PL(C)D4:3xCa2+ hydrolse PI(4,5)P2 to I(1,4,5)P3 and DAG at the ER membrane

Stable Identifier
Reaction [transition]
Homo sapiens
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At the endoplasmic reticulum (ER) membrane, 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (PLCD4) and phospholipase D4 (PLD4) hydrolyse phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to inositol 1,4,5-trisphosphate (I(1,4,5)P3) and diacylglycerol (DAG). Both lipases are thought to require three Ca2+ ions per subunit for activity. PLD4 is attached to the ER membrane via its PH domain while its C2 domain binds to the PI(4,5)P2 in the membrane (Lee et al. 2004). Overexpression or dysregulated expression of PLCD4 may initiate oncogenesis in certain tissues through upregulation of ErbB expression and activation of ERK pathway. PLCD4 can therefore be a useful tumor marker for breast or testicular cancer tissues (Leung et al. 2004).
Literature References
PubMed ID Title Journal Year
15140260 Phospholipase C delta-4 overexpression upregulates ErbB1/2 expression, Erk signaling pathway, and proliferation in MCF-7 cells

Ball, A, Morris, V, Coon, M, Singer, JW, Brewer, J, Waggoner, D, Leung, DW, Tompkins, C

Mol Cancer 2004
15037625 The pleckstrin homology domain of phosphoinositide-specific phospholipase Cdelta4 is not a critical determinant of the membrane localization of the enzyme

Balla, T, Jalink, K, Balla, A, VĂ¡rnai, P, Rhee, SG, Lee, SB

J Biol Chem 2004
Catalyst Activity

phosphatidylinositol phospholipase C activity of PL(C)D4:3xCa2+ [endoplasmic reticulum membrane]

Orthologous Events
Cross References
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