Human SND2 mediates ER targeting of GPI‐anchored proteins with low hydrophobic GPI attachment signals
Autor: | Tetsuya Hirata, Yi-Shi Liu, Xiao-Dong Gao, Xin-Yu Guo, Morihisa Fujita, Taroh Kinoshita, Jing Yang |
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Rok vydání: | 2021 |
Předmět: |
Signal peptide
Glycosylphosphatidylinositols Biophysics Gene Expression CD59 Antigens CD59 Protein Sorting Signals Endoplasmic Reticulum GPI-Linked Proteins medicine.disease_cause Biochemistry 03 medical and health sciences Protein Domains Antigens CD Structural Biology Protein targeting Genetics medicine Humans Receptor Molecular Biology 030304 developmental biology 0303 health sciences Signal recognition particle Er targeting CD55 Antigens Chemistry Arsenite Transporting ATPases Endoplasmic reticulum 030302 biochemistry & molecular biology Membrane Proteins Cell Biology Gpi anchored protein Neoplasm Proteins Cell biology carbohydrates (lipids) Protein Transport HEK293 Cells lipids (amino acids peptides and proteins) Hydrophobic and Hydrophilic Interactions SEC Translocation Channels Protein Binding |
Zdroj: | FEBS Letters. 595:1542-1558 |
ISSN: | 1873-3468 0014-5793 |
Popis: | 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. |
Databáze: | OpenAIRE |
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