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

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

Stable Identifier

R-HSA-1855214

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum membrane, cytosol

ReviewStatus

5/5

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

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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, Várnai, P, Rhee, SG, Lee, SB	J Biol Chem	2004