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Phosphatidylinositol glycan anchor biosynthesis, class K

GPI transamidase, GPI8, Gpi8p
This gene encodes a member of the cysteine protease family C13 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 a member of the multisubunit enzyme, GPI transamidase and is thought to be its enzymatic component. GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by catalyzing the transfer of fully assembled GPI units to proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: GAA1, V1a, CAN, ACID, PIG-U
Papers on GPI transamidase
A Surface Biotinylation Strategy for Reproducible Plasma Membrane Protein Purification and Tracking of Genetic and Drug-Induced Alterations.
Bennett et al., Vienna, Austria. In J Proteome Res, Feb 2016
Glycosylphosphatidylinositol (GPI)-anchored proteins were depleted in PM purifications from cells deficient in the GPI transamidase component PIGS, and treatment of cells with tunicamycin significantly reduced the abundance of N-glycoproteins in surface purifications.
Evolutionary engineering of a wine yeast strain revealed a key role of inositol and mannoprotein metabolism during low-temperature fermentation.
Guillamón et al., Paterna, Spain. In Bmc Genomics, 2014
GAA1 encodes a GPI transamidase complex subunit that adds GPI, which is required for inositol synthesis, to newly synthesized proteins, including mannoproteins.
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.
TBX2 represses CST6 resulting in uncontrolled legumain activity to sustain breast cancer proliferation: a novel cancer-selective target pathway with therapeutic opportunities.
Mullan et al., Belfast, United Kingdom. In Oncotarget, 2014
Knockdown of LGMN and the only other known AEP enzyme (GPI8) by siRNA confirmed that LGMN was the enzyme responsible for maintaining breast cancer proliferation.
Elevated levels of glycosylphosphatidylinositol (GPI) anchored proteins in plasma from human cancers detected by C. septicum alpha toxin.
Abbott et al., Athens, United States. In Cancer Biomark, 2014
Certain enzymes within the GPI biosynthetic pathway, particularly the subunits of the GPI transamidase, are elevated in various human cancers.
Biosynthesis and deficiencies of glycosylphosphatidylinositol.
Kinoshita, Ōsaka, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2013
GPI preassembled in the endoplasmic reticulum is attached to the protein's carboxyl-terminus as a post-translational modification by GPI transamidase.
GPI transamidase and GPI anchored proteins: oncogenes and biomarkers for cancer.
Hendrickson et al., Detroit, United States. In Crit Rev Biochem Mol Biol, 2013
This post-translational glycolipid modification is introduced into proteins via the action of the enzyme GPI transamidase (GPI-T).
Low-resolution structure of the soluble domain GPAA1 (yGPAA170-247) of the glycosylphosphatidylinositol transamidase subunit GPAA1 from Saccharomyces cerevisiae.
Grüber et al., Singapore, Singapore. In Biosci Rep, 2012
The Saccharomyces cerevisiae GPI transamidase complex consists of the subunits yPIG-K (Gpi8p), yPIG-S (Gpi17p), yPIG-T (Gpi16p), yPIG-U (CDC91/GAB1) and yGPAA1.
Defining the boundaries of species specificity for the Saccharomyces cerevisiae glycosylphosphatidylinositol transamidase using a quantitative in vivo assay.
Hendrickson et al., Baltimore, United States. In Biosci Rep, 2012
The attachment of the GPI anchor is mediated by GPI-T (GPI transamidase), a multimeric, membrane-bound enzyme located in the ER (endoplasmic reticulum).
Proteomic identification of glycosylphosphatidylinositol anchor-dependent membrane proteins elevated in breast carcinoma.
Abbott et al., Athens, United States. In J Biol Chem, 2012
The glycosylphosphatidylinositol (GPI) anchor is a lipid and glycan modification added to the C terminus of certain proteins in the endoplasmic reticulum by the activity of a multiple subunit enzyme complex known as the GPI transamidase (GPIT).
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
Secretion of ALP requires GPI transamidase, which in normal cells, cleaves the C-terminal GPI attachment signal peptide and replaces it with GPI.
Synthesis of truncated analogues for studying the process of glycosyl phosphatidylinositol modification.
Hendrickson et al., Detroit, United States. In Org Lett, 2010
The synthesis of truncated GPI anchor analogues is reported; these compounds were designed for use as soluble substrates for GPI transamidase (GPI-T), the enzyme that appends the GPI anchor onto proteins.
Characterization of GPIT-1 and GPIT-2, two auxiliary components of the Neurospora crassa GPI transamidase complex.
Free et al., Buffalo, United States. In Mycologia, 2009
The glycosylphosphatidylinositol (GPI) transamidase contains five known subunits and functions in the lumen of the ER to produce GPI-anchored proteins.
Truncation of the caspase-related subunit (Gpi8p) of Saccharomyces cerevisiae GPI transamidase: dimerization revealed.
Hendrickson et al., Baltimore, United States. In Arch Biochem Biophys, 2007
analysis of truncation of Gpi8p of Saccharomyces cerevisiae GPI transamidase
Recent developments in the molecular, biochemical and functional characterization of GPI8 and the GPI-anchoring mechanism [review].
Garg et al., Galveston, United States. In Mol Membr Biol, 2006
This final step in the transfer of the GPI to a protein is catalyzed by GPI8 of the putative transamidase complex (TAM).
Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge.
Kinoshita et al., Ōsaka, Japan. In J Biol Chem, 2003
GPI8 and PIG-T form a functionally important intermolecular disulfide bridge
Enzymes and auxiliary factors for GPI lipid anchor biosynthesis and post-translational transfer to proteins.
Eisenhaber et al., Vienna, Austria. In Bioessays, 2003
The lumenal part of PIG-T/GPI16 apparently consists of a beta-propeller with a central hole that regulates the access of substrate protein C termini to the active site of the cysteine protease PIG-K/GPI8 (gating mechanism) as well as of a polypeptide hook that embraces PIG-K/GPI8.
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