Acetylcholinesterase: C-terminal domains, molecular forms and functional localization.
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.
Massoulié
J
J
Laboratoire de Neurobiologie Cellulaire et Moléculaire, CNRS-URA 1857, Paris, France.
Anselmet
A
A
Bon
S
S
Krejci
E
E
Legay
C
C
Morel
N
N
Simon
S
S
D000110:Acetylcholinesterase / Q000032:analysis / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000737:chemistry; D006801:Humans; D007527:Isoenzymes / Q000032:analysis / Q000737:chemistry*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D007527:Isoenzymes; D003094:Collagen; D000110:Acetylcholinesterase