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

被引:64
作者
Massoulie, J [1 ]
Anselmet, A [1 ]
Bon, S [1 ]
Krejci, E [1 ]
Legay, C [1 ]
Morel, N [1 ]
Simon, S [1 ]
机构
[1] Ecole Normale Super, CNRS, URA 1857, Neurobiol Cellulaire & Mol Lab, F-75230 Paris 05, France
关键词
acetylcholinesterase; anchoring; basal lamina; collagen;
D O I
10.1016/S0928-4257(98)80007-7
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
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 produce glycolipid (GPI)-anchored dimers and AChE(T) 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. ((C)Elsevier, Paris).
引用
收藏
页码:183 / 190
页数:8
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