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Congenital Disorders of Glycosylation
Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
A novel homozygous mutation in the human ALG12 gene results in an aberrant profile of oligomannose N-glycans in patient's serum.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Novel ALG12 variants and hydronephrosis in siblings with impaired N-glycosylation.
Glioma
Characterization of the 5'-flanking region of the mouse asparagine-linked glycosylation 12 homolog gene.
Hydronephrosis
Novel ALG12 variants and hydronephrosis in siblings with impaired N-glycosylation.
Metabolic Diseases
A novel homozygous mutation in the human ALG12 gene results in an aberrant profile of oligomannose N-glycans in patient's serum.
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malfunction
loss-of-function mutations in EBS4 results in transfer of incompletely assembled glycans to polypeptides. The complete assembly of the lipid-linked glycans is essential for successful quality control of defective glycoproteins in Arabidopsis
malfunction
the alg12 mutant accumulates Manalpha1,2Manalpha1,2Manalpha1,3(Manalpha1,2Manalpha1,3Manalpha1,6)-Manbeta1,4-GlcNAcbeta1-4GlcNAcalpha/beta
malfunction
-
the variant surface glycoprotein sVSG221 synthesized by the ALG12-/- parasites shows different glycosylation patterns to that synthesized by wild-type cells, changes in sVSG221 glycosylation induced by the deletion of the ALG12 gene, overview
physiological function
-
oligosaccharyltransferase TbSTT3A is able to transfer Man7GlcNAc2 as well as Man5GlcNAc2 to its preferred acidic glycosylation site at residue Asn263 of variant surface protein. In a mutant lacking enzymic activity, i.e. in the absence of Man9GlcNAc2-PP-Dol, oligosaccharyltransferase TbSTT3B transfers both Man7GlcNAc2 and Man5GlcNAc2 to the remaining site at Asn428 of variant surface protein, albeit with low efficiency
physiological function
overexpression of enzyme in a dwarf mutant, bri1-9, the phenotypes of which are caused by endoplasmic reticulum retention and endoplasmic reticulum-associated degradation of a brassinosteroid receptor, BRASSINOSTEROID-INSENSITIVE 1, and a mutant lacking EBS3 activity, which catalyzes the ER luminal addition of two terminal alpha1,2 mannose residues in assembling the three-branched N-glycan precursor [glucose(Glc)]3(Man)9[N-acetylglucosamine(GlcNAc)]2, adds an alpha1,6-mannose to the truncated N-glycan precursor accumulated in the double mutant, promotes the bri1-9 endoplasmic reticulum-associated degradation, and neutralizes the EBS3 mutant suppressor phenotype
physiological function
-
the TbALG12 gene encodes the alpha1-6-mannosyltransferase that converts Man7GlcNAc2-PP-Dol to Man8GlcNAc2-PP-Dol
physiological function
-
generation of a HepG2 cell model of Alg12-congenital disorders of glycosylation by down-regulating dolichyl-P-mannose Man7GlcNAc2-PP-dolichol mannosyltransferase (Alg12), in order to provoke the accumulation of Man7GlcNAc2-PP-dolichol. The accumulation of Man7GlcNAc2-PP-dolichol in ALG12-downregulated cells coincides with the inhibition in cell growth noted between 4 and 8 days posttransfection. In down-regulated cells, brefeldin A provokes Golgi apparatus-endomannosidase trimming of Glc3Man9GlcNAc2-PP dolichol to yield a Man8GlcNAc2-PP-dolichol structure that does not give rise to cytoplasmic Man8GlcNAc2-P. Brefeldin A also strikingly increases oligosaccharyl phosphates derived from mature diphosphodolichol within the endomembrane system without affecting levels of Man7GlcNAc2-PP-dolichol or cytoplasmic Man7GlcNAc2-P
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E38K
the wild-type EBS4 gene but not the mutated EBS4 plasmid carrying the E38K mutation (ebs4-3) is able to complement the yeast DELTAalg12 mutation
R100W
residue R100 is located near the end of the largest luminal loop between the first two predicted transmembrane segments and is absolutely conserved in all known ALG9 enzymes. Mutation suppresses a dwarf mutant, bri1-9, the phenotypes of which are caused by endoplasmic reticulum retention and endoplasmic reticulum-associated degradation of a brassinosteroid receptor, BRASSINOSTEROID-INSENSITIVE 1, BR1. The mutation prevents the Glc3Man9GlcNAc2 assembly and inhibits the endoplasmic reticulum-associated degradation of bri1-9. Overexpression of EBS4 in the R100W bri1-9 mutant, which encodes the Arabidopsis ortholog of the yeast ALG12 catalyzing the ER luminal alpha1,6 Man addition, adds an alpha1,6 Man to the truncated N-glycan precursor accumulated in R100W bri1-9, promotes the bri1-9 endoplasmic reticulum-associated degradation, and neutralizes the R100W suppressor phenotype
T70I
mutation leads to attenuated calcium response to the bacterial flagellin flg22 peptide and several other elicitors. Mutant protein is correctly targeted to the plasma membrane, and several of the receptors expressed in the T70I background are underglycosylated
F142V
the F142V replacement in hALG12p is the cause of inefficient addition of the eighth mannose residue onto Man7GlcNAc2-PP-dolichol during glycoprotein biosynthesis in a patient with type I congenital disorders of glycosylation. The patient is homozygous for the point mutation that causes an amino acid substitution in a conserved region of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl alpha6-mannosyltransferase. Skin biopsy fibroblasts from a CDG I patient have a reduced capacity to add the eighth mannose residue onto the lipid-linked oligosaccharide precursor. The fibroblasts of the patient are capable of the direct transfer of Man7GlcNAc2 from dolichol onto protein and that this N-linked structure can be glucosylated by UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum
R146Q
congenital disorder of glycosylation type lg is identified in a child presenting with psychomotor retardation, hypotonia, growth retardation, dysmorphic features and anorexia. In the patients fibroblasts, the biosynthetic intermediate GlcNAc2Man7 oligosaccharide is detected both on the lipid carrier dolichyl pyrophosphate and on newly synthesized glycoproteins, pointing to a defect in the dolichyl pyrophosphateGlcNAc2Man7-dependent ALG12 alpha1,6 mannosyltransferase. Analysis of the ALG12 cDNA in the CDG patient revealed compound heterozygosity for two point mutations that result in the amino acid substitutions T67M and R146Q, respectively. The impact of these mutations on ALG12 protein function is investigated in the Saccharomyces cerevisiae alg12 glycosylation mutant by showing that the yeast ALG12 gene bearing the homologous mutations T61M and R161Q and the human mutant ALG12 cDNA alleles fail to normalize the growth defect phenotype of the alg12 yeast model, whereas expression of the normal ALG12 cDNA complements the yeast mutation. The ALG12 mannosyltransferase defect defines a type of congenital disorder of glycosylation, designated CDG-Ig
T67M
congenital disorder of glycosylation type lg is identified in a child presenting with psychomotor retardation, hypotonia, growth retardation, dysmorphic features and anorexia. In the patients fibroblasts, the biosynthetic intermediate GlcNAc2Man7 oligosaccharide is detected both on the lipid carrier dolichyl pyrophosphate and on newly synthesized glycoproteins, pointing to a defect in the dolichyl pyrophosphateGlcNAc2Man7-dependent ALG12 alpha1,6 mannosyltransferase. Analysis of the ALG12 cDNA in the CDG patient revealed compound heterozygosity for two point mutations that result in the amino acid substitutions T67M and R146Q, respectively. The impact of these mutations on ALG12 protein function is investigated in the Saccharomyces cerevisiae alg12 glycosylation mutant by showing that the yeast ALG12 gene bearing the homologous mutations T61M and R161Q and the human mutant ALG12 cDNA alleles fail to normalize the growth defect phenotype of the alg12 yeast model, whereas expression of the normal ALG12 cDNA complements the yeast mutation. The ALG12 mannosyltransferase defect defines a type of congenital disorder of glycosylation, designated CDG-Ig
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Chantret, I.; Dupre, T.; Delenda, C.; Bucher, S.; Dancourt, J.; Barnier, A.; Charollais, A.; Heron, D.; Bader-Meunier, B.; Danos, O.; Seta, N.; Durand, G.; Oriol, R.; Codogno, P.; Moore, S.E.H.
Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase
J. Biol. Chem.
277
25815-25822
2002
Homo sapiens (Q9BV10), Homo sapiens
brenda
Grubenmann, C.E.; Frank, C.G.; Kjaergaard, S.; Berger, E.G.; Aebi, M.; Hennet, T.
ALG12 mannosyltransferase defect in congenital disorder of glycosylation type Ig
Hum. Mol. Genet.
11
2331-2339
2002
Homo sapiens (Q9BV10), Homo sapiens
brenda
Cipollo, J.F.; Trimble, R.B.
The Saccharomyces cerevisiae alg12delta mutant reveals a role for the middle-arm alpha1,2Man- and upper-arm alpha1,2Manalpha1,6Man-residues of Glc(3)Man(9)GlcNAc(2)-PP-Dol in regulating glycoprotein glycan processing in the endoplasmic reticulum and Golgi apparatus
Glycobiology
12
749-762
2002
Saccharomyces cerevisiae (P53730), Saccharomyces cerevisiae
brenda
Hong, Z.; Jin, H.; Fitchette, A.C.; Xia, Y.; Monk, A.M.; Faye, L.; Li, J.
Mutations of an alpha1,6 mannosyltransferase inhibit endoplasmic reticulum-associated degradation of defective brassinosteroid receptors in Arabidopsis
Plant Cell
21
3792-3802
2009
Arabidopsis thaliana (A8MR93), Arabidopsis thaliana
brenda
Izquierdo, L.; Mehlert, A.; Ferguson, M.A.
The lipid-linked oligosaccharide donor specificities of Trypanosoma brucei oligosaccharyltransferases
Glycobiology
22
696-703
2012
Trypanosoma brucei
brenda
Hong, Z.; Kajiura, H.; Su, W.; Jin, H.; Kimura, A.; Fujiyama, K.; Li, J.
Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis
Proc. Natl. Acad. Sci. USA
109
11437-11442
2012
Arabidopsis thaliana (A8MR93)
brenda
Massarweh, A.; Bosco, M.E.; Iatmanen-Harbi, S.; Tessier, C.; Amana, L.; Busca, P.; Chantret, I.; Gravier-Pelletier, C.; Moore, S.E.
Brefeldin A promotes the appearance of oligosaccharyl phosphates (OSP) derived from Glc3Man9GlcNAc2-PP-dolichol within the endomembrane system of HepG2 cells
J. Lipid Res.
57
1477-1491
2016
Homo sapiens
brenda
Trempel, F.; Eschen-Lippold, L.; Bauer, N.; Ranf, S.; Westphal, L.; Scheel, D.; Lee, J.
A mutation in asparagine-linked glycosylation 12 (ALG12) leads to receptor misglycosylation and attenuated responses to multiple microbial elicitors
FEBS Lett.
2020
1873-3468
2020
Arabidopsis thaliana (A8MR93)
brenda
Sturiale, L.; Bianca, S.; Garozzo, D.; Terracciano, A.; Agolini, E.; Messina, A.; Palmigiano, A.; Esposito, F.; Barone, C.; Novelli, A.; Fiumara, A.; Jaeken, J.; Barone, R.
ALG12-CDG novel glycophenotype insights endorse the molecular defect
Glycoconj. J.
36
461-472
2019
Homo sapiens (Q9BV10), Homo sapiens
brenda
2.4.1.260 dolichyl-P-Man:Man7GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase
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