Efficient proximity labeling in living cells and organisms with TurboID

By Tess C. Branon, Justin A. Bosch, Ariana D. Sanchez, N. Udeshi, Tanya Svinkina, Steven A. Carr, J. Feldman, Norbert Perrimon, A. Ting. Nature Biotechnology, 2018

1,681 citations recorded by the source corpus.

Protein interaction networks and protein compartmentalization underlie all signaling and regulatory processes in cells. Enzyme-catalyzed proximity labeling (PL) has emerged as a new approach to study the spatial and interaction characteristics of proteins in living cells. However, current PL methods require over 18 h of labeling time or utilize chemicals with limited cell permeability or high toxicity. We used yeast display-based directed evolution to engineer two promiscuous mutants of biotin ligase, TurboID and miniTurbo, which catalyze PL with much greater efficiency than BioID or BioID2, and enable 10-min PL in cells with non-toxic and easily deliverable biotin. Furthermore, TurboID extends biotin-based PL to flies and worms.

Subfields: Cell Biology, Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/77941a491bd04e0e9d590642ec655bee791568e0

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Citations in the corpus

• Autophagy promotes immune evasion of pancreatic cancer by degrading MHC-I (2020, positive): “To identify autophagy receptor protein(s) involved in MHC-I degradation in PDAC cells, we generated a proximity biotinylation assay whereby HLA-A was fused to the biotin ligase, TurboID (TrID) 16 and Flag (HLA-A-TrID).”