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Posttranslational modification as a means of anchoring acetylcholinesterase to the cell surface
Author(s) -
Silman Israel,
Futerman Anthony H.
Publication year - 1987
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360260021
Subject(s) - chemistry , anchoring , acetylcholinesterase , covalent bond , biophysics , protein subunit , enzyme , membrane , biochemistry , stereochemistry , organic chemistry , structural engineering , gene , engineering , biology
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.