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

Inken Lorenzen1, Ahmad Trad, Joachim Grötzinger

  • 1Biochemisches Institut der Christian-Albrechts-Universität Kiel, Olshausenstr. 40, 24118 Kiel, Germany. ilorenzen@biochem.uni-kiel.de

Biochemical and Biophysical Research Communications
|October 29, 2011
PubMed

Insights

The metalloprotease protein 17 (ADAM17) functions as a multimer in cell membranes. This multimerization, crucial for its activity, is facilitated by its EGF-like domain, shedding membrane proteins and impacting physiological processes.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • ADAM17 is a metalloprotease involved in shedding membrane proteins.
  • This shedding influences physiological and pathophysiological processes.
  • The molecular mechanism of ADAM17 activation is not well understood.

Purpose of the Study:

  • To investigate the role of multimerization in ADAM17 activation.
  • To determine if ADAM17 exists as a multimer in the cell membrane.
  • To identify the domain responsible for ADAM17 multimerization.

Main Methods:

  • Cell-based assays to study ADAM17 localization and interactions.
  • Biochemical methods to analyze protein multimerization.
  • Domain-specific mutagenesis to probe functional regions.

Main Results:

  • ADAM17 was confirmed to exist as a multimer in the cell membrane.
  • Multimerization of ADAM17 is mediated by its EGF-like domain.
  • This multimerization is likely critical for ADAM17's catalytic activity.

Conclusions:

  • ADAM17 multimerization is a key aspect of its molecular mechanism.
  • The EGF-like domain plays a crucial role in mediating ADAM17 function.
  • Understanding ADAM17 multimerization may offer therapeutic insights.

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