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A novel structure of GPI anchored proteins

ABSTRACT: 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.

INSTRUMENT(S): Bruker software

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Epithelial Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: Yoshiko Murakami

LAB HEAD: Taroh Kinoshita

PROVIDER: PXD022032 | Pride | 2022-05-31

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	F070152.dat	Other
	F070152.mgf	Mgf
	F070152.mzid.gz	Mzid
	F070153.dat	Other
	F070153.mgf	Mgf

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1 - 5 of 16

Publications

Ethanolamine-phosphate on the second mannose is a preferential bridge for some GPI-anchored proteins.

Ishida Mizuki M Maki Yuta Y Ninomiya Akinori A Takada Yoko Y Campeau Philippe P Kinoshita Taroh T Murakami Yoshiko Y

EMBO reports 20220523 7

Glycosylphosphatidylinositols (GPIs) are glycolipids that anchor many proteins (GPI-APs) on the cell surface. The core glycan of GPI precursor has three mannoses, which in mammals, are all modified by ethanolamine-phosphate (EthN-P). It is postulated that EthN-P on the third mannose (EthN-P-Man3) is the bridge between GPI and the protein and the second (EthN-P-Man2) is removed after GPI-protein attachment. However, EthN-P-Man2 may not be always transient, as mutations of PIGG, the enzyme that tr ...[more]

PMID: 35603428

Similar Datasets

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

2022-05-31 | PXD029851 | 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

Homo sapiens

Project description:GPI-anchored Timp1 protein

| PRJNA173439 | ENA

Zinc supply mediated by ZNT5-ZNT6 and ZNT7 is critical to glycosylphosphatidylinositol-anchored protein expression

Project description:Glycosylphosphatidylinositol (GPI)-anchored proteins play crucial roles in various enzyme activities, cell signaling and adhesion, and immune responses. ZNT type zinc transporter proteins mobilize cytosolic zinc to the extracellular space and intracellular compartments. Here, we report that the early secretory pathway ZNTs [ZNT5-ZNT6 heterodimers (ZNT5-6) and ZNT7 homodimers (ZNT7)], which supply zinc into the lumen of organelles, are essential for GPI-anchored protein expression on the cell surface. Loss of ZNT5-6 and ZNT7 zinc transport functions results in a significant reduction of GPI-anchored proteins similar to that of mutant cells lacking phosphatidylinositol glycan anchor biosynthesis (PIG) genes. Disrupted ZNT5 and ZNT7 genes in medaka fish show touch-insensitive phenotypes similar to those of zebrafish PIG mutants. These findings provide a previously unappreciated insight into the regulation of GPI-anchored protein expression and of protein quality control in the early secretory pathway.

2022-05-04 | PXD032172 | Pride

Comparative haploid genetic screens reveal divergent pathways in the biogenesis and trafficking of glycophosphatidylinositol (GPI)-anchored proteins

Project description:Comparative haploid genetic screens to annotate common and specialized genes required for the biogenesis of individual GPI anchored proteins. SEC62 and SEC63 were required for proper PrP targeting, and were dispensable for CD59. CD59 however, required a GPI side chain modification for maturation, in addition to the aspartyl intramembrane cleaving protease: SPPL3.

2015-05-13 | GSE68796 | GEO

Transcriptional analyses of neuron and glia specific knockdown of PIG-A in Drosophila melanogaster

Project description:We performed neuron and glia specific knockdown of PIG-A in Drosophila to understand the molecular defects that occur with loss of GPI anchored proteins. PIG-A encodes an enzyme responsible for the first step in GPI anchor biosynthesis. Loss of PIG-A in neurons and glia results in different neurological defects.

2023-10-31 | GSE241512 | GEO

Expression data of human fetal liver hematopoietic stem and progenitors cells [Set 2]

Project description:Advances in pluripotent stem cell and reprogramming technologies have given hope of generating hematopoietic stem cells (HSC) in culture. To succeed, greater understanding of the self-renewing HSC during human development is required. We discovered that glycophosphatidylinositol-anchored surface protein GPI-80 (Vanin 2) defines a distinct subpopulation of human fetal hematopoietic stem/progenitor cells (HSPC) with self-renewal ability. CD34+CD90+CD38-GPI-80+ HSPC were the sole population that maintained proliferative potential and undifferentiated state in bone marrow stroma co-culture, and engrafted in immunodeficient mice. GPI-80 expression also enabled tracking of HSC migration between human fetal hematopoietic niches. The most highly enriched surface protein in GPI-80+ HSPC as compared to their progeny was Integrin alpha-M (ITGAM), which in leukocytes cooperates with GPI-80 to support migration. Knockdown of either GPI-80 or ITGAM was sufficient to perturb undifferentiated HSPC in stroma co-culture. These findings indicate that human fetal HSC utilize common mechanisms with leukocytes for cell-cell interactions governing HSC self-renewal. We used microarrays to identify genes enriched in the GPI-80+ hematopoietic stem and progenitor population in fetal liver. RNA was extracted from enriched fetal liver hematopoietic stem and progenitor cells, and downstream progenitors, for comparison based on Affymetrix arrays.

2015-01-23 | E-GEOD-54315 | biostudies-arrayexpress

Identification of Glycosylphosphatidylinositol Anchored Proteins and ω-sites Using TiO2-Based Affinity Purification

Project description:Glycosylphosphatidylinositol anchored proteins (GPI-APs) in the outer leaflet of the membrane microdomains, commonly referred to as lipid rafts, play important roles in many biological processes. To enable large-scale site-specific analysis of GPI anchoring, we developed a method for identification of ω-sites by mass spectrometry by combining titanium dioxide-based affinity purification and hydrogen fluoride treatment. This method was able to identify ~3-fold more GPI-APs than our previous method: the new technique identified a total of 73 ω-sites derived from 49 GPI-APs. In 13 of the 49 GPI-APs identified, the GPI-anchor attached to multiple amino acids in the C-terminal site, yielding a variety of different protein species. This method allows us to simultaneously identify many GPI-AP protein species with different ω-sites.

2016-05-27 | PXD003105 | Pride

Expression data of human fetal liver hematopoietic stem and progenitors cells [Set 1]

Project description:Advances in pluripotent stem cell and reprogramming technologies have given hope of generating hematopoietic stem cells (HSC) in culture. To succeed, greater understanding of the self-renewing HSC during human development is required. We discovered that glycophosphatidylinositol-anchored surface protein GPI-80 (Vanin 2) defines a distinct subpopulation of human fetal hematopoietic stem/progenitor cells (HSPC) with self-renewal ability. CD34+CD90+CD38-GPI-80+ HSPC were the sole population that maintained proliferative potential and undifferentiated state in bone marrow stroma co-culture, and engrafted in immunodeficient mice. GPI-80 expression also enabled tracking of HSC migration between human fetal hematopoietic niches. The most highly enriched surface protein in GPI-80+ HSPC as compared to their progeny was Integrin alpha-M (ITGAM), which in leukocytes cooperates with GPI-80 to support migration. Knockdown of either GPI-80 or ITGAM was sufficient to perturb undifferentiated HSPC in stroma co-culture. These findings indicate that human fetal HSC utilize common mechanisms with leukocytes for cell-cell interactions governing HSC self-renewal. We used microarrays to identify genes enriched in the CD90+ hematopoietic stem and progenitor population in fetal liver. RNA was extracted from enriched fetal liver hematopoietic stem and progenitor cells, and downstream progenitors, for comparison based on Affymetrix arrays.

2015-01-23 | E-GEOD-54314 | biostudies-arrayexpress

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