The Assembly of Proline-rich Membrane Anchor (PRiMA)-linked Acetylcholinesterase Enzyme GLYCOSYLATION IS REQUIRED FOR ENZYMATIC ACTIVITY BUT NOT FOR OLIGOMERIZATION
作者： Vicky P. Chen , Roy C. Y. Choi , Wallace K. B. Chan , K. Wing Leung , Ava J. Y. Guo
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摘要: Acetylcholinesterase (AChE) anchors onto cell membranes by a transmembrane protein PRiMA (proline-rich membrane anchor) as tetrameric form in vertebrate brain. The assembly of AChE tetramer with requires the C-terminal “t-peptide” catalytic subunit (AChET). Although mature is well known N-glycosylated, role glycosylation forming physiologically active PRiMA-linked has not been studied. Here, several lines evidence indicate that N-linked AChET plays major for acquisition full enzymatic activity but does affect its oligomerization. expression mutant, which all N-glycosylation sites were deleted, together HEK293T cells produced glycan-depleted much higher Km value compared wild type. This enzyme was assembled endoplasmic reticulum transported to Golgi apparatus or plasma membrane.
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