Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain.
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.
Biochemisches Institut der Christian-Albrechts-Universität Kiel, Olshausenstr. 40, 24118 Kiel, Germany. ilorenzen@biochem.uni-kiel.de
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I
Lorenzen
Ahmad
A
Trad
Joachim
J
Grötzinger
D051722:ADAM Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000072198:ADAM17 Protein; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004815:Epidermal Growth Factor / Q000737:chemistry; D057809:HEK293 Cells; D006801:Humans; D047468:Immunoprecipitation; D051379:Mice; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary
D004815:Epidermal Growth Factor; D051722:ADAM Proteins; D000072198:ADAM17 Protein; C000606462:ADAM17 protein, human; C000606463:Adam17 protein, mouse