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 (AChE H) and of type T (AChE T) are the most important: AChE H subunits produced glycolipid (GPI)-anchored dimers and AChE T subunits produce hetero-oligometric forms such as membrane-bound tetramer 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 cholinegic synapses.
Published Version
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