Cross-talks of glycosylphosphatidylinositol biosynthesis with glycosphingolipid biosynthesis and ER-associated degradation

Yicheng Wang, Yusuke Maeda, Yi-Shi Liu, Yoko Takada, Akinori Ninomiya, Tetsuya Hirata, Morihisa Fujita, Yoshiko Murakami and Taroh Kinoshita ()
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Yicheng Wang: Osaka University
Yusuke Maeda: Osaka University
Yi-Shi Liu: Jiangnan University
Yoko Takada: Osaka University
Akinori Ninomiya: Osaka University
Tetsuya Hirata: Osaka University
Morihisa Fujita: Jiangnan University
Yoshiko Murakami: Osaka University
Taroh Kinoshita: Osaka University

Nature Communications, 2020, vol. 11, issue 1, 1-18

Abstract: Abstract Glycosylphosphatidylinositol (GPI)-anchored proteins and glycosphingolipids interact with each other in the mammalian plasma membranes, forming dynamic microdomains. How their interaction starts in the cells has been unclear. Here, based on a genome-wide CRISPR-Cas9 genetic screen for genes required for GPI side-chain modification by galactose in the Golgi apparatus, we report that β1,3-galactosyltransferase 4 (B3GALT4), the previously characterized GM1 ganglioside synthase, additionally functions in transferring galactose to the N-acetylgalactosamine side-chain of GPI. Furthermore, B3GALT4 requires lactosylceramide for the efficient GPI side-chain galactosylation. Thus, our work demonstrates previously unexpected functional relationships between GPI-anchored proteins and glycosphingolipids in the Golgi. Through the same screening, we also show that GPI biosynthesis in the endoplasmic reticulum (ER) is severely suppressed by ER-associated degradation to prevent GPI accumulation when the transfer of synthesized GPI to proteins is defective. Our data demonstrates cross-talks of GPI biosynthesis with glycosphingolipid biosynthesis and the ER quality control system.

Date: 2020
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DOI: 10.1038/s41467-020-14678-2

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