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The Glycolipid-Addition Signal of Acetylcholinesterase

Cellular Compartmentation, Cleavage, GPI Addition and Secretion
  • Suzanne Bon
  • Françoise Coussen
  • Jean Massoulié

Abstract

Various types of acetylcholinesterase (AChE) subunits are characterized by specific C-terminal peptides. In Torpedo and mammals, alternative exons encode H peptides, which contain a C-terminal signal for glypiation, i. e. cleavage and addition of a glycolipid (GPI) anchor. The H peptides of Torpedo and rat AChE show no homology, except for the presence of cysteines at their N-terminal end, allowing the formation of disulfide-linked dimers, and of a C-terminal hydrophobic region.

Keywords

AChE Activity Hydrophobic Region Chimeric Protein Wide Context Retention Signal 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Suzanne Bon
    • 1
  • Françoise Coussen
    • 1
  • Jean Massoulié
    • 1
  1. 1.Neurobiologie Cellulaire et MoléculaireCNRS URA 1857, Ecole Normale SupérieureParisFrance

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