Glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)

Glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5, also known as GDE2) is a six‐transmembrane phosphodiesterase enzyme that mediates the hydrolysis of glycerophosphodiesters, including the cleavage of glycosylphosphatidylinositol (GPI) anchors from surface proteins[1][3]. GDPD5 is critical for multiple developmental and cellular processes, most notably promoting spinal motor neuron differentiation, neuronal survival, and neurite outgrowth[3]. It also regulates choline and glycerophosphocholine metabolism, influencing osmotic balance in cells[2][1]. In cancer, aberrant GDPD5 expression is associated with tumor progression, metastasis, epithelial–mesenchymal transition, and chemoresistance, while in the nervous system its activity is required for proper neuron differentiation and survival[1][3]. GDPD5 is an emerging therapeutic target for oncology and neurodegenerative disorders but currently has no established small-molecule inhibitors or approved drugs[1].

Other names

GDE2PP1665glycerophosphodiester phosphodiesterase 2glycerophosphocholine phosphodiesterase GDPD5phosphoinositide phospholipase C GDPD5Glycerophosphodiester phosphodiesterase domain-containing protein 5

Enzymatic cleavage of GPI anchors to modulate protein localization and activity; Hydrolysis of glycerophosphocholine affecting osmolyte and choline pathway metabolites