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Posttranslational modification as a means of anchoring acetylcholinesterase to the cell surface

✍ Scribed by Israel Silman; Anthony H. Futerman


Publisher
Wiley (John Wiley & Sons)
Year
1987
Tongue
English
Weight
908 KB
Volume
26
Category
Article
ISSN
0006-3525

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✦ Synopsis


Acetylcholinesterase (AChE) exists in multiple molecular forms that differ in their quaternary structure and mode of attachment to the cell surface. Attachment is achieved by posttranslational modification of the catalytic subunits. Two such modifications are described. One modification involves the attachment to subunit tetramers, via disulfide bridges, of a collagen-like fibrous anchor that serves to attach the enzyme, by ionic interactions, to the extracellular matrix. A second modification involves the covalent attachment of a single phosphatidylinositol residue, which serves to anchor the enzyme hydrophobically in the lipid bilayer of the plasma membrane. The detailed molecular structure, assembly, and modes of anchoring of these two classes of AChE are discussed.


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