Journal
FEBS LETTERS
Volume 586, Issue 19, Pages 3500-3502Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.07.078
Keywords
Amphiregulin; Epidermal growth factor receptor; Pro-protein processing; ADAM 17
Funding
- Albert Einstein College of Medicine
- Career Catalyst Award from Susan G. Komen for the Cure [KG100888]
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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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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