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Phosphatidylinositol glycan anchor biosynthesis, class T

phosphatidylinositol glycan class T, PIGT
This gene encodes a protein that is involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. This protein is an essential component of the multisubunit enzyme, GPI transamidase. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2010] (from NCBI)
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Top mentioned proteins: HAD, GAA1, ASXL1, E2F1, CAN
Papers on phosphatidylinositol glycan class T
Expanding the clinical and molecular characteristics of PIGT-CDG, a disorder of glycosylphosphatidylinositol anchors.
New
Wolfe et al., Bethesda, United States. In Mol Genet Metab, Jun 2015
PIGT-CDG, an autosomal recessive syndromic intellectual disability disorder of glycosylphosphatidylinositol (GPI) anchors, was recently described in two independent kindreds [Multiple Congenital Anomalies-Hypotonia-Seizures Syndrome 3 (OMIM, #615398)].
Novel compound heterozygous PIGT mutations caused multiple congenital anomalies-hypotonia-seizures syndrome 3.
Matsumoto et al., Yokohama, Japan. In Neurogenetics, 2014
Arg488Trp), in PIGT encoding a subunit of the GPI transamidase complex.
A case of paroxysmal nocturnal hemoglobinuria caused by a germline mutation and a somatic mutation in PIGT.
Schrezenmeier et al., Berlin, Germany. In Blood, 2013
We identified a heterozygous germline splice site mutation in PIGT and a somatic 8-MB deletion in granulocytes affecting the other copy of PIGT.
A novel intellectual disability syndrome caused by GPI anchor deficiency due to homozygous mutations in PIGT.
Nordgren et al., Stockholm, Sweden. In J Med Genet, 2013
RESULTS: The results from WES identified a homozygous mutation, c.547A>C (p.Thr183Pro), in PIGT; Sanger sequencing of additional family members confirmed segregation with the disease.
Proteomic identification of glycosylphosphatidylinositol anchor-dependent membrane proteins elevated in breast carcinoma.
Abbott et al., Athens, United States. In J Biol Chem, 2012
We also expressed short interfering RNAs targeting the expression of the GPAA1 and PIGT subunits of GPIT in breast cancer cell lines to identify proteins in which membrane localization is dependent on GPI anchor addition.
Identification of copy number gain and overexpressed genes on chromosome arm 20q by an integrative genomic approach in cervical cancer: potential role in progression.
Murty et al., New York City, United States. In Genes Chromosomes Cancer, 2008
These include a number of functionally important genes in cell cycle regulation (E2F1, TPX2, KIF3B, PIGT, and B4GALT5), nuclear function (CSEL1), viral replication (PSMA7 and LAMA5), methylation and chromatin remodeling (ASXL1, AHCY, and C20orf20), and transcription regulation (TCEA2).
Overexpression of glycosylphosphatidylinositol (GPI) transamidase subunits phosphatidylinositol glycan class T and/or GPI anchor attachment 1 induces tumorigenesis and contributes to invasion in human breast cancer.
Trink et al., Baltimore, United States. In Cancer Res, 2006
Based on the oncogenic role of phosphatidylinositol glycan (PIG) class U in human tumors, we explored the role of two additional subunits of the glycosylphosphatidylinositol (GPI) transamidase complex in human breast cancer.
Endoplasmic reticulum localization of Gaa1 and PIG-T, subunits of the glycosylphosphatidylinositol transamidase complex.
GeneRIF
Menon et al., Madison, United States. In J Biol Chem, 2005
ER-localized because of information in its transmembrane span
Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge.
GeneRIF
Kinoshita et al., Ōsaka, Japan. In J Biol Chem, 2003
GPI8 and PIG-T form a functionally important intermolecular disulfide bridge
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