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Related Experiment Video

Updated: Nov 9, 2025

A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9

A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9

Published on: August 28, 2018

Substrate-biased activity-based probes identify proteases that cleave receptor CDCP1.

Thomas Kryza¹, Tashbib Khan¹, Scott Lovell^2,3

¹Mater Research Institute, The University of Queensland, Translational Research Institute, Woolloongabba, Queensland, Australia.

Nature Chemical Biology

|April 16, 2021

Summary

This summary is machine-generated.

CUB domain-containing protein 1 (CDCP1) is a cancer target. New probes identified urokinase (uPA) as a key enzyme that cleaves CDCP1, promoting cancer metastasis. Targeting this cleavage may disrupt cancer progression.

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Published on: May 25, 2018

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Last Updated: Nov 9, 2025

A High-Throughput Luciferase Assay to Evaluate Proteolysis of the Single-Turnover Protease PCSK9

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Published on: August 28, 2018

High-Throughput Cellular Profiling of Targeted Protein Degradation Compounds Using HiBiT CRISPR Cell Lines

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The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

The Determination of Protease Specificity in Mouse Tissue Extracts by MALDI-TOF Mass Spectrometry: Manipulating PH to Cause Specificity Changes

Published on: May 25, 2018

Area of Science:

Oncology
Proteomics
Molecular Biology

Background:

CUB domain-containing protein 1 (CDCP1) is an oncogenic transmembrane receptor implicated in cancer.
Proteolytic cleavage of CDCP1 promotes cancer metastasis through poorly understood mechanisms.

Purpose of the Study:

To rapidly identify proteases responsible for CDCP1 cleavage.
To investigate the role of CDCP1 proteolysis in cancer metastasis.

Main Methods:

Development and application of a substrate-biased activity-based probe (sbABP) for protease identification.
In vivo preclinical models to assess metastasis promotion by CDCP1 proteolysis.

Main Results:

Identified urokinase (uPA) as the master regulator of CDCP1 proteolysis.
Demonstrated that uPA directly cleaves CDCP1 and activates plasmin for further cleavage.
Coexpression of uPA and CDCP1 predicts poor disease outcome across multiple cancers.
uPA-mediated CDCP1 proteolysis was shown to promote metastasis in vivo.

Conclusions:

CDCP1 cleavage is a potential therapeutic target for cancer treatment.
sbABP technology is a valuable tool for identifying disease-relevant proteases.
uPA-mediated CDCP1 cleavage drives cancer metastasis.