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Proximity-Dependent Biotinylation Approaches to Explore the Dynamic Compartmentalized Proteome
Ugo Dionne1, Anne-Claude Gingras1,2
1Lunenfeld-Tanenbaum Research Institute, Sinai Health, Toronto, ON, Canada.
Frontiers in Molecular Biosciences
|March 21, 2022
Summary
Proximity-dependent biotinylation methods like BioID and APEX can map protein locations. This review explores how these techniques can reveal the impact of post-translational modifications on protein compartmentalization.
Area of Science:
- Cellular Biology
- Proteomics
- Biochemistry
Background:
- Proximity-dependent biotinylation (BioID, APEX) is crucial for mapping protein localization within cellular compartments.
- Post-translational modifications (PTMs) regulate protein associations with cellular structures, but their role in compartmentalization is not fully understood.
- Systematic investigation of PTMs' effects on protein localization using proximity proteomics is lacking.
Purpose of the Study:
- To review the progress in proximity-dependent biotinylation techniques.
- To discuss how these methods can elucidate the role of PTMs in protein compartmentalization.
- To highlight the potential of proximity proteomics in understanding protein localization regulation.
Main Methods:
- Review of proximity-dependent biotinylation strategies (BioID, APEX, and derivatives).
- Discussion of post-translational modifications (PTMs) and their impact on protein localization.
- Exploration of proximity proteomics for studying protein-PTM-compartment interactions.
Main Results:
- Proximity-dependent biotinylation has advanced the study of cellular structures.
- PTMs significantly influence protein associations with cellular compartments.
- Systematic investigation using these methods can reveal PTM contributions to protein compartmentalization.
Conclusions:
- Proximity-dependent biotinylation offers powerful tools for cell biology research.
- Understanding PTMs' roles in protein compartmentalization is essential.
- Future research should leverage proximity proteomics to explore PTM-mediated localization.
