Related Experiment Video
Updated: Aug 6, 2026

Inducible LAP-tagged Stable Cell Lines for Investigating Protein Function, Spatiotemporal Localization and Protein Interaction Networks
Published on: December 24, 2016
Biotin Ligase-Based Reporter for Detecting Protease Activity
Jennifer Sescil1,2, Isabel Solowiej1,2, Guanwei Zhou2,3
1Department of Chemistry, University of Michigan, Ann Arbor, Michigan48109-1382, United States.
Abstract:
Protease cleavage is a crucial process, associated with cellular signaling and viral infection. Here, we present a novel sensing motif based on a proximity-dependent biotin ligase, TurboID. The sensor, Biotin Annotating Genetically Encoded Ligase-based Sensor (BAGELS), was created by engineering TurboID such that it is only active following protease activity, linking cleavage events to the biotinylation of proximal proteins. BAGELS produces a signal-to-background ratio of approximately 48 when tested with and without protease. This reporter represents the first protease activity sensor with biotin ligase readout in neurons and HEK293T cells. We demonstrate the reporter's use for characterization of protease inhibitors and multiplexed imaging with fluorogenic sensors. Overall, this sensor offers a versatile, enzymatically amplified biotin-based readout compatible with biotin-based detection techniques.

