Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain

Biochem Biophys Res Commun. 2011 Nov 18;415(2):330-6. doi: 10.1016/j.bbrc.2011.10.056. Epub 2011 Oct 18.

Abstract

A disintegrin and metalloprotease protein 17 (ADAM17) is a transmembrane zinc dependent metalloprotease. The catalytic activity of the enzyme results in the shedding of a broad range of membrane proteins. The release of the corresponding ectodomains induces a switch in various physiological and pathophysiological processes. So far there is not much information about the molecular mechanism of ADAM17 activation available. As for other transmembrane proteases, multimerisation may play a critical role in the activation and function of ADAM17. The present work demonstrates that ADAM17 indeed exists as a multimer in the cell membrane and that this multimerisation is mediated by its EGF-like domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADAM Proteins / chemistry
  • ADAM Proteins / genetics
  • ADAM Proteins / metabolism*
  • ADAM17 Protein
  • Animals
  • Cell Membrane / enzymology
  • Epidermal Growth Factor / chemistry
  • HEK293 Cells
  • Humans
  • Immunoprecipitation
  • Mice
  • Protein Multimerization
  • Protein Structure, Tertiary

Substances

  • Epidermal Growth Factor
  • ADAM Proteins
  • ADAM17 Protein
  • ADAM17 protein, human
  • Adam17 protein, mouse