N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase-Reference-Cited by-同舟云学术

N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase

Published:2012-08 Issue:1 Volume:523 Page:71-75
ISSN:0304-3940
Container-title:Neuroscience Letters
language:en
Short-container-title:Neuroscience Letters

Author:

Chan Wallace K.B.,Chen Vicky P.,Luk Wilson K.W.,Choi Roy C.Y.,Tsim Karl W.K.

Publisher

Elsevier BV

Subject

General Neuroscience

Reference26 articles.

1. The C-terminal t peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathway;Belbeoc’h;EMBO Journal,2003

2. The membrane anchor of mammalian brain acetylcholinesterase consists of a single glycosylated protein of 22kDa;Boschetti;FEBS Letters,1996

3. The assembly of PRiMA-linked acetylcholinesterase: glycosylation is required for enzymatic activity but not for oligomerization;Chen;Journal of Biological Chemistry,2011

4. The PRiMA-linked cholinesterase tetramers are assembled from homodimers: hybrid molecules composed of acetylcholinesterase and butyrylcholinesterase dimers are up-regulated during development of chicken brain;Chen;Journal of Biological Chemistry,2010

5. Calcitonin gene-related peptide increases the expression of acetylcholinesterase in cultured chick myotubes;Choi;Neuroscience Letters,1996

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4. Presenilin-1 influences processing of the acetylcholinesterase membrane anchor PRiMA;Neurobiology of Aging;2014-07

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