L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth.

@article{Maretzky2005L1IS,
  title={L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth.},
  author={Thorsten Maretzky and Marc Schulte and Andreas Ludwig and Stefan Rose-John and Carl P Blobel and Dieter Hartmann and Peter Altevogt and Paul Saftig and Karina Reiss},
  journal={Molecular and cellular biology},
  year={2005},
  volume={25 20},
  pages={9040-53}
}
The immunoglobulin superfamily recognition molecule L1 plays important functional roles in the developing and adult nervous system. Metalloprotease-mediated cleavage of this adhesion molecule has been shown to stimulate cellular migration and neurite outgrowth. We demonstrate here that L1 cleavage is mediated by two distinct members of the disintegrin and metalloprotease family, ADAM10 and ADAM17. This cleavage is differently regulated and leads to the generation of a membrane bound C-terminal… CONTINUE READING
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