GPLD1 hydrolyses GPI-anchors from proteins

Stable Identifier
R-HSA-8940388
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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.

Literature References
PubMed ID Title Journal Year
2443973 A glycan-phosphatidylinositol-specific phospholipase D in human serum

Davitz, MA, Hereld, D, Shak, S, Krakow, J, Englund, PT, Nussenzweig, V

Science 1987
11072085 Structure and expression of the human glycosylphosphatidylinositol phospholipase D1 (GPLD1) gene

Schofield, JN, Rademacher, TW

Biochim. Biophys. Acta 2000
3422494 A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma

Low, MG, Prasad, AR

Proc. Natl. Acad. Sci. U.S.A. 1988
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Catalyst Activity
Title
glycosylphosphatidylinositol phospholipase D activity of GPLD1 [extracellular region]
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Orthologous Events
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