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

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...

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Published inEMBO reports Vol. 23; no. 7; pp. e54352 - n/a
Main Authors Ishida, Mizuki, Maki, Yuta, Ninomiya, Akinori, Takada, Yoko, Campeau, Philippe, Kinoshita, Taroh, Murakami, Yoshiko
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 05.07.2022
Springer Nature B.V
John Wiley and Sons Inc
Subjects
Animals
Attachment
CD59 antigen
CD73
Cell surface
EMBO20
EMBO24
Ethanolamine
Ethanolamines - metabolism
Glycan
Glycolipids
Glycosylphosphatidylinositol
Glycosylphosphatidylinositols - genetics
Glycosylphosphatidylinositols - metabolism
GPI-Linked Proteins - genetics
inherited GPI deficiency
Localization
Mammals - metabolism
Mannose
Mannose - metabolism
mass spectrometry
Mutation
Nucleotidase
Phosphates
PIGB
PIGG
Proteins
PIGB
mass spectrometry
CD73
inherited GPI deficiency
PIGG
Online AccessGet full text

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Abstract 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 transfers EthN‐P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN‐P on Man2 is the preferential bridge in some GPI‐APs, among them, the Ect‐5’‐nucleotidase and Netrin G2. We find that CD59, a GPI‐AP, is attached via EthN‐P‐Man2 both in PIGB ‐knockout cells, in which GPI lacks Man3, and with a small fraction in wild‐type cells. Our findings modify the current view of GPI anchoring and provide a mechanistic basis for IGDs caused by PIGG mutations. Synopsis This study challenges the dogma that GPI‐anchored proteins are always attached to the third mannose in GPI via an ethanolamine‐phosphate (EthN‐P) bridge by providing evidence for an alternative attachment to the second mannose via EthN‐P. Some proteins preferentially use the alternative mode of attachment to GPI, highlighting the importance of the EthN‐P transferred to the second mannose by PIGG. In cells that lack either the third mannose in GPI (PIGB‐KO) or the EthN‐P linked to the third mannose (PIGO‐KO), the GPI‐anchored proteins CD59 and DAF are attached to EthN‐P linked to the second mannose, allowing their membrane localization at low levels. Approximately 10% of CD59 on wild‐type HEK293 cells are similarly attached to the second mannose via EthN‐P. NT5E and NetrinG2, in contrast to CD59, are preferentially attached to the EthN‐P linked to the second mannose. Graphical Abstract This study challenges the dogma that GPI‐anchored proteins are always attached to the third mannose in GPI via an ethanolamine‐phosphate (EthN‐P) bridge by providing evidence for an alternative attachment to the second mannose via EthN‐P. Some proteins preferentially use the alternative mode of attachment to GPI, highlighting the importance of the EthN‐P transferred to the second mannose by PIGG.
AbstractList 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 transfers EthN-P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN-P on Man2 is the preferential bridge in some GPI-APs, among them, the Ect-5'-nucleotidase and Netrin G2. We find that CD59, a GPI-AP, is attached via EthN-P-Man2 both in PIGB-knockout cells, in which GPI lacks Man3, and with a small fraction in wild-type cells. Our findings modify the current view of GPI anchoring and provide a mechanistic basis for IGDs caused by PIGG mutations.
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 transfers EthN‐P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN‐P on Man2 is the preferential bridge in some GPI‐APs, among them, the Ect‐5’‐nucleotidase and Netrin G2. We find that CD59, a GPI‐AP, is attached via EthN‐P‐Man2 both in PIGB ‐knockout cells, in which GPI lacks Man3, and with a small fraction in wild‐type cells. Our findings modify the current view of GPI anchoring and provide a mechanistic basis for IGDs caused by PIGG mutations. image This study challenges the dogma that GPI‐anchored proteins are always attached to the third mannose in GPI via an ethanolamine‐phosphate (EthN‐P) bridge by providing evidence for an alternative attachment to the second mannose via EthN‐P. Some proteins preferentially use the alternative mode of attachment to GPI, highlighting the importance of the EthN‐P transferred to the second mannose by PIGG. In cells that lack either the third mannose in GPI (PIGB‐KO) or the EthN‐P linked to the third mannose (PIGO‐KO), the GPI‐anchored proteins CD59 and DAF are attached to EthN‐P linked to the second mannose, allowing their membrane localization at low levels. Approximately 10% of CD59 on wild‐type HEK293 cells are similarly attached to the second mannose via EthN‐P. NT5E and NetrinG2, in contrast to CD59, are preferentially attached to the EthN‐P linked to the second mannose.
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 transfers EthN‐P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN‐P on Man2 is the preferential bridge in some GPI‐APs, among them, the Ect‐5’‐nucleotidase and Netrin G2. We find that CD59, a GPI‐AP, is attached via EthN‐P‐Man2 both in PIGB ‐knockout cells, in which GPI lacks Man3, and with a small fraction in wild‐type cells. Our findings modify the current view of GPI anchoring and provide a mechanistic basis for IGDs caused by PIGG mutations. This study challenges the dogma that GPI‐anchored proteins are always attached to the third mannose in GPI via an ethanolamine‐phosphate (EthN‐P) bridge by providing evidence for an alternative attachment to the second mannose via EthN‐P. Some proteins preferentially use the alternative mode of attachment to GPI, highlighting the importance of the EthN‐P transferred to the second mannose by PIGG.
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 transfers EthN-P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN-P on Man2 is the preferential bridge in some GPI-APs, among them, the Ect-5'-nucleotidase and Netrin G2. We find that CD59, a GPI-AP, is attached via EthN-P-Man2 both in PIGB-knockout cells, in which GPI lacks Man3, and with a small fraction in wild-type cells. Our findings modify the current view of GPI anchoring and provide a mechanistic basis for IGDs caused by PIGG mutations.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 transfers EthN-P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN-P on Man2 is the preferential bridge in some GPI-APs, among them, the Ect-5'-nucleotidase and Netrin G2. We find that CD59, a GPI-AP, is attached via EthN-P-Man2 both in PIGB-knockout cells, in which GPI lacks Man3, and with a small fraction in wild-type cells. Our findings modify the current view of GPI anchoring and provide a mechanistic basis for IGDs caused by PIGG mutations.
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 transfers EthN‐P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN‐P on Man2 is the preferential bridge in some GPI‐APs, among them, the Ect‐5’‐nucleotidase and Netrin G2. We find that CD59, a GPI‐AP, is attached via EthN‐P‐Man2 both in PIGB‐knockout cells, in which GPI lacks Man3, and with a small fraction in wild‐type cells. Our findings modify the current view of GPI anchoring and provide a mechanistic basis for IGDs caused by PIGG mutations. Synopsis This study challenges the dogma that GPI‐anchored proteins are always attached to the third mannose in GPI via an ethanolamine‐phosphate (EthN‐P) bridge by providing evidence for an alternative attachment to the second mannose via EthN‐P. Some proteins preferentially use the alternative mode of attachment to GPI, highlighting the importance of the EthN‐P transferred to the second mannose by PIGG. In cells that lack either the third mannose in GPI (PIGB‐KO) or the EthN‐P linked to the third mannose (PIGO‐KO), the GPI‐anchored proteins CD59 and DAF are attached to EthN‐P linked to the second mannose, allowing their membrane localization at low levels. Approximately 10% of CD59 on wild‐type HEK293 cells are similarly attached to the second mannose via EthN‐P. NT5E and NetrinG2, in contrast to CD59, are preferentially attached to the EthN‐P linked to the second mannose. This study challenges the dogma that GPI‐anchored proteins are always attached to the third mannose in GPI via an ethanolamine‐phosphate (EthN‐P) bridge by providing evidence for an alternative attachment to the second mannose via EthN‐P. Some proteins preferentially use the alternative mode of attachment to GPI, highlighting the importance of the EthN‐P transferred to the second mannose by PIGG.
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 transfers EthN‐P to Man2, result in inherited GPI deficiencies (IGDs), characterized by neuronal dysfunctions. Here, we show that EthN‐P on Man2 is the preferential bridge in some GPI‐APs, among them, the Ect‐5’‐nucleotidase and Netrin G2. We find that CD59, a GPI‐AP, is attached via EthN‐P‐Man2 both in PIGB ‐knockout cells, in which GPI lacks Man3, and with a small fraction in wild‐type cells. Our findings modify the current view of GPI anchoring and provide a mechanistic basis for IGDs caused by PIGG mutations. Synopsis This study challenges the dogma that GPI‐anchored proteins are always attached to the third mannose in GPI via an ethanolamine‐phosphate (EthN‐P) bridge by providing evidence for an alternative attachment to the second mannose via EthN‐P. Some proteins preferentially use the alternative mode of attachment to GPI, highlighting the importance of the EthN‐P transferred to the second mannose by PIGG. In cells that lack either the third mannose in GPI (PIGB‐KO) or the EthN‐P linked to the third mannose (PIGO‐KO), the GPI‐anchored proteins CD59 and DAF are attached to EthN‐P linked to the second mannose, allowing their membrane localization at low levels. Approximately 10% of CD59 on wild‐type HEK293 cells are similarly attached to the second mannose via EthN‐P. NT5E and NetrinG2, in contrast to CD59, are preferentially attached to the EthN‐P linked to the second mannose. Graphical Abstract This study challenges the dogma that GPI‐anchored proteins are always attached to the third mannose in GPI via an ethanolamine‐phosphate (EthN‐P) bridge by providing evidence for an alternative attachment to the second mannose via EthN‐P. Some proteins preferentially use the alternative mode of attachment to GPI, highlighting the importance of the EthN‐P transferred to the second mannose by PIGG.
Author Ishida, Mizuki
Kinoshita, Taroh
Murakami, Yoshiko
Takada, Yoko
Ninomiya, Akinori
Campeau, Philippe
Maki, Yuta
AuthorAffiliation 1 Yabumoto Department of Intractable Disease Research Research Institute for Microbial Diseases Osaka University Suita Japan
3 Project Research Center for Fundamental Sciences Graduate School of Science Osaka University Toyonaka Japan
7 Center for Infectious Disease Education and Research Osaka University Suita Japan
6 Department of Pediatrics CHU Sainte‐Justine and University of Montreal Montreal QC Canada
2 Department of Chemistry Osaka University Toyonaka Japan
4 Central Instrumentation Laboratory Research Institute for Microbial Diseases Osaka University Suita Japan
5 WPI Immunology Frontier Research Center Osaka University Suita Japan
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– name: 2 Department of Chemistry Osaka University Toyonaka Japan
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Issue 7
Keywords PIGB
mass spectrometry
CD73
inherited GPI deficiency
PIGG
Language English
License 2022 The Authors.
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Snippet Glycosylphosphatidylinositols (GPIs) are glycolipids that anchor many proteins (GPI‐APs) on the cell surface. The core glycan of GPI precursor has three...
Glycosylphosphatidylinositols (GPIs) are glycolipids that anchor many proteins (GPI-APs) on the cell surface. The core glycan of GPI precursor has three...
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StartPage e54352
SubjectTerms Animals
Attachment
CD59 antigen
CD73
Cell surface
EMBO20
EMBO24
Ethanolamine
Ethanolamines - metabolism
Glycan
Glycolipids
Glycosylphosphatidylinositol
Glycosylphosphatidylinositols - genetics
Glycosylphosphatidylinositols - metabolism
GPI-Linked Proteins - genetics
inherited GPI deficiency
Localization
Mammals - metabolism
Mannose
Mannose - metabolism
mass spectrometry
Mutation
Nucleotidase
Phosphates
PIGB
PIGG
Proteins
Title Ethanolamine‐phosphate on the second mannose is a preferential bridge for some GPI‐anchored proteins
URI https://link.springer.com/article/10.15252/embr.202154352
https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fembr.202154352
https://www.ncbi.nlm.nih.gov/pubmed/35603428
https://www.proquest.com/docview/2684380445
https://www.proquest.com/docview/2668218056
https://pubmed.ncbi.nlm.nih.gov/PMC9253782
Volume 23
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