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Determination of GPI structure of human CD59 in various KO CHO cells

ABSTRACT: To determine GPI structure of human CD59 in PGAP4-KO, PGAP3-KO, PGAP5-KO, and PGAP2-KO CHO cells.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Tetsuya Hirata

LAB HEAD: Taroh Kinoshita

PROVIDER: PXD008230 | Pride | 2018-01-30

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	150325_PGAP4.dat	Other
	150325_PGAP4.mgf	Mgf
	150325_PGAP4.mzid.pride.mztab.gz	Mztab
	150325_PGAP4.mzid.xml.gz	Mzid
	150325_PGAP4.pride.mgf.gz	Mgf

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Publications

Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain.

Hirata Tetsuya T Mishra Sushil K SK Nakamura Shota S Saito Kazunobu K Motooka Daisuke D Takada Yoko Y Kanzawa Noriyuki N Murakami Yoshiko Y Maeda Yusuke Y Fujita Morihisa M Yamaguchi Yoshiki Y Kinoshita Taroh T

Nature communications 20180126 1

Many eukaryotic proteins are anchored to the cell surface via the glycolipid glycosylphosphatidylinositol (GPI). Mammalian GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications, which are added via a yet unresolved process. Here we identify the Golgi-resident GPI-GalNAc transferase PGAP4 and show by mass spectrometry that PGAP4 knockout cells lose GPI-GalNAc structures. Furthermore, we demonstrate that PGAP4, in contrast to known Golgi glycosyltransferases, ...[more]

PMID: 29374258

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Determination of GPI structure of human CD59 in HEK293 cells

Project description:To determine GPI structure of human CD59 in wild-type,B3GALT4-KO, PIGZ-B3GALT4-DKO HEK293 cells.

2020-02-17 | PXD014226 | Pride

A novel structure of GPI anchored proteins

Project description:GPI anchors many proteins to the cell surface. GPI precursor has three mannoses, all of which are modified by ethanolamine-phosphate (EthN-P). It has been believed that EthN-P on the third mannose is always used as a bridge to the protein and EthN-P on the second mannose is removed after GPI is attached to the protein. Based on the finding that PIGB-knockout cells lacking the third mannose and PIGO-knockout cells lacking EthN-P linked to the third mannose expressed low levels of CD59 and DAF, GPI-APs and that those residual GPI-APs were lost by further knockout of PIGG. Using mass-spectrometry we determined that CD59 expressed on PIGB-knockout cells is attached to GPI via EthN-P linked to the second mannose. This linkage structure is also found in wild type cells. Our data modifies the current view of GPI anchors and provides mechanistic basis of inherited GPI deficiency caused by PIGG mutations.

2022-05-31 | PXD021996 | Pride

GPI-glycan structures of Prion from PGAP4-KO mouse brains

Project description:To determine glycosylphosphatidylinositol (GPI) structures of prion proteins isolated from PGAP4-KO mouse brains.

2022-04-04 | PXD029189 | Pride

A novel structure of GPI anchored proteins-NT5E

Project description:GPI anchors many proteins to the cell surface. GPI precursor has three mannoses, all of which are modified by ethanolamine-phosphate (EthN-P). It has been believed that EthN-P on the third mannose is always used as a bridge to the protein and EthN-P on the second mannose is removed after GPI is attached to the protein. In fact, several GPI-anchored proteins are not appreciably reduced on cells defective in PIGG, which transfers EthN-P to the second mannose. Nevertheless, mutations in PIGG cause neuronal abnormalities. Here, we show that EthN-P on the second mannose is used as a preferential bridge for several GPI-anchored proteins. Our data modifies the current view of GPI anchors and provides mechanistic basis of PIGG deficiencies.

2022-05-31 | PXD029850 | Pride

A novel structure of GPI anchored proteins NTNG2

Project description:GPI anchors many proteins to the cell surface. GPI precursor has three mannoses, all of which are modified by ethanolamine-phosphate (EthN-P). It has been believed that EthN-P on the third mannose is always used as a bridge to the protein and EthN-P on the second mannose is removed after GPI is attached to the protein. In fact, several GPI-anchored proteins are not appreciably reduced on cells defective in PIGG, which transfers EthN-P to the second mannose. Nevertheless, mutations in PIGG cause neuronal abnormalities. Here, we show that EthN-P on the second mannose is used as a preferential bridge for several GPI-anchored proteins. Our data modifies the current view of GPI anchors and provides mechanistic basis of PIGG deficiencies.

2022-05-31 | PXD029851 | Pride

GPI-glycan structures of human Prion from a human brain

Project description:To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins isolated from a human brain.

2020-04-22 | PXD017656 | Pride

GPI-glycan structures of human Prion (M232R) from knock-in mice_LC-MSMS

Project description:To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins with M232R mutation isolated from knock-in mice those express human prion protein instead of mouse one.

2023-03-08 | PXD037584 | Pride

GPI-glycan structures of human Prion from knock-in mice_LC-MSMS

Project description:To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins isolated from knock-in mice those express human prion protein instead of mouse one.

2020-04-22 | PXD017655 | Pride

GPI-glycan structures of Prion from WT mouse brains

Project description:To determine glycosylphosphatidylinositol (GPI) structures of prion proteins isolated from mouse brains.

2022-04-04 | PXD029190 | Pride

An Alternative Splicing Switch Regulates Embryonic Stem Cell Pluripotency and Reprogramming [protein binding microarray]

Project description:Alternative splicing (AS) is a key process underlying the expansion of proteomic diversity and the regulation of gene expression. However, the contribution of AS to the control of embryonic stem cell (ESC) pluripotency is not well understood. Here, we identify an evolutionarily conserved ESC-specific AS event that changes the DNA binding preference of the forkhead family transcription factor FOXP1. We show that the ESC-specific isoform of FOXP1 stimulates the expression of transcription factor genes required for pluripotency including OCT4, NANOG, NR5A2 and GDF3, while concomitantly repressing genes required for ESC differentiation. Remarkably, this isoform also promotes the maintenance of ESC pluripotency and the efficient reprogramming of somatic cells to induced pluripotent stem cells. These results reveal an AS switch that plays a pivotal role in the regulation of pluripotency through the control of critical ESC-specific transcriptional programs. Protein binding microarray (PBM) experiments were performed for two isoforms of the DNA binding domain of the human FOXP1 gene. Briefly, the PBMs involved binding GST-tagged DNA-binding proteins to two double-stranded 4*44K Agilent microarrays, each containing a different DeBruijn sequence design, in order to determine their sequence preferences. The method is described in Berger et al., Nature Biotechnology 2006.

2011-09-14 | E-GEOD-31007 | biostudies-arrayexpress

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