Glycoprotein Maturation and the UPR

Hülsmeier, Andreas J.; Welti, Michael; Hennet, Thierry

doi:10.1016/b978-0-12-385928-0.00010-9

Cited by 16 publications

(14 citation statements)

References 23 publications

(25 reference statements)

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“…In the ER, various chaperones directly assist folding of nascent peptides as they enter the ER lumen (Ma and Hendershot, 2004). The quality control (QC) machinery remodels the newly synthesized protein via multiple posttranslational modifications, including formation of disulfide bonds (Feige and Hendershot, 2011) and N-linked glycosylation (Hulsmeier et al , 2011). Failure to correctly complete these tasks can result in a misfolded protein.…”

Section: Introductionmentioning

confidence: 99%

Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells

Lajoie

Moir

Willis

et al. 2012

MBoC

101

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Section: Introductionmentioning

confidence: 99%

Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells

Lajoie

Moir

Willis

et al. 2012

MBoC

101

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“…[39] N-glycan is involved in protein transport in the endoplasmic reticulum and is essential for the initiation of various proteins. [40] Our analysis suggests that N-glycan structural changes may be common to these cancers.…”

Section: Identification Of Commonalities Among Different Diseasesmentioning

confidence: 77%

Omics‐based Identification of Glycan Structures as Biomarkers for a Variety of Diseases

Akiyoshi

Iwata

Berenger

et al. 2019

Molecular Informatics

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Glycans play important roles in cell communication, protein interaction, and immunity, and structural changes in glycans are associated with the regulation of a range of biological pathways involved in disease. However, our understanding of the detailed relationships between specific diseases and glycans is very limited. In this study, we proposed an omics-based method to investigate the correlations between glycans and a wide range of human diseases. We analyzed the gene expression patterns of glycogenes (glycosyltransferases and glycosidases) for 79 different diseases. A biological pathway-based glycogene signature was constructed to identify the alteration in glycan biosynthesis and the associated glycan structures for each disease state. The degradation of N-glycan and keratan sulfate, for example, may promote the growth or metastasis of multiple types of cancer, including endometrial, gastric, and nasopharyngeal. Our results also revealed that commonalities between diseases can be interpreted using glycogene expression patterns, as well as the associated glycan structure patterns at the level of the affected pathway. The proposed method is expected to be useful for understanding the relationships between glycans, glycogenes, and disease and identifying disease-specific glycan biomarkers.

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“…Product analysis of R707 glycosyltransferase assay -About 200 pmol of glycosyltransferase assay product were subjected to MALDI-MS analysis. MALDI-MS were acquired essentially as described earlier (13).…”

Section: Experimental/ Materials and Methodsmentioning

confidence: 99%

Giant mimivirus R707 encodes a glycogenin paralogue polymerizing glucose through α- and β-glycosidic linkages

Rommel

Hülsmeier

Jurt

et al. 2016

Biochemical Journal

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Acanthamoeba polyphaga mimivirus is a giant virus encoding 1262 genes among which many were previously thought to be exclusive to cellular life. For example, mimivirus genes encode enzymes involved in the biosynthesis of nucleotide sugars and putative glycosyltransferases. We identified in mimivirus a glycogenin-1 homologous gene encoded by the open reading frame R707. The R707 protein was found to be active as a polymerizing glucosyltransferase enzyme. Like glycogenin-1, R707 activity was divalent-metal-ion-dependent and relied on an intact DXD motif. In contrast with glycogenin-1, R707 was, however, not self-glucosylating. Interestingly, the product of R707 catalysis featured α1-6, β1-6 and α1-4 glycosidic linkages. Mimivirus R707 is the first reported glycosyltransferase able to catalyse the formation of both α and β linkages. Mimivirus-encoded glycans play a role in the infection of host amoebae. Co-infection of Acanthamoeba with mimivirus and amylose and chitin hydrolysate reduced the number of infected amoebae, thus supporting the importance of polysaccharide chains in the uptake of mimivirus by amoebae. The identification of a glycosyltransferase capable of forming α and β linkages underlines the peculiarity of mimivirus and enforces the concept of a host-independent glycosylation machinery in mimivirus.

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Glycoprotein Maturation and the UPR

Cited by 16 publications

References 23 publications

Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells

Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells

Omics‐based Identification of Glycan Structures as Biomarkers for a Variety of Diseases

Giant mimivirus R707 encodes a glycogenin paralogue polymerizing glucose through α- and β-glycosidic linkages

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