GPLD1 hydrolyses GPI-anchors from proteins

Some proteins function at the cell's surface, attached to the plasma membrane via GPI (glycosylphosphatidylinositol) anchors and include enzymes, receptors, cell adhesion molecules and antigens. These GPI-anchored proteins participate in many important cellular functions including immune recognition, complement regulation and intracellular signaling. Phosphatidylinositol-glycan-specific phospholipase D (GPLD1) (Schofield et al. 2000) is a secreted protein that specifically cleaves GPI-anchored proteins by cleaving the linkage between the phosphate and inositol in GPI (Davitz et al. 1987, Low & Prasad 1988). In addition, it also localises to the ER where it can cleave GPI anchor intermediates transiting to the plasma membrane (not shown here). GPLD1 may play a role in the regulation of GPI-anchored proteins on (intra)cellular membranes.

某些蛋白质在细胞表面发挥作用，通过GPI（糖基磷脂酰肌醇）锚定连接至质膜，其中包括酶、受体、细胞粘附分子和抗原。这些GPI锚定蛋白参与众多重要的细胞功能，如免疫识别、补体调控和细胞内信号传导。磷脂酰肌醇糖基特异性磷脂酶D（GPLD1）（Schofield等，2000年）是一种分泌蛋白，它通过切断GPI中磷酸与肌醇之间的连接，特异性地裂解GPI锚定蛋白（Davitz等，1987年，Low与Prasad，1988年）。此外，它还定位于内质网，在那里它可以裂解正在向质膜转运的GPI锚定中间体（此处未展示）。GPLD1可能在调节细胞（内）膜上的GPI锚定蛋白方面发挥作用。