Journal
EMBO REPORTS
Volume 12, Issue 5, Pages 421-427Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/embor.2011.50
Keywords
cancer; EGF receptor; intramembrane protease; mammal; rhomboid
Categories
Funding
- International Human Frontier Science Program Organization
- EMBO
- Marie Curie Intraeuropean Fellowship
- Austrian Fonds zur Forderung der wissenschaftlichen Forschung (FWF)
- Austrian Academy of Science
- MRC [MC_U105178780] Funding Source: UKRI
- Medical Research Council [MC_U105178780] Funding Source: researchfish
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The epidermal growth factor receptor (EGFR) has several functions in mammalian development and disease, particularly cancer. Most EGF ligands are synthesized as membrane-tethered precursors, and their proteolytic release activates signalling. In Drosophila, rhomboid intramembrane proteases catalyse the release of EGF-family ligands; however, in mammals this seems to be primarily achieved by ADAM-family metalloproteases. We report here that EGF is an efficient substrate of the mammalian rhomboid RHBDL2. RHBDL2 cleaves EGF just outside its transmembrane domain, thereby facilitating its secretion and triggering activation of the EGFR. We have identified endogenous RHBDL2 activity in several tumour cell lines.
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