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

Hirano, Yoshinori; Gao, Yong-Guang; Stephenson, Daniel J.; Vu, Ngoc T.; Malinina, Lucy; Simanshu, Dhirendra K.; Chalfant, Charles E.; Patel, Dinshaw J.; Brown, Rhoderick E.

doi:10.7554/eLife.44760

Title: Structural basis of phosphatidylcholine recognition by the C2–domain of cytosolic phospholipase A₂α

Journal Article · Fri May 03 00:00:00 EDT 2019 · eLife

DOI:https://doi.org/10.7554/eLife.44760· OSTI ID:1526068

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^[3]; Vu, Ngoc T. ^[4];

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^[6]; Patel, Dinshaw J. ^[5];

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Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, United States; Graduate School of Biological Sciences, Nara Institute of Science and Technology (NAIST), Takayama, Japan
Hormel Institute, University of Minnesota, Austin, United States
Department of Biochemistry and Molecular Biology, Virginia Commonwealth University Medical Center, Richmond, United States; Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, United States
Department of Biochemistry and Molecular Biology, Virginia Commonwealth University Medical Center, Richmond, United States
Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, United States
Department of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, United States; Research Service, James A. Haley Veterans Hospital, Tampa, United States; The Moffitt Cancer Center, Tampa, United States

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 a key role in lipid headgroup recognition via cation–π interaction with the PC trimethylammonium group. Mutagenesis analyses confirm that Tyr96 and Asn65 function in PC binding selectivity by the C2-domain and in the regulation of cPLA₂α activity. The DHPC-binding mode of the cPLA₂α C2-domain, which differs from phosphatidylserine or phosphatidylinositol 4,5-bisphosphate binding by other C2-domains, expands and deepens knowledge of the lipid-binding mechanisms mediated by C2-domains.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: DOE - OTHERNIHFOREIGN

OSTI ID:: 1526068

Journal Information:: eLife, Vol. 8, Issue 2019; ISSN 2050-084X

Publisher:: eLife Sciences Publications, Ltd.

Country of Publication:: United States

Language:: ENGLISH

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