Membrane-proximal domain of a disintegrin and metalloprotease-17 represents the putative molecular switch of its shedding activity operated by protein-disulfide isomerase.

@article{Dsterhft2013MembraneproximalDO,
  title={Membrane-proximal domain of a disintegrin and metalloprotease-17 represents the putative molecular switch of its shedding activity operated by protein-disulfide isomerase.},
  author={Stefan D{\"u}sterh{\"o}ft and Sascha Jung and Chien-Wen Hung and Andreas Tholey and Frank D. S{\"o}nnichsen and Joachim Gr{\"o}tzinger and Inken Lorenzen},
  journal={Journal of the American Chemical Society},
  year={2013},
  volume={135 15},
  pages={5776-81}
}
A disintegrin and metalloprotease-17 (ADAM17) is a major sheddase responsible for the regulation of a wide range of biological processes, like cellular differentiation, regeneration, or cancer progression. Hitherto, the mechanism regulating the enzymatic activity of ADAM17 is poorly understood. Recently, protein-disulfide isomerase (PDI) was shown to interact with ADAM17 and to down-regulate its enzymatic activity. Here we demonstrate by NMR spectroscopy and tandem-mass spectrometry that PDI… CONTINUE READING