Proximity-Dependent Biotinylation Approaches to Explore the Dynamic Compartmentalized Proteome

Ugo Dionne; Anne-Claude Gingras

doi:10.3389/fmolb.2022.852911

Proximity-Dependent Biotinylation Approaches to Explore the Dynamic Compartmentalized Proteome

Front Mol Biosci. 2022 Mar 4:9:852911. doi: 10.3389/fmolb.2022.852911. eCollection 2022.

Authors

Ugo Dionne¹, Anne-Claude Gingras^{1

2}

Affiliations

¹ Lunenfeld-Tanenbaum Research Institute, Sinai Health, Toronto, ON, Canada.
² Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada.

Abstract

In recent years, proximity-dependent biotinylation approaches, including BioID, APEX, and their derivatives, have been widely used to define the compositions of organelles and other structures in cultured cells and model organisms. The associations between specific proteins and given compartments are regulated by several post-translational modifications (PTMs); however, these effects have not been systematically investigated using proximity proteomics. Here, we discuss the progress made in this field and how proximity-dependent biotinylation strategies could elucidate the contributions of PTMs, such as phosphorylation, to the compartmentalization of proteins.

Keywords: APEX; BioID; cellular organization; mass spectrometry; phosphorylation; post-translational modification; proximity-dependent biotinylation.

Publication types

Review