Over 100 glycosylphosphatidylinositol-anchored proteins (GPI-APs) are encoded in the mammalian genome. It is not well understood how these targeted and translocated to endoplasmic reticulum (ER). Here, we reveal that many GPI-APs, such as CD59, CD55, CD109, utilize human SND2 (hSND2)-dependent ER targeting machinery. We also found signal recognition particle receptors seem cooperate with hSND2 ...

At least 150 different human proteins are anchored to the outer leaflet of the plasma membrane via glycosylphosphatidylinositol (GPI). GPI preassembled in the endoplasmic reticulum is attached to the protein's carboxyl-terminus as a post-translational modification by GPI transamidase. Twenty-two PIG (for Phosphatidyl Inositol Glycan) genes are involved in the biosynthesis and protein-attachment...

The glycosylphosphatidylinositol membrane anchor of human placental alkaline phosphatase was isolated by exhaustive proteolysis followed by hydrophobic interaction chromatography. The resulting glycosylphosphatidylinositol-peptide was subjected to compositional analysis and chemical and enzymic modifications. The neutral-glycan fraction, prepared by dephosphorylation followed by HNO2 deaminatio...

A total of 10–20% plasma membrane proteins are anchored by glycosylphosphatidylinositol (GPI). GPI is attached to transamidase (GPI‐T), which contains five subunits named PIGK, PIGS, PIGT, PIGU, and GPAA1. We previously reported that PIGT localizes near the nucleus in Drosophila . However, localizations other four remain unknown. Here, we show a catalytic subunit GPI‐T, mainly endoplasmic retic...

Induction of proinflammatory cytokine responses by glycosylphosphatidylinositols (GPIs) of intraerythrocytic Plasmodium falciparum is believed to contribute to malaria pathogenesis. In this study, we purified the GPIs of P. falciparum to homogeneity and determined their structures by biochemical degradations and mass spectrometry. The parasite GPIs differ from those of the host in that they con...