Structural basis of phosphatidylcholine recognition by the C2-domain of cytosolic phospholipase A₂α.

ABSTRACT: Ca²⁺-stimulated translocation of cytosolic phospholipase A₂α (cPLA₂α) to the Golgi induces arachidonic acid production, the rate-limiting step in pro-inflammatory eicosanoid synthesis. Structural insights into the cPLA₂α preference for phosphatidylcholine (PC)-enriched membranes have remained elusive. Here, we report the structure of the cPLA₂α C2-domain (at 2.2 Å resolution), which contains bound 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) and Ca²⁺ ions. Two Ca²⁺ are complexed at previously reported locations in the lipid-free C2-domain. One of these Ca²⁺ions, along with a third Ca²⁺, bridges the C2-domain to the DHPC phosphate group, which also interacts with Asn65. Tyr96 plays

SUBMITTER: Hirano Y 

PROVIDER: S-EPMC6550875 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature