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The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Activation of ADAM 12 protease by copper.

F Loechel1, U M Wewer

  • 1Institute of Molecular Pathology, University of Copenhagen, Frederik V's Vej 11, DK-2100 Copenhagen, Denmark.

FEBS Letters
|October 10, 2001
PubMed
Summary

The metalloprotease ADAM 12-S is activated by copper ions (Cu(II)). This copper activation mechanism is separate from the cysteine switch, involving specific cysteine residues in the catalytic domain for copper binding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Protease activation is crucial for various biological processes.
  • Latent proteases often require specific mechanisms for activation.
  • ADAM 12, a metalloprotease, plays roles in cell adhesion and signaling.

Purpose of the Study:

  • To investigate the activation mechanism of the disintegrin metalloprotease ADAM 12-S.
  • To determine the role of copper ions (Cu(II)) in ADAM 12-S activation.
  • To elucidate the relationship between the cysteine switch and copper-dependent activation.

Main Methods:

  • Site-directed mutagenesis of ADAM 12 propeptide and catalytic domain cysteine residues.
  • Enzymatic activity assays to measure ADAM 12-S activation.

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  • Biochemical analysis of copper binding effects on protease activity.

    • Main Results:

    • ADAM 12-S is activated by Cu(II), indicating a novel activation pathway.
    • Copper activation is independent of the canonical cysteine switch in the propeptide.
    • Mutation of a specific unpaired cysteine in the catalytic domain abolished copper sensitivity.
    • Furin cleavage and copper binding appear to be sequential steps in ADAM 12 activation.

    Conclusions:

    • Copper ions are direct activators of ADAM 12-S.
    • ADAM 12 activation involves a multi-step process including furin cleavage and copper binding.
    • The catalytic domain's cysteine residue is essential for copper-mediated activation, distinct from the propeptide's cysteine switch.