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Updated: Jul 8, 2026

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
Published on: March 5, 2018
Caspase cleavage of the MET receptor generates an HGF interfering fragment
Julien Deheuninck1, Bénédicte Foveau, Gautier Goormachtigh
1UMR-8161, Institut de Biologie de Lille, CNRS, Université de Lille-1, Université de Lille-2, Institut Pasteur de Lille, BP 447, F-59021 Lille Cedex, France.
Abstract:
The MET tyrosine kinase receptor activated by its ligand HGF/SF, induces several cellular responses, including survival. Nonetheless, the MET receptor is cleaved in stress conditions by caspases within its intracellular region, generating a 40kDa fragment, p40 MET, with pro-apoptotic properties. Here, we established that this cleavage splits the receptor at the juxtamembrane ESVD site, causing the concomitant generation of p100 MET, corresponding to the entire extracellular region of the MET receptor still spanning the membrane. This fragment is able to bind HGF/SF and to prevent HGF-dependent signaling downstream of full MET, demonstrating its function as a decoy receptor.
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