Clarification of the C-terminal proteolytic processing site of human Amphiregulin

Kelly S. Levano, Paraic A. Kenny

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)3500-3502
Number of pages3
JournalFEBS Letters
Volume586
Issue number19
DOIs
StatePublished - Sep 21 2012

Fingerprint

Lysine
Processing
Proteins
Protein Sequence Analysis
Ligands
Purification
Amphiregulin

Keywords

  • ADAM17
  • Amphiregulin
  • Epidermal growth factor receptor
  • Pro-protein processing

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

Clarification of the C-terminal proteolytic processing site of human Amphiregulin. / Levano, Kelly S.; Kenny, Paraic A.

In: FEBS Letters, Vol. 586, No. 19, 21.09.2012, p. 3500-3502.

Research output: Contribution to journalArticle

Levano, Kelly S. ; Kenny, Paraic A. / Clarification of the C-terminal proteolytic processing site of human Amphiregulin. In: FEBS Letters. 2012 ; Vol. 586, No. 19. pp. 3500-3502.
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