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Asparagine-linked glycosylation 6, alpha-1,3-glucosyltransferase homolog

ALG6
This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the first glucose residue to the growing lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene are associated with congenital disorders of glycosylation type Ic. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CDG-Ia, ALG8, alg5, Alpha-1, Transferrin
Papers on ALG6
Electroclinical Features of Early-Onset Epileptic Encephalopathies in Congenital Disorders of Glycosylation (CDGs).
New
Jaeken et al., Catania, Italy. In Jimd Rep, Nov 2015
We describe a series of patients with EOEE and genetically confirmed CDG (ALG3-CDG, ALG6-CDG, DPM2-CDG, ALG1-CDG).
Reduced expression of the oligosaccharyltransferase exacerbates protein hypoglycosylation in cells lacking the fully assembled oligosaccharide donor.
New
Gilmore et al., Worcester, United States. In Glycobiology, Jul 2015
We monitored glycosylation of proteins in asparagine-linked glycosylation 6 (ALG6) deficient cell lines that assemble Dol-PP-GlcNAc(2)Man(9) as the largest oligosaccharide donor.
Congenital disorders of glycosylation with emphasis on cerebellar involvement.
Review
Jaeken et al., Catania, Italy. In Semin Neurol, 2014
It has also been reported in some patients with ALG1-CDG, ALG3-CDG, ALG9-CDG, ALG6-CDG, ALG8-CDG, PIGA-CDG, DPM1-CDG, DPM2-CDG, B4GALT1-CDG, SLC35A2-CDG, COG1-CDG, COG5-CDG, COG7-CDG, and COG8-CDG.
Functional and evolutionary analysis of the AP1/SEP/AGL6 superclade of MADS-box genes in the basal eudicot Epimedium sagittatum.
Wang et al., Beijing, China. In Ann Bot, 2014
Yeast three-hybrid analysis revealed that EsFUL1-like, EsAGL6-like and EsAGL2-1 (representing the three major lineages of the Epimedium AGL/SEP/ALG6 superclade) could act as bridging proteins in ternary complexes with both EsAP3-2 (B class) and EsPI (B class), which do not heterodimerize themselves.
PMM2-CDG: phenotype and genotype in four affected family members.
Severini et al., Trieste, Italy. In Gene, 2014
The most severely affected member had in addition an ALG6 mutation known to exacerbate the phenotype of patients with PMM2-CDG.
Congenital disorder of glycosylation type Ic: report of a Japanese case.
Okamoto et al., Odawara, Japan. In Brain Dev, 2013
CDG-Ic is caused by mutation in the ALG6 gene encoding alpha-1,3-glucosyltransferase.
ALG6-CDG in South Africa: Genotype-Phenotype Description of Five Novel Patients.
Jaeken et al., Potchefstroom, South Africa. In Jimd Rep, 2012
ALG6-CDG (formerly named CDG-Ic) (phenotype OMIM 603147, genotype OMIM 604566), is caused by defective endoplasmic reticulum α-1,3-glucosyltransferase (E.C 2.4.1.267)
Genome-wide linkage and copy number variation analysis reveals 710 kb duplication on chromosome 1p31.3 responsible for autosomal dominant omphalocele.
Butler et al., Genève, Switzerland. In J Med Genet, 2012
The 710 kb duplication at 1p31.3 band contains seven known genes including FOXD3, ALG6, ITGB3BP, KIAA1799, DLEU2L, PGM1, and the proximal portion of ROR1.
Frequency Determination of α-1,3 Glucosyltransferase p.Y131H and p.F304S Polymorphisms in the Croatian Population Revealed Five Novel Single Nucleotide Polymorphisms in the hALG6 Gene.
GeneRIF
Dumic et al., Zagreb, Croatia. In Genet Test Mol Biomarkers, 2012
Five novel base substitutions in the hALG6 gene were also found: three in exon 5 (c.383T>C, c.390G>A, and c.429G>C) and two in a downstream intervening sequence (IVS5+17C/T and IVS5+34G/A).
Engineering Yarrowia lipolytica to produce glycoproteins homogeneously modified with the universal Man3GlcNAc2 N-glycan core.
Callewaert et al., Gent, Belgium. In Plos One, 2011
To avoid underoccupancy of glycosylation sites, we concomitantly overexpressed ALG6.
Pubertal development in ALG6 deficiency (congenital disorder of glycosylation type Ic).
Sarafoglou et al., Minneapolis, United States. In Mol Genet Metab, 2011
Information on the hypothalamic pituitary ovarian axis in congenital disorders of glycosylation (CDG) females is scarce.
Analysis and metabolic engineering of lipid-linked oligosaccharides in glycosylation-deficient CHO cells.
Krag et al., Baltimore, United States. In Biochem Biophys Res Commun, 2010
B4-2-1 cells, which have a mutation in the dolichol phosphate-mannose synthase (DPM2) gene, accumulated LLO with the structure Man(5)GlcNAc(2)-P-P-Dol, while MI8-5 cells, which lack glucosyltransferase I (ALG6) activity, accumulated Man(9)GlcNAc(2)-P-P-Dol. CHO-K1 and MI5-4 cells both produced primarily the complete LLO, Glc(3)Man(9)GlcNAc(2)-P-P-Dol, though the relative quantity was lower in MI5-4.
A novel mutation and first report of dilated cardiomyopathy in ALG6-CDG (CDG-Ic): a case report.
Jaeken et al., Riyadh, Saudi Arabia. In Orphanet J Rare Dis, 2009
ALG6-CDG (CDGIc) is an endoplasmatic reticulum defect in N-glycan assembly.
Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides.
Review
Hennet et al., Zürich, Switzerland. In Hum Mutat, 2009
This review sets the state of the art by listing all mutations identified in the 15 genes (PMM2, MPI, DPAGT1, ALG1, ALG2, ALG3, ALG9, ALG12, ALG6, ALG8, DOLK, DPM1, DPM3, MPDU1, and RFT1) that yield a deficiency of dolichol-linked oligosaccharide biosynthesis.
Congenital disorder of glycosylation Ic due to a de novo deletion and an hALG-6 mutation.
GeneRIF
Freeze et al., Los Angeles, United States. In Biochem Biophys Res Commun, 2006
Our findings extend the causes of CDG to larger DNA deletions and identify the first Japanese CDG-Ic mutation.
A frequent mild mutation in ALG6 may exacerbate the clinical severity of patients with congenital disorder of glycosylation Ia (CDG-Ia) caused by phosphomannomutase deficiency.
GeneRIF
Freeze et al., Los Angeles, United States. In Hum Mol Genet, 2002
A frequent mild mutation in ALG6 may exacerbate the clinical severity of patients with congenital disorder of glycosylation Ia (CDG-Ia) caused by phosphomannomutase deficiency.
Balancing N-linked glycosylation to avoid disease.
Review
Westphal et al., Los Angeles, United States. In Biochimie, 2001
Another disorder, CDG-Ic, is caused by mutations in ALG6, an alpha 1,3glucosyl transferase used for lipid-linked precursor synthesis, yet some function-compromising mutations occur at a high frequency in this gene also.
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