scholarly journals Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control

2016 ◽  
Vol 25 (11) ◽  
pp. 2095-2101 ◽  
Author(s):  
Tadashi Satoh ◽  
Takayasu Toshimori ◽  
Masanori Noda ◽  
Susumu Uchiyama ◽  
Koichi Kato
Keyword(s):  
Quality Control ◽  
Regulatory Subunits ◽  
Glucosidase Ii ◽  
Interaction Mode ◽  
Glycoprotein Quality Control

scholarly journals Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Tadashi Satoh ◽  
Takayasu Toshimori ◽  
Gengwei Yan ◽  
Takumi Yamaguchi ◽  
Koichi Kato
Keyword(s):  
Quality Control ◽  
Structural Basis ◽  
Glucosidase Ii ◽  
Glycoprotein Quality Control

scholarly journals Trypanosoma cruziCalreticulin Is a Lectin That Binds Monoglucosylated Oligosaccharides but Not Protein Moieties of Glycoproteins

1999 ◽  
Vol 10 (5) ◽  
pp. 1381-1394 ◽  
Author(s):  
Carlos Labriola ◽  
Juan J. Cazzulo ◽  
Armando J. Parodi
Keyword(s):  
Quality Control ◽  
Mammalian Cells ◽  
Protozoan Parasite ◽  
Glucosidase Ii ◽  
The Third ◽  
Oligosaccharide Processing ◽  
Encoding Gene ◽  
Higher Eukaryotes ◽  
Lysosomal Proteinase ◽  
Protein Moiety

Trypanosoma cruzi is a protozoan parasite that belongs to an early branch in evolution. Although it lacks several features of the pathway of protein N-glycosylation and oligosaccharide processing present in the endoplasmic reticulum of higher eukaryotes, it displays UDP-Glc:glycoprotein glucosyltransferase and glucosidase II activities. It is herewith reported that this protozoan also expresses a calreticulin-like molecule, the third component of the quality control of glycoprotein folding. No calnexin-encoding gene was detected. Recombinant T. cruzi calreticulin specifically recognized free monoglucosylated high-mannose-type oligosaccharides. Addition of anti-calreticulin serum to extracts obtained from cells pulse–chased with [35S]Met plus [35S]Cys immunoprecipitated two proteins that were identified as calreticulin and the lysosomal proteinase cruzipain (a major soluble glycoprotein). The latter but not the former protein disappeared from immunoprecipitates upon chasing cells. Contrary to what happens in mammalian cells, addition of the glucosidase II inhibitor 1-deoxynojirimycin promoted calreticulin–cruzipain interaction. This result is consistent with the known pathway of proteinN-glycosylation and oligosaccharide processing occurring in T. cruzi. A treatment of the calreticulin-cruzipain complexes with endo-β-N-acetylglucosaminidase H either before or after addition of anti-calreticulin serum completely disrupted calreticulin–cruzipain interaction. In addition, mature monoglucosylated but not unglucosylated cruzipain isolated from lysosomes was found to interact with recombinant calreticulin. It was concluded that the quality control of glycoprotein folding appeared early in evolution, and that T. cruzi calreticulin binds monoglucosylated oligosaccharides but not the protein moiety of cruzipain. Furthermore, evidence is presented indicating that glucosyltransferase glucosylated cruzipain at its last folding stages.

scholarly journals Malectin Participates in a Backup Glycoprotein Quality Control Pathway in the Mammalian ER

PLoS ONE ◽  
2011 ◽  
Vol 6 (1) ◽  
pp. e16304 ◽  
Author(s):  
Carmela Galli ◽  
Riccardo Bernasconi ◽  
Tatiana Soldà ◽  
Verena Calanca ◽  
Maurizio Molinari
Keyword(s):  
Quality Control ◽  
Glycoprotein Quality Control

scholarly journals UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control

2010 ◽  
Vol 21 (5) ◽  
pp. 491-499 ◽  
Author(s):  
Cecilia D’Alessio ◽  
Julio J. Caramelo ◽  
Armando J. Parodi
Keyword(s):  
Quality Control ◽  
Er Quality Control ◽  
Glucosidase Ii

Design and Synthesis of Oligosaccharides that Interfere with Glycoprotein Quality-control systems

ChemBioChem ◽  
2005 ◽  
Vol 6 (12) ◽  
pp. 2281-2289 ◽  
Author(s):  
Midori A. Arai ◽  
Ichiro Matsuo ◽  
Shinya Hagihara ◽  
Kiichiro Totani ◽  
Jun-ichi Maruyama ◽  
...  
Keyword(s):  
Quality Control ◽  
Control Systems ◽  
Design And Synthesis ◽  
Glycoprotein Quality Control

Dissecting glycoprotein quality control in the secretory pathway

2001 ◽  
Vol 26 (10) ◽  
pp. 619-624 ◽  
Author(s):  
Christopher M Cabral ◽  
Yan Liu ◽  
Richard N Sifers
Keyword(s):  
Quality Control ◽  
Secretory Pathway ◽  
Glycoprotein Quality Control

scholarly journals A Novel Route for F-box Protein-mediated Ubiquitination Links CHIP to Glycoprotein Quality Control

2006 ◽  
Vol 281 (29) ◽  
pp. 20242-20251 ◽  
Author(s):  
Rick F. Nelson ◽  
Kevin A. Glenn ◽  
Victor M. Miller ◽  
Hsiang Wen ◽  
Henry L. Paulson
Keyword(s):  
Quality Control ◽  
F Box Protein ◽  
Glycoprotein Quality Control
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