Exploration of oligosaccharide-protein interactions in glycoprotein quality control by synthetic approaches

2006 ◽  
Vol 6 (6) ◽  
pp. 290-302 ◽  
Author(s):  
Shinya Hagihara ◽  
Kiichiro Totani ◽  
Yukishige Ito
Keyword(s):  
Quality Control ◽  
Protein Interactions ◽  
Synthetic Approaches ◽  
Glycoprotein Quality Control

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

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

scholarly journals Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system

2011 ◽  
Vol 22 (16) ◽  
pp. 2810-2822 ◽  
Author(s):  
Shujuan Pan ◽  
Shufang Wang ◽  
Budi Utama ◽  
Lu Huang ◽  
Neil Blok ◽  
...  
Keyword(s):  
Quality Control ◽  
Golgi Complex ◽  
Mammalian Cells ◽  
Spatial Separation ◽  
Mechanistic Explanation ◽  
Binding Motif ◽  
Exact Role ◽  
Partial Redistribution ◽  
Rate Limiting ◽  
Glycoprotein Quality Control

The Golgi complex has been implicated as a possible component of endoplasmic reticulum (ER) glycoprotein quality control, although the elucidation of its exact role is lacking. ERManI, a putative ER resident mannosidase, plays a rate-limiting role in generating a signal that targets misfolded N-linked glycoproteins for ER-associated degradation (ERAD). Herein we demonstrate that the endogenous human homologue predominantly resides in the Golgi complex, where it is subjected to O-glycosylation. To distinguish the intracellular site where the glycoprotein ERAD signal is generated, a COPI-binding motif was appended to the N terminus of the recombinant protein to facilitate its retrograde translocation back to the ER. Partial redistribution of the modified ERManI was observed along with an accelerated rate at which N-linked glycans of misfolded α1-antitrypsin variant NHK were trimmed. Despite these observations, the rate of NHK degradation was not accelerated, implicating the Golgi complex as the site for glycoprotein ERAD substrate tagging. Taken together, these data provide a potential mechanistic explanation for the spatial separation by which glycoprotein quality control components operate in mammalian cells.

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