Alg14 organizes the formation of a multiglycosyltransferase complex involved in initiation of lipid-linked oligosaccharide biosynthesis

Lu, Jishun; Takahashi, Tetsuo; Ohoka, Atsuko; Nakajima, Kazuyuki; Hashimoto, Ryo; Miura, Nobuaki; Tachikawa, Hiroyuki; Gao, Xiao‐Dong

doi:10.1093/glycob/cwr162

Cited by 47 publications

(39 citation statements)

References 46 publications

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“…3A), strongly supporting previous findings that Alg7p associates with Alg14p to form a hetero-oligomeric GPT/NAGT complex on the rER membrane in Saccharomyces cerevisiae, demonstrated with in vitro co-immunoprecipitation assays (16). Furthermore, we also recently demonstrated that the N-terminal domain of yeast Alg14p is essential for the formation of this enzymatic complex (17), strongly suggesting that the first two steps that initiate DLO synthesis are tightly coupled with each other, and that this process is highly conserved between yeast and humans.…”

Section: C-1 Halg7p Halg14p and Halg13p Form A Gpt/nagt Complexsupporting

confidence: 91%

Physical Interactions among Human Glycosyltransferases Involved in Dolichol-Linked Oligosaccharide Biosynthesis

Takahashi¹,

Gao²

2012

TIGG

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In eukaryotic glycoproteins, the N-glycan plays an important role with respect to both their structure and function. On the rough endoplasmic reticulum (rER) membrane, the N-glycan precursor is biosynthesized as a dolichol-linked oligosaccharide (DLO), which consists of fourteen sugars linked to pyrophosphoryl-dolichol. For completion of fulllength DLO (Glc 3 Man 9 GlcNAc 2 -PP-dolichol), activities of at least eleven glycosyltransferases localized on the rER membrane are essential. Although twelve human genes for these enzymes have been identified, any physical interactions among them have not yet been systematically analyzed. In this review, we describe several physical interactions among them that were uncovered using the yeast split-ubiquitin system. Moreover, on the basis of observations obtained by this technique, novel models for networking among human glycosyltransferases can be proposed.

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Section: C-1 Halg7p Halg14p and Halg13p Form A Gpt/nagt Complexsupporting

confidence: 91%

Physical Interactions among Human Glycosyltransferases Involved in Dolichol-Linked Oligosaccharide Biosynthesis

Takahashi¹,

Gao²

2012

TIGG

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“…A protein complex, encoded by the ALG13 and ALG14 loci transfers the second GlcNAc residue [31][32][33]. Interestingly, the UDP-GlcNAc utilising enzymes form a complex composed of Alg7p, Alg13p and Alg14p, whereby Alg14p is the organizing subunit [34,35].…”

Section: The Assembly Of the Lipid-linked Oligosaccharidementioning

confidence: 99%

N-linked protein glycosylation in the ER

Aebi

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

592

516

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N-linked protein glycosylation in the endoplasmic reticulum (ER) is a conserved two phase process in eukaryotic cells. It involves the assembly of an oligosaccharide on a lipid carrier, dolichylpyrophosphate and the transfer of the oligosaccharide to selected asparagine residues of polypeptides that have entered the lumen of the ER. The assembly of the oligosaccharide (LLO) takes place at the ER membrane and requires the activity of several specific glycosyltransferases. The biosynthesis of the LLO initiates at the cytoplasmic side of the ER membrane and terminates in the lumen where oligosaccharyltransferase (OST) selects N-X-S/T sequons of polypeptide and generates the N-glycosidic linkage between the side chain amide of asparagine and the oligosaccharide. The N-glycosylation pathway in the ER modifies a multitude of proteins at one or more asparagine residues with a unique carbohydrate structure that is used as a signalling molecule in their folding pathway. In a later stage of glycoprotein processing, the same systemic modification is used in the Golgi compartment, but in this process, remodelling of the N-linked glycans in a protein-, cell-type and species specific manner generates the high structural diversity of N-linked glycans observed in eukaryotic organisms. This article summarizes the current knowledge of the N-glycosylation pathway in the ER that results in the covalent attachment of an oligosaccharide to asparagine residues of polypeptide chains and focuses on the model organism Saccharomyces cerevisiae. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum.

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“…It was proposed that Alg7p, Alg13p, and Alg14p form a complex that utilizes UDP-GlcNAc as the common substrate and facilitates efficient glycosylation by passing on LLO intermediates to consecutive active sites without diffusion (Noffz et al 2009). Investigations on this complex formation indicated that Alg14p serves as the central organizing subunit that interacts with Alg13p and, in addition, recruits Alg7p into the complex (Lu et al 2012).…”

Section: Initial Steps Of Llo Biosynthesis On the Cytoplasmic Side Ofmentioning

confidence: 99%

N-Linked Protein Glycosylation in the Endoplasmic Reticulum

Breitling

Aebi

2013

Cold Spring Harbor Perspectives in Biology

228

203

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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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Alg14 organizes the formation of a multiglycosyltransferase complex involved in initiation of lipid-linked oligosaccharide biosynthesis

Cited by 47 publications

References 46 publications

Physical Interactions among Human Glycosyltransferases Involved in Dolichol-Linked Oligosaccharide Biosynthesis

Physical Interactions among Human Glycosyltransferases Involved in Dolichol-Linked Oligosaccharide Biosynthesis

N-linked protein glycosylation in the ER

N-Linked Protein Glycosylation in the Endoplasmic Reticulum

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