Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 38, Pages 32948-32961Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.261248
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Funding
- Research Grants Council of Hong Kong [662407, 660409, 662911, F-HK21/06T]
- Croucher Foundation [CAS-CF07/08.SC03]
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Acetylcholinesterase (AChE) anchors onto cell membranes by a transmembrane protein PRiMA (proline-rich membrane anchor) as a tetrameric form in vertebrate brain. The assembly of AChE tetramer with PRiMA requires the C-terminal t-peptide in AChE catalytic subunit (AChE(T)). Although mature AChE is well known N-glycosylated, the role of glycosylation in forming the physiologically active PRiMA-linked AChE tetramer has not been studied. Here, several lines of evidence indicate that the N-linked glycosylation of AChET plays a major role for acquisition of AChE full enzymatic activity but does not affect its oligomerization. The expression of the AChET mutant, in which all N-glycosylation sites were deleted, together with PRiMA in HEK293T cells produced a glycan-depleted PRiMA-linked AChE tetramer but with a much higher K-m value as compared with the wild type. This glycan-depleted enzyme was assembled in endoplasmic reticulum but was not transported to Golgi apparatus or plasma membrane.
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