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Calreticulin discriminates the proximal region at the N-glycosylation site of Glc1Man9GlcNAc2 ligand.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2015 Oct 23; Vol. 466 (3), pp. 350-5. Date of Electronic Publication: 2015 Sep 09. - Publication Year :
- 2015
-
Abstract
- Calreticulin (CRT) is well known as a lectin-like chaperone that recognizes Glc1Man9GlcNAc2 (G1M9)-glycoproteins in the endoplasmic reticulum (ER). However, whether CRT can directly interact with the aglycone moiety (protein portion) of the glycoprotein remains controversial. To improve our understanding of CRT interactions, structure-defined G1M9-derivatives with different aglycones (-OH, -Gly-NH2, and -Gly-Glu-(t)Bu) were used as CRT ligands, and their interactions with recombinant CRT were analyzed using thermal shift analysis. The results showed that CRT binds strongly to a G1M9-ligand in the order -Gly-Glu-(t)Bu > -Gly-NH2 > -OH, which is the same as that of the reglucosylation of Man9GlcNAc2 (M9)-derivatives by the folding sensor enzyme UGGT (UDP-glucose: glycoprotein glucosyltransferase). Our results indicate that, similar to UGGT, CRT discriminates the proximal region at the N-glycosylation site, suggesting a similar mechanism mediating the recognition of aglycone moieties in the ER glycoprotein quality control system.<br /> (Copyright © 2015 Elsevier Inc. All rights reserved.)
- Subjects :
- Acetylglucosamine chemistry
Animals
Binding Sites
Chickens
Endoplasmic Reticulum metabolism
Glucosyltransferases chemistry
Glycoproteins chemistry
Glycosylation
Hot Temperature
Hydrophobic and Hydrophilic Interactions
Immunoglobulins chemistry
Ligands
Molecular Chaperones chemistry
Protein Binding
Protein Folding
Recombinant Proteins chemistry
Calreticulin metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 466
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 26362185
- Full Text :
- https://doi.org/10.1016/j.bbrc.2015.09.026