Title : N-linked glycosylation of
proline-rich membrane anchor (
PRiMA ) is not required for assembly and trafficking of globular tetrameric
acetylcholinesterase
Abstract :
- Acetylcholinesterase ( AChE ) is organized into globular tetramers ( G(4) ) 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 ( AChE ( T ))
- The glycosylation of AChE ( T ) 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 AChE ( T ), 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
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. glycosylation, , PRiMA, -, -
- 0. glycosylation, , acetylcholinesterase, -, -
- 3. glycosylation, , AChE, -, -
- 3. glycosylation, , T, -, -
- 4. glycoprotein, , PRiMA, -, -
- 4. glycoprotein, , glycoprotein, -, -
- 4. glycosylation, , -, -, sites
- 5. glycosylation, , PRiMA, -, asparagine-43
- 5. glycosylation, , PRiMA, -, site
- 6. glycosylation, , PRiMA, -, -
- 7. glycoproteins, , glycoproteins, -, -
- 7. glycosylation, , glycoproteins, -, -
Output(Part-Of) (sent_index,
protein,
site):
- 4. PRiMA, sites
- 4. glycoprotein, sites
- 5. PRiMA, asparagine-43
- 5. PRiMA, site
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 5. PRiMA, -, asparagine-43