Abstract
Amphiregulin, like other ErbB ligands, is synthesized as a pro-protein which requires cleavage at the cell surface to release the active signaling domain. Prior studies using a variety of approaches have not yielded a consensus about the precise cleavage site. Here we report the purification and protein sequencing of the cell-associated human Amphiregulin stalk which remains following cleavage of the signaling domain. These data indicate that human Amphiregulin is cleaved at Lysine 187, a site homologous to the cleavage site reported in the mouse protein and distinct from the Lysine 184 site previously reported for the human protein.
Original language | English (US) |
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Pages (from-to) | 3500-3502 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 586 |
Issue number | 19 |
DOIs | |
State | Published - Sep 21 2012 |
Keywords
- ADAM17
- Amphiregulin
- Epidermal growth factor receptor
- Pro-protein processing
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology