gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1

T-synthase, C1GALT1, beta 1,3-galactosyltransferase, PLT1
The protein encoded by this gene generates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for many extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice suggest that this gene plays a key role in thrombopoiesis and kidney homeostasis.[provided by RefSeq, Sep 2010] (from NCBI)
Top mentioned proteins: Cosmc, IgA, CAN, ACID, glycosyltransferase
Papers on T-synthase
The Arabidopsis thaliana elongator complex subunit 2 epigenetically affects root development.
New
Ding et al., Jinan, China. In J Exp Bot, Aug 2015
The key transcription factors responsible for maintaining root stem cell and QC identity, such as AP2 transcription factors PLT1 (PLETHORA1) and PLT2 (PLETHORA2), GRAS transcription factors such as SCR (SCARECROW) and SHR (SHORT ROOT) and WUSCHEL-RELATED HOMEOBOX5 transcription factor WOX5, were all strongly down-regulated in the mutant.
Promoters of Human Cosmc and T-synthase Genes Are Similar in Structure, Yet Different in Epigenetic Regulation.
New
Ju et al., Amsterdam, Netherlands. In J Biol Chem, Aug 2015
The T-synthase (core 1 β3-galactosyltransferase) and its molecular chaperone Cosmc regulate the biosynthesis of mucin type O-glycans on glycoproteins, and evidence suggests that both T-synthase and Cosmc are transcriptionally suppressed in several human diseases, although the transcriptional regulation of these two genes is not understood.
The Arabidopsis SWI2/SNF2 Chromatin Remodeling ATPase BRAHMA Targets Directly to PINs and Is Required for Root Stem Cell Niche Maintenance.
New
Wu et al., Taipei, Taiwan. In Plant Cell, Jun 2015
Mutations of BRM affected auxin distribution by reducing local expression of several PIN-FORMED (PIN) genes in the stem cells and impaired the expression of the stem cell transcription factor genes PLETHORA (PLT1) and PLT2.
Relationship between rs1047763 polymorphism of the C1GALT1 gene and susceptibility to immunoglobulin A nephropathy in Xinjiang Uyghur people.
Lu et al., Tengzhou, China. In Genet Mol Res, 2014
We explored the relationship between rs1047763, a single-nucleotide polymorphism (SNP) of the C1GALT1 gene, and genetic susceptibility to immunoglobulin A nephropathy (IgAN) in Xinjiang Uyghur people.
Association between C1GALT1 variants and genetic susceptibility to IgA nephropathy in Uygur.
Lu et al., China. In Genet Mol Res, 2014
Analyses of serum IgA1 from IgAN patients revealed abnormal galactosylation of the O-linked carbohydrate moieties of IgA that may result from altered activity in the core of 1 b1,3-galactosyltransferase (C1GalT1).
Aberrant Cosmc genes result in Tn antigen expression in human colorectal carcinoma cell line HT-29.
Hu et al., Yantai, China. In Int J Clin Exp Pathol, 2014
Cosmc resides in X24 encoded by a single gene and functions as a specific molecular chaperone for T-synthase.
The Cosmc connection to the Tn antigen in cancer.
Review
Cummings et al., Atlanta, United States. In Cancer Biomark, 2014
This precursor is generated in the Golgi apparatus on newly synthesized glycoproteins by a family of polypeptide α-N-acetylgalactosaminyltransferases (ppGalNAcTs) and then extended to the common core 1 O-glycan Galβ1-3GalNAcα1-O-Ser/Thr (T antigen) by a single enzyme termed the T-synthase (core 1 β3-galactosyltransferase or C1GalT).
Tn and sialyl-Tn antigens, aberrant O-glycomics as human disease markers.
Review
Cummings et al., Atlanta, United States. In Proteomics Clin Appl, 2013
The major pathological mechanism for expression of the Tn and STn antigens is compromised T-synthase activity, resulting from alteration of the X-linked gene that encodes for Cosmc, a molecular chaperone specifically required for the correct folding of T-synthase to form active enzyme.
Search for genetic association between IgA nephropathy and candidate genes selected by function or by gene mapping at loci IGAN2 and IGAN3.
GeneRIF
European IgA Nephropathy Consortium et al., Torino, Italy. In Nephrol Dial Transplant, 2012
C1GALT1 polymorphisms influence the risk to develop IgA nephropathy and proteinuria.
Tight complex formation between Cosmc chaperone and its specific client non-native T-synthase leads to enzyme activity and client-driven dissociation.
GeneRIF
Cummings et al., Atlanta, United States. In J Biol Chem, 2012
Results show that soluble Cosmc directly interacts in a specific manner with denatured, but not native, T-synthase to form a noncovalent and reversible complex that results in the acquisition of T-synthase catalytic activity.
Targeted disruption of core 1 β1,3-galactosyltransferase (C1galt1) induces apical endocytic trafficking in human corneal keratinocytes.
GeneRIF
Argüeso et al., Madrid, Spain. In Plos One, 2011
using RNA interfering system targeting the core 1 ss1,3-galactosyltransferase to explore the role of mucin-type carbohydrates in apical endocytic trafficking in human corneal keratinocytes
Co-translational function of Cosmc, core 1 synthase specific molecular chaperone, revealed by a cell-free translation system.
GeneRIF
Narimatsu et al., Tsukuba, Japan. In Febs Lett, 2011
Results indicate that Cosmc mediates the co-translational activation of C1GalT and that it may prevent the unfavorable aggregation of C1GalT.
The Tn antigen-structural simplicity and biological complexity.
Review
Cummings et al., Atlanta, United States. In Angew Chem Int Ed Engl, 2011
The Tn antigen is normally modified by a specific galactosyltransferase (T-synthase) in the Golgi apparatus of cells.
Control of Arabidopsis apical-basal embryo polarity by antagonistic transcription factors.
Impact
Long et al., San Diego, United States. In Nature, 2010
Here we show that the PLT1 and PLT2 genes are direct targets of the transcriptional co-repressor TOPLESS (TPL) and that PLT1/2 are necessary for the homeotic conversion of shoots to roots in tpl-1 mutants.
The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase.
GeneRIF
Cummings et al., Atlanta, United States. In J Biol Chem, 2010
The chaperone activity of Cosmc is specific, does not require ATP in vitro, and is effective toward T-synthase but not another beta-galactosyltransferase
Pathogenetic significance of aberrant glycosylation of IgA1 in IgA nephropathy.
Review
Gejyo et al., Niigata, Japan. In Clin Exp Nephrol, 2008
Although genes encoding enzymes involved in the O-glycosylation process, such as C1GALT1, have been reported to be responsible for susceptibility to IgAN, recent evidence suggests that the abnormality is restricted to a small fraction of B cell populations and arises from dysregulated IgA1 production and secretion in mucosal immune system.
Protein glycosylation: chaperone mutation in Tn syndrome.
Impact
GeneRIF
Cummings et al., Oklahoma City, United States. In Nature, 2005
Tn syndrome is associated with a somatic mutation in Cosmc, a gene on the X chromosome that encodes a molecular 'chaperone' that is required for the proper folding and hence full activity of T-synthase
The PLETHORA genes mediate patterning of the Arabidopsis root stem cell niche.
Impact
Scheres et al., Utrecht, Netherlands. In Cell, 2004
Here, we identify the PLETHORA1 (PLT1) and PLT2 genes encoding AP2 class putative transcription factors, which are essential for QC specification and stem cell activity.
Bt toxin resistance from loss of a putative carbohydrate-modifying enzyme.
Impact
Aroian et al., San Diego, United States. In Science, 2001
Here we report the cloning of a Bt toxin resistance gene, Caenorhabditis elegans bre-5, which encodes a putative beta-1,3-galactosyltransferase.
Pathogenesis of IgA nephropathy.
Review
Allen et al., Leicester, United Kingdom. In Ann Med Interne (paris), 1999
This reduced galactosylation may be due to a functional defect in plasma cell beta 1,3-galactosyltransferase. Altered hinge region glycosylation may alter IgA1 structure, modifying interactions with matrix proteins, IgA receptors and complement, and therefore influence mesangial deposition and subsequent injury through mechanisms other than classical antigen-antibody reactions.
share on facebooktweetadd +1mail to friends