Mechanisms and principles of N-linked protein glycosylation

Schwarz, Flavio; Aebi, Markus

doi:10.1016/j.sbi.2011.08.005

Cited by 581 publications

(533 citation statements)

References 54 publications

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“…Duplication and diversification of single subunit OSTs seems to represent an alternative strategy to enlarge the array of proteins accessible for glycosylation (Schwarz and Aebi 2011). For instance, T. brucei and Leishmania major encode STT3 paralogs with distinct preferences for their polypeptide substrate (Parsaie Nasab et al 2008;Izquierdo et al 2009).…”

Section: The Oligosaccharyltransferase Complex Versus Single Proteinmentioning

confidence: 99%

“…Because N-glycosylation is essential for protein folding as well as quality control of this process, higher levels of glycosylation increase the chance of successful protein folding. Therefore the increasing complexity of the N-glycosylation process in the ER observed in eukaryotes might correlate with the selective pressure to accommodate as many N-glycosylation sites as possible (Schwarz and Aebi 2011).…”

Section: Cotranslational or Posttranslational Modification?mentioning

confidence: 99%

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N-Linked Protein Glycosylation in the Endoplasmic Reticulum

Breitling

Aebi

2013

Cold Spring Harbor Perspectives in Biology

228

201

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The attachment of glycans to asparagine residues of proteins is an abundant and highly conserved essential modification in eukaryotes. The N-glycosylation process includes two principal phases: the assembly of a lipid-linked oligosaccharide (LLO) and the transfer of the oligosaccharide to selected asparagine residues of polypeptide chains. Biosynthesis of the LLO takes place at both sides of the endoplasmic reticulum (ER) membrane and it involves a series of specific glycosyltransferases that catalyze the assembly of the branched oligosaccharide in a highly defined way. Oligosaccharyltransferase (OST) selects the Asn-X-Ser/Thr consensus sequence on polypeptide chains and generates the N-glycosidic linkage between the side-chain amide of asparagine and the oligosaccharide. This ER-localized pathway results in a systemic modification of the proteome, the basis for the Golgi-catalyzed modification of the N-linked glycans, generating the large diversity of N-glycoproteome in eukaryotic cells. This article focuses on the processes in the ER. Based on the highly conserved nature of this pathway we concentrate on the mechanisms in the eukaryotic model organism Saccharomyces cerevisiae.

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Section: The Oligosaccharyltransferase Complex Versus Single Proteinmentioning

confidence: 99%

Section: Cotranslational or Posttranslational Modification?mentioning

confidence: 99%

N-Linked Protein Glycosylation in the Endoplasmic Reticulum

Breitling

Aebi

2013

Cold Spring Harbor Perspectives in Biology

228

201

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“…eukaryotes, bacteria and archaea (Calo et al, 2010;Helenius & Aebi, 2004;Jones et al, 2009;Larkin & Imperiali, 2011;Nothaft & Szymanski, 2010;Schwarz & Aebi, 2011;Weerapana & Imperiali, 2006). Monophosphate lipid carriers are also used in the synthesis of bacterial cell envelope polymers such as peptidoglycan, lipopolysaccharides and teichoic acids (Bouhss et al, 2008;Cantagrel & Lefeber, 2011;de Kruijff et al, 2008;Lovering et al, 2012;Reusch & Salton, 1984;Swoboda et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…S1C) (Cantagrel & Lefeber, 2011;Helenius & Aebi, 2004;Larkin & Imperiali, 2011;Schwarz & Aebi, 2011;Welti, 2013). This review will focus on the enzymes in eukaryotes and prokaryotes that generate the monophosphorylated lipid carrier either through phosphorylation of the alcohol or dephosphorylation of the pyrophosphate polyisoprenoid moiety, with the latter being coupled to de novo synthesis of the lipid carrier or through a recycling pathway.…”

Section: Introductionmentioning

confidence: 99%

Conservation of the PTEN catalytic motif in the bacterial undecaprenyl pyrophosphate phosphatase, BacA/UppP

Bickford

Nick

2013

Microbiology

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Isoprenoid lipid carriers are essential in protein glycosylation and bacterial cell envelope biosynthesis. The enzymes involved in their metabolism (synthases, kinases and phosphatases) are therefore critical to cell viability. In this review, we focus on two broad groups of isoprenoid pyrophosphate phosphatases. One group, containing phosphatidic acid phosphatase motifs, includes the eukaryotic dolichyl pyrophosphate phosphatases and proposed recycling bacterial undecaprenol pyrophosphate phosphatases, PgpB, YbjB and YeiU/LpxT. The second group comprises the bacterial undecaprenol pyrophosphate phosphatase, BacA/UppP, responsible for initial formation of undecaprenyl phosphate, which we predict contains a tyrosine phosphate phosphatase motif resembling that of the tumour suppressor, phosphatase and tensin homologue (PTEN). Based on protein sequence alignments across species and 2D structure predictions, we propose catalytic and lipid recognition motifs unique to BacA/UppP enzymes. The verification of our proposed active-site residues would provide new strategies for the development of substratespecific inhibitors which mimic both the lipid and pyrophosphate moieties, leading to the development of novel antimicrobial agents.

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“…In eukaryotes, nascent polypeptide is N-glycosylated by the enzyme oligosaccharyltransferase (OTase) after entry into the endoplasmic reticulum (ER) lumen through the translocon [4,5,6]. N-glycans enhance the efficiency of glycoprotein folding in the ER by increasing the solubility of folding nascent polypeptide and by recruiting the disulfide isomerase ERp57 through the lectins calnexin and calreticulin [7,8,9,10].…”

Section: Introductionmentioning

confidence: 99%