Proteomics

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A novel structure of GPI anchored proteins NTNG2

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): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

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

SUBMITTER: Yoshiko Murakami  

LAB HEAD: Taroh Kinoshita

PROVIDER: PXD029851 | Pride | 2022-05-31

REPOSITORIES: Pride

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F077272.dat Other
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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]

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