Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases.

Journal article

The polytopic membrane protein Rhomboid-1 promotes the cleavage of the membrane-anchored TGFalpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Until now, the mechanism of this key signaling regulator has been obscure, but our analysis suggests that Rhomboid-1 is a novel intramembrane serine protease that directly cleaves Spitz. In accordance with the putative Rhomboid active site being in the membrane bilayer, Spitz is cleaved within its transmembrane domain,...

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Authors: Urban, S; Lee, JR; Freeman, M

• Publication status: Published
• Journal: Cell
• Volume: 107
• Issue: 2
• Pages: 173-182
• Publication date: 2001-10-01
• DOI: 10.1016/s0092-8674(01)00525-6
• EISSN: 1097-4172
• ISSN: 0092-8674
• Language: English
• Keywords: Protein Binding; Catalysis; Humans; Blotting, Western; DNA Mutational Analysis; CHO Cells; Microscopy, Fluorescence; Sequence Homology, Amino Acid; Dose-Response Relationship, Drug; Drosophila Proteins; Protein Structure, Tertiary; Cell Membrane; Epidermal Growth Factor; Cell Line; Drosophila; Cricetinae; Mice; Animals; Hela Cells; COS Cells; Serine Endopeptidases; Amino Acid Sequence; Receptor, Epidermal Growth Factor; Membrane Proteins; Transfection; Molecular Sequence Data; Models, Biological