ArticleProceedings of the National Academy of Sciences of the United States of America2015
Membranes serve as allosteric activators of phospholipase A2, enabling it to extract, bind, and hydrolyze phospholipid substrates.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
56 citing papers in PubMed, 95 citations in OpenAlex.
- Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Specificity mechanism of Group VIA calcium-independent phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2025Article
- Conformational Dynamics and Activation of Membrane-Associated Human Group IVA Cytosolic Phospholipase AThe journal of physical chemistry letters · 2025Article
- The mechanism of allosteric regulation of calcium-independent phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2024Article
- A Membrane-Assisted Mechanism for the Release of Ceramide from the CERT START Domain.The journal of physical chemistry. B · 2024Article
- Site-directed spin label EPR studies of the structure and membrane interactions of the bacterial phospholipase ExoU.Applied magnetic resonance · 2024Article
- Multifaceted membrane interactions of human Atg3 promote LC3-phosphatidylethanolamine conjugation during autophagy.Nature communications · 2023Article
- Molecular basis of unique specificity and regulation of group VIA calcium-independent phospholipase APharmacology & therapeutics · 2023Review
- The Phospholipase A2 Superfamily: Structure, Isozymes, Catalysis, Physiologic and Pathologic Roles.International journal of molecular sciences · 2023Review
- Regulatory mechanisms triggered by enzyme interactions with lipid membrane surfaces.Frontiers in molecular biosciences · 2023Review
- Membrane Association Allosterically Regulates Phospholipase AAccounts of chemical research · 2022Article
- Phosphatidylcholine Cation-Tyrosine π Complexes: Motifs for Membrane Binding by a Bacterial Phospholipase C.Molecules (Basel, Switzerland) · 2022Review
- Article
- Bioactive lipids and metabolic syndrome-a symposium report.Annals of the New York Academy of Sciences · 2022Article
- Allosteric regulation by membranes and hydrophobic subsites in phospholipase AThe Journal of biological chemistry · 2022Review
- Lipoprotein-associated phospholipase AProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Each phospholipase ABiochimica et biophysica acta. Molecular and cell biology of lipids · 2022Article
- Mechanistic Understanding from Molecular Dynamics in Pharmaceutical Research 2: Lipid Membrane in Drug Design.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Purification of Cytosolic Phospholipase ABio-protocol · 2021Article
- Omega-3 versus Omega-6 fatty acid availability is controlled by hydrophobic site geometries of phospholipase AJournal of lipid research · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Defining the molecular details and consequences of the association of water-soluble proteins with membranes is fundamental to understanding protein-lipid interactions and membrane functioning. Phospholipase A2 (PLA2) enzymes, which catalyze the hydrolysis of phospholipid substrates that compose the membrane bilayers, provide the ideal system for studying protein-lipid interactions. Our study focuses on understanding the catalytic cycle of two different human PLA2s: the cytosolic Group IVA cPLA2 and calcium-independent Group VIA iPLA2. Computer-aided techniques guided by deuterium exchange mass spectrometry data, were used to create structural complexes of each enzyme with a single phospholipid substrate molecule, whereas the substrate extraction process was studied using steered molecular dynamics simulations. Molecular dynamic simulations of the enzyme-substrate-membrane systems revealed important information about the mechanisms by which these enzymes associate with the membrane and then extract and bind their phospholipid substrate. Our data support the hypothesis that the membrane acts as an allosteric ligand that binds at the allosteric site of the enzyme's interfacial surface, shifting its conformation from a closed (inactive) state in water to an open (active) state at the membrane interface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.