Membrane homeostasis in bacteria relies on the controlled degradation of endogenous phospholipids by intracellular phospholipases A, however their structures and catalytic mechanism are still poorly understood.

The C2-domain of cytoplasmic phospholipase A₂α is structurally designed to target PC-rich membrane regions to increase the enzymatic efficiency of the catalytic domain, which prefers PCs with polyunsaturated acyl chains.

PLC-γ isozymes are activated by a combination of receptor engagement and membrane proximity.

Phosphatidic acid regulates recycling of endocytosed plasma membrane vesicles in polarized cells through a retromer and Arf1 dependent process.

Bardet–Biedl syndrome 3 (BBS3) protein promotes phospholipase D to load onto the BBSome at the ciliary tip for moving out of the cilium via intraflagellar transport.

GDE3 is a transmembrane GPI-specific phospholipase C that sheds the urokinase receptor (uPAR) from the cell surface resulting in loss of uPAR function in breast cancer cells and reduced tumor growth.

Pseudomonas aeruginosa defends against interbacterial antagonism through the coordinated expression of previously uncharacterized pathways that grant threat-specific protection.

SAA removes toxic products of lipolysis of the cell membrane by sPLA₂, indicating that SAA and sPLA₂ act synergistically to clear debris from injured sites, as required for tissue healing.

The high-resolution X-ray crystal structure of PLC-γ1 reveals a unifying model for the regulation of the PLC-γ isozymes.

Sec14l3/SEC14L2 respond to upstream Wnt/Frizzled/Dvl stimulation to recruit and activate phospholipase Cδ4a (Plcδ4a) to further initiate calcium release.