کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4344441 | 1296655 | 2012 | 5 صفحه PDF | دانلود رایگان |
Acetylcholinesterase (AChE) is organized into globular tetramers (G4) by a structural protein called proline-rich membrane anchor (PRiMA), anchoring it into the cell membrane of neurons in the brain. The assembly of AChE tetramers with PRiMA requires the presence of a C-terminal “t-peptide” in the AChE catalytic subunit (AChET). The glycosylation of AChET is known to be required for its proper assembly and trafficking; however, the role of PRiMA glycosylation in the oligomer assembly has not been revealed. PRiMA is a glycoprotein containing two putative N-linked glycosylation sites. By using site-directed mutagenesis, the asparagine-43 was identified to be the N-linked glycosylation site of PRiMA. Abolishing glycosylation on mouse PRiMA appeared not to affect its assembly with AChET, the enzymatic properties of AChE, and the membrane trafficking of PRiMA-linked AChE tetramers. This result is contrary to the reports that glycosylation is essential for conformation and trafficking of membrane glycoproteins.
► PRiMA is a glycoprotein containing a single N-glycosylation site at asparagin-43.
► N-glycosylation of PRiMA is not essential for the formation of G4 AChE.
► N-glycosylation of PRiMA is not required for the membrane trafficking of G4 AChE.
Journal: Neuroscience Letters - Volume 523, Issue 1, 8 August 2012, Pages 71–75