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Split-BioID a conditional proteomics approach to monitor the composition of spatiotemporally defined protein complexes

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  • Isabel Myriam Schopp

    (CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
    Biochemie-Zentrum Heidelberg (BZH))

  • Cinthia Claudia Amaya Ramirez

    (CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
    Biochemie-Zentrum Heidelberg (BZH))

  • Jerneja Debeljak

    (CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
    Biochemie-Zentrum Heidelberg (BZH))

  • Elisa Kreibich

    (CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
    Biochemie-Zentrum Heidelberg (BZH))

  • Merle Skribbe

    (CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
    Biochemie-Zentrum Heidelberg (BZH))

  • Klemens Wild

    (Biochemie-Zentrum Heidelberg (BZH))

  • Julien Béthune

    (CellNetworks Junior Research Group Posttranscriptional Regulation of mRNA Expression and Localization, Heidelberg University
    Biochemie-Zentrum Heidelberg (BZH))

Abstract

Understanding the function of the thousands of cellular proteins is a central question in molecular cell biology. As proteins are typically part of multiple dynamic and often overlapping macromolecular complexes exerting distinct functions, the identification of protein–protein interactions (PPI) and their assignment to specific complexes is a crucial but challenging task. We present a protein fragments complementation assay integrated with the proximity-dependent biotinylation technique BioID. Activated on the interaction of two proteins, split-BioID is a conditional proteomics approach that allows in a single and simple assay to both experimentally validate binary PPI and to unbiasedly identify additional interacting factors. Applying our method to the miRNA-mediated silencing pathway, we can probe the proteomes of two distinct functional complexes containing the Ago2 protein and uncover the protein GIGYF2 as a regulator of miRNA-mediated translation repression. Hence, we provide a novel tool to study dynamic spatiotemporally defined protein complexes in their native cellular environment.

Suggested Citation

  • Isabel Myriam Schopp & Cinthia Claudia Amaya Ramirez & Jerneja Debeljak & Elisa Kreibich & Merle Skribbe & Klemens Wild & Julien Béthune, 2017. "Split-BioID a conditional proteomics approach to monitor the composition of spatiotemporally defined protein complexes," Nature Communications, Nature, vol. 8(1), pages 1-14, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15690
    DOI: 10.1038/ncomms15690
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    Cited by:

    1. Orhi Barroso-Gomila & Fredrik Trulsson & Veronica Muratore & Iñigo Canosa & Laura Merino-Cacho & Ana Rosa Cortazar & Coralia Pérez & Mikel Azkargorta & Ibon Iloro & Arkaitz Carracedo & Ana M. Aransay , 2021. "Identification of proximal SUMO-dependent interactors using SUMO-ID," Nature Communications, Nature, vol. 12(1), pages 1-19, December.

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