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. 2021 Nov 2;65(5):813–845. doi: 10.1042/EBC20200067

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© 2021 The Author(s).

This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY). Open access for this article was enabled by the participation of University College London in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with JISC.

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(A) Site of action of various phospholipases (A₁, A₂, C and D) on a typical glycerol-phospholipid. The FAs at the sn-1 and sn-2 positions are removed by phospholipases A₁ and A₂ respectively. Phospholipase C and D attack the phosphodiester bond at different positions. Site of action of sphingomyelinase (SMase) on SM. SMase attacks the phosphodiester bond. (B) Examples of well-known phospholipases that cleave specific substrates. Phospholipase A₁ removes stearic acid from PI to make sn-2 arachidonyl lyso-PI, a potent signalling molecule. Cytosolic phospholipase A₂ (cPLA₂) removes arachidonic acid from either PC or PE used for the synthesis of prostaglandins, leukotrienes and thromboxanes. Phospholipase C hydrolyses PI(4,5)P₂ that generates two second messengers, I(1,4,5)P₃ and DAG. Phospholipase D hydrolyses PC to make PA and choline. SM can be attacked by SMase to make ceramide and phosphocholine.