Acetylcholinesterase: C-terminal domains, molecular forms and functional localization

J Physiol Paris. Jun-Aug 1998;92(3-4):183-90. doi: 10.1016/s0928-4257(98)80007-7.

Abstract

Acetylcholinesterase (AChE) possesses short C-terminal peptides that are not necessary for catalytic activity. These peptides belong to different classes (R, H, T, S) and define the post-translational processing and targeting of the enzyme. In vertebrates, subunits of type H (AChEH) and of type T (AChET) are the most important: AChEH subunits produce glycolipid (GPI)-anchored dimers and AChET subunits produce hetero-oligomeric forms such as membrane-bound tetramers in the mammalian brain (containing a 20 kDa hydrophobic protein) and asymmetric collagen-tailed forms in neuromuscular junctions (containing a specific collagen, ColQ). The T peptide allows the formation of tetrameric assemblies with a proline-rich attachment domain (PRAD) of collagen ColQ. These complex molecular structures condition the functional localization of the enzyme in the supramolecular architecture of cholinergic synapses.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylcholinesterase / analysis
  • Acetylcholinesterase / chemistry*
  • Amino Acid Sequence
  • Animals
  • Collagen / chemistry
  • Humans
  • Isoenzymes / analysis
  • Isoenzymes / chemistry*
  • Molecular Sequence Data
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary*
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • Isoenzymes
  • Collagen
  • Acetylcholinesterase