionSUBSplit UbiquitinTernary interactionYeastmbSUS

Related Experiment Videos

  • Includes protocols for the SUS Bridge assay (SUB) for ternary interactions.

    • Main Results:

    • mbSUS allows in vivo analysis of full-length membrane proteins in their native cellular context.
    • The mating-based approach is suitable for both small- and large-scale PPI studies.
    • The SUB assay is optimized for detecting ternary protein interactions.

    Conclusions:

    • mbSUS is a robust system for studying ER membrane protein PPIs.
    • The protocol facilitates understanding of complex protein interactions in vivo.
    • This method advances the study of membrane protein functions and interactions.