Post-GPI attachment to proteins factor 6 (PGAP6)

Post-GPI attachment to proteins factor 6 (PGAP6) is a transmembrane phospholipase A2 enzyme involved in post-translational lipid remodeling of glycosylphosphatidylinositol (GPI) anchors. It specifically removes a fatty acyl-chain at the sn-2 position of the GPI anchor, which is essential for the maturation and function of a subset of GPI-anchored proteins. PGAP6 has a large extracellular N-terminal domain and seven transmembrane domains, and belongs to the CREST superfamily of lipases. Its enzymatic activity is highly specific, targeting only a limited set of GPI-anchored proteins, notably triggering the release (shedding) of CRIPTO, a GPI-anchored co-receptor critical for Nodal signaling in embryonic development. By enabling the release of soluble CRIPTO, PGAP6 finely regulates intercellular signaling events, particularly in early embryogenesis. Pathogenic variants in PGAP6 have been associated with neurological and developmental disorders, and dysfunction in GPI-anchor processing can broadly affect cell signaling and development[1][2][5][6].

Other names

TMEM6TMEM8TMEM8AGPI-PLA2M83GPI processing phospholipase A2Protein M83Transmembrane protein 6Transmembrane protein 8Transmembrane protein 8Afive-span transmembrane protein M83post-glycosylphosphatidylinositol attachment to proteins 6