gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Phosphatidylinositol glycan anchor biosynthesis, class L

PIG-L, N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase, N-acetylglucosaminylphosphatidylinositol deacetylase, phosphatidylinositol glycan class L
catalyzes the N-deacetylation of N-acetyl-D-glucosaminylphosphatidylinositol in the second step of GPI anchor biosynthesis [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: ACID, STEP, PIG-M, HAD, FRAG1
Papers on PIG-L
Both PIGA and PIGL mutations cause GPI-a deficient isolates in the Tk6 cell line.
Albertini et al., Burlington, United States. In Environ Mol Mutagen, Oct 2015
To determine the molecular bases of the remaining GPI-a deficient isolates, real-time analysis for all the 25 autosomal GPI-a pathway genes was performed on the isolates without PIGA mutations, determining that PIGL mRNA was absent for many.
Mutations in PIGL in a patient with Mabry syndrome.
Aoki et al., Sendai, Japan. In Am J Med Genet A, Apr 2015
The result revealed a compound heterozygote with a 13-bp deletion in exon 1 (c.36_48del) and a two-base deletion in exon 2 (c.254_255del) in phosphatidylinositol glycan anchor, class L (PIGL) that caused frameshifts resulting in premature terminations.
A putative de-N-acetylase of the PIG-L superfamily affects fluoroquinolone tolerance in Pseudomonas aeruginosa.
Michiels et al., Leuven, Belgium. In Pathog Dis, 2014
A major cause of treatment failure of infections caused by Pseudomonas aeruginosa is the presence of antibiotic-insensitive persister cells.
PGAP2 mutations, affecting the GPI-anchor-synthesis pathway, cause hyperphosphatasia with mental retardation syndrome.
Horn et al., Berlin, Germany. In Am J Hum Genet, 2013
To date, mutations have been identified in six genes (PIGA, PIGL, PIGM, PIGN, PIGO, and PIGV) encoding proteins in the GPI-anchor-synthesis pathway in individuals with severe neurological features, including seizures, muscular hypotonia, and intellectual disability.
Hypomorphic mutations in PGAP2, encoding a GPI-anchor-remodeling protein, cause autosomal-recessive intellectual disability.
Abou Jamra et al., Copenhagen, Denmark. In Am J Hum Genet, 2013
Germline mutations in six genes (PIGA, PIGL, PIGM, PIGV, PIGN, and PIGO) in the ER-located part of the GPI-anchor-biosynthesis pathway have been reported, and all are associated with phenotypes extending from malformation and lethality to severe intellectual disability, epilepsy, minor dysmorphisms, and elevated alkaline phosphatase (ALP).
Catalysis by N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase (PIG-L) from Entamoeba histolytica: new roles for conserved residues.
Komath et al., New Delhi, India. In J Biol Chem, 2013
We showed previously that Entamoeba histolytica PIG-L exhibits a novel metal-independent albeit metal-stimulated activity.
[Study on gene differential expressions of substance and energy metabolism in chronic superficial gastritis patients of Pi deficiency syndrome and of pi-wei hygropyrexia syndrome].
Wang et al., Guangzhou, China. In Zhongguo Zhong Xi Yi Jie He Za Zhi, 2012
Of them, genes correlated to lipid metabolism included CRLS1, LRP11, FUT9, GPCPD1, PIGL, SULT1A4, B3GNT1, ST8SIA4, and ACADVL, mainly involved in the metabolic processes of fatty acid, cholesterol, phospholipids, and glycolipid.
Mutations in the glycosylphosphatidylinositol gene PIGL cause CHIME syndrome.
Freeze et al., Los Angeles, United States. In Am J Hum Genet, 2012
Whole-exome sequencing on five previously reported CHIME cases identified PIGL (N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase) as required for glycosylphosphatidylinositol anchor formation.
Mechanism for release of alkaline phosphatase caused by glycosylphosphatidylinositol deficiency in patients with hyperphosphatasia mental retardation syndrome.
Kinoshita et al., Ōsaka, Japan. In J Biol Chem, 2012
In contrast, ALP was degraded in PIGL-, DPM2-, or PIGX-deficient CHO cells, in which incomplete shorter GPIs that lacked mannose were accumulated.
N-acetyl-D-glucosaminylphosphatidylinositol de-N-acetylase from Entamoeba histolytica: metal alters catalytic rates but not substrate affinity.
Komath et al., New Delhi, India. In J Biol Chem, 2011
PIG-L/GPI12 proteins are endoplasmic reticulum-resident membrane proteins involved in the second step of glycosylphosphatidylinositol anchor biosynthesis in eukaryotes.
Babesia bovis contains an abundant parasite-specific protein-free glycerophosphatidylinositol and the genes predicted for its assembly.
Florin-Christensen et al., Argentina. In Vet Parasitol, 2010
The potential of B. bovis to assemble the presented free GPI species was verified by the existence of seven genes in its genome that putatively encode the following GPI biosynthetic enzymes: PI N-acetyl-GlcN-transferase (PIG-A and GPI-1), N-acetyl-GlcN-PI-de-N-acetylase (PIG-L), acyltransferase (PIG-W), dolichyl-phosphate mannosyl transferase (DPM-1), GPI mannosyltransferase I (PIG-M), and GPI mannosyltransferase II (PIG-V).
Silencing of genes required for glycosylphosphatidylinositol anchor biosynthesis in Burkitt lymphoma.
Brodsky et al., Baltimore, United States. In Exp Hematol, 2009
Quantitative polymerase chain reaction and microarray analysis demonstrate that the level of mRNA for PIGL and PIGY is lower in the FLAER(neg) Ramos cells and that mRNA levels of PIGY are reduced in the Akata and Daudi cells.
Reduction of cell surface glycosylphosphatidylinositol conjugates in Entamoeba histolytica by antisense blocking of E. histolytica GlcNAc-phosphatidylinositol deacetylase expression: effect on cell proliferation, endocytosis, and adhesion to target cells.
Bhattacharya et al., New Delhi, India. In Infect Immun, 2005
Of the genes identified, one of the early genes, GlcNAc-phosphatidylinositol deacetylase (PIG-L), was partially characterized.
The N-acetyl-D-glucosaminylphosphatidylinositol De-N-acetylase of glycosylphosphatidylinositol biosynthesis is a zinc metalloenzyme.
Ferguson et al., Dundee, United Kingdom. In J Biol Chem, 2005
N-acetyl-D-glucosaminylphosphatidylinositol De-N-acetylase of glycosylphosphatidylinositol biosynthesis is a zinc metalloenzyme
Subcellular localization and targeting of N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the second enzyme in the glycosylphosphatidylinositol biosynthetic pathway.
Menon et al., Madison, United States. In J Biol Chem, 2004
The second step in glycosylphosphatidylinositol biosynthesis is the de-N-acetylation of N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) catalyzed by N-acetylglucosaminylphosphatidylinositol deacetylase (PIG-L).
Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8.
Yokoyama et al., Yokohama, Japan. In Protein Sci, 2003
The TT1542 homologs in eukaryotes, PIG-L in mammals, and GPI12 in yeast and protozoa, have N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) de-N-acetylase activity.
share on facebooktweetadd +1mail to friends