1998
DOI: 10.1590/s0100-879x1998000500002
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Abstract: The present review deals with the stages of synthesis and processing of asparagine-linked oligosaccharides occurring in the lumen of the endoplasmic reticulum and their relationship to the acquisition by glycoproteins of their proper tertiary structures. Special emphasis is placed on reactions taking place in trypanosomatid protozoa since their study has allowed the detection of the transient glucosylation of glycoproteins catalyzed by UDP-Glc:glycoprotein glucosyltransferase and glucosidase II. The former enz… Show more

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Cited by 17 publications
(8 citation statements)
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“…The latter confirmed previous studies [56], and detection of glucosyltransferase I also confirmed an earlier analysis [33]. Interestingly, despite the absence of a Glc 3 Man 9 precursor glycan from trypanosomatid nascent polypeptides [32], an ERQC system based on monitoring of protein-folding via transient reglucosylation cycles can be reconstructed in silico . Further, this system includes the PDI-related factors ERp52 and ERp72, which interact with calnexin/calreticulin; this system, together with the Ero1/ERp44 complex is fully represented (Table 1).…”
Section: Resultssupporting
confidence: 86%
See 1 more Smart Citation
“…The latter confirmed previous studies [56], and detection of glucosyltransferase I also confirmed an earlier analysis [33]. Interestingly, despite the absence of a Glc 3 Man 9 precursor glycan from trypanosomatid nascent polypeptides [32], an ERQC system based on monitoring of protein-folding via transient reglucosylation cycles can be reconstructed in silico . Further, this system includes the PDI-related factors ERp52 and ERp72, which interact with calnexin/calreticulin; this system, together with the Ero1/ERp44 complex is fully represented (Table 1).…”
Section: Resultssupporting
confidence: 86%
“…Significantly, ongoing VSG biosynthesis is essential as suppression leads to growth arrest [31]. Trypanosomatids lack the Glc 3 Man 9 GlcNAc 2 structure, but do transfer a Glc 1 Man 9 GlcNAc 2 oligosaccharide to nascent chains [32]. Glc 1 Man 9 GlcNAc 2 is capable of transient deglucosylation/reglucosylation [20], [33].…”
Section: Introductionmentioning
confidence: 99%
“…Interestingly, both HUT1L and AtUTr1 bear a C-terminal lysine-rich motif implicated in ER localization (61). Within the ER, AtUTr1 participates in the unfolded protein response, through provision of ER UDP-Glc required for the glucosylation/glucosidase cycle occurring as part of protein folding and quality control (29,62,63). Were Leishmania HUT1L similarly involved in the protein folding cycle in Leishmania, its loss could prove lethal to the cell, since unlike other organisms, the core glycans added to nascent trypanosomatid glycoproteins lack Glc residues and must necessarily be acquired in the ER (64).…”
Section: Discussionmentioning
confidence: 99%
“…16). If the recognition signal constituted by the monoglucosylated glycan (GlcMan 9 GlcNAc 2 ) is prematurely clipped off by a glucosidase II, incompletely folded glycoproteins can still be recognized by UDP-Glc: glycoprotein glucosyltransferase and relabeled for retention in the endoplasmic reticulum [304,305]. As with UDP-N-acetylglucosamine:lysosomal enzyme Nacetylglucosamine-1-phosphotransferase and UDP-Nacetylgalactosamine:glycoprotein hormone N-acetylgalactosaminyltransferase, a recognition site on the target glycoprotein is indispensable for this glycosyltransferase to regenerate monoglucosylated N-glycans [101].…”
Section: Review Articlementioning
confidence: 99%