Expression of ATP-binding cassette transporter A1 is induced by nerve injury and its deficiency affects neurite tip morphology and elongation in cultured neurons.

Axonal regeneration requires changes in the lipid dynamics of the axon membrane for growth and extension. Here, we examined the expression of genes associated with lipid transport after nerve injury. The expression of ATP-binding cassette transporter-A1 (ABCA1), which participates in the transport of cholesterol from the plasma membrane, was markedly upregulated in motor and sensory neurons after nerve injury.

Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I.

Within the endoplasmic reticulum (ER), mannoses and glucoses, donated from dolichol-phosphate-mannose and -glucose, are transferred to N-glycan and GPI-anchor precursors, and serine/threonine residues in many proteins. Glycosyltransferases that mediate these reactions are ER-resident multitransmembrane proteins with common characteristics, forming a superfamily of >10 enzymes. Here, we report an essential component of glycosylphosphatidylinositol-mannosyltransferase I (GPI-MT-I), which transfers the first of the four mannoses in the GPI-anchor precursors.

GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol.

Many eukaryotic cell surface proteins are anchored to the membrane via glycosylphosphatidylinositol (GPI). GPI is synthesized from phosphatidylinositol by stepwise reactions and attached en bloc to nascent proteins. In mammalian cells, the major GPI species transferred to proteins is termed H7.

PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol.

Glycosylphosphatidylinositol (GPI) is a glycolipid that anchors many proteins to the eukaryotic cell surface. The biosynthetic pathway of GPI is mediated by sequential additions of sugars and other components to phosphatidylinositol. Four mannoses in the GPI are transferred from dolichol-phosphate-mannose (Dol-P-Man) and are linked through different glycosidic linkages.