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Calreticulin discriminates the proximal region at the N-glycosylation site of Glc1Man9GlcNAc2 ligand.

Posted by on in 2015
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Hirano M1Adachi Y1Ito Y2Totani K3. 2015. Biochem Biophys Res Commun. 466(3):350-5. doi: 10.1016/j.bbrc.2015.09.026. Epub 2015 Sep 9.

  • 1Department of Materials and Life Science, Seikei University, 3-3-1 Kichijoji-kita, Musashino, Tokyo 180-8633, Japan.
  • 2Synthetic Cellular Chemistry Laboratory, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan; ERATO, Japan Science and Technology Agency, Ito Glycotrilogy Project, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
  • 3Department of Materials and Life Science, Seikei University, 3-3-1 Kichijoji-kita, Musashino, Tokyo 180-8633, Japan. Electronic address: ktotani@st.seikei.ac.jp.

Abstract

 

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.

Copyright © 2015 Elsevier Inc. All rights reserved.

KEYWORDS:

Chaperone; Endoplasmic reticulum; Glycoprotein; Lectin; Thermal shift analysis

PMID:
 
26362185
 
[PubMed - indexed for MEDLINE]
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