Human SND2 mediates ER targeting of GPI-anchored proteins with low hydrophobic GPI attachment signals

FEBS Letters

article

Jing Yang¹  Tetsuya Hirata²  Yi-Shi Liu¹  Xin-Yu Guo¹  Xiao-Dong Gao¹  Taroh Kinoshita⁴  Morihisa Fujita¹ 

[1] Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University;Institute for Glyco-core Research ,(iGCORE), Gifu University;Center for Highly Advanced Integration of Nano and Life Sciences ,(G-CHAIN), Gifu University;Research Institute for Microbial Diseases, Osaka University;WPI Immunology Frontier Research Center, Osaka University

关键词: endoplasmic reticulum;    glycosylphosphatidylinositol;    protein targeting;    signal recognition particle;    SND2;   

DOI  :  10.1002/1873-3468.14083

来源: John Wiley & Sons Ltd.

【 摘 要 】

Over 100 glycosylphosphatidylinositol-anchored proteins (GPI-APs) are encoded in the mammalian genome. It is not well understood how these proteins are targeted and translocated to the endoplasmic reticulum (ER). Here, we reveal that many GPI-APs, such as CD59, CD55, and CD109, utilize human SND2 (hSND2)-dependent ER targeting machinery. We also found that signal recognition particle receptors seem to cooperate with hSND2 to target GPI-APs to the ER. Both the N-terminal signal sequence and C-terminal GPI attachment signal of GPI-APs contribute to ER targeting via the hSND2-dependent pathway. Particularly, the hydrophobicity of the C-terminal GPI attachment signal acts as the determinant of hSND2 dependency. Our results explain the route and mechanism of the ER targeting of GPI-APs in mammalian cells.

【 授权许可】

Unknown