Abstract
Phosphatidic acid (PA) is an abundant negatively-charged phospholipid and has long been considered to be an important signaling molecule in diverse cellular events. Thus, the identification of proteins that specifically interact with PA is of considerable interest to understand the regulatory roles of PA. Herein, lipid-affinity purification and mass spectrometric analysis reveals 43 proteins, 19 known and 24 novel, as PA-binding proteins. A lipid-protein overlay assay confirmed that GDI1, PACSIN1, and DPYSL2 interact with not only with PA but also with other phospholipids. These results might be helpful for deciphering the functional effect of PA in the brain.
Keywords:
Brain; LC–MS/MS; Lipid–protein interaction; Phosphatidic acid.
Copyright © 2015 Elsevier Ireland Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Brain / metabolism*
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Carrier Proteins / metabolism*
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Cytoskeletal Proteins
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Guanine Nucleotide Dissociation Inhibitors / metabolism*
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Intercellular Signaling Peptides and Proteins / metabolism*
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Intracellular Signaling Peptides and Proteins / metabolism*
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Male
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Membrane Proteins / metabolism*
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Myristoylated Alanine-Rich C Kinase Substrate
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Nerve Tissue Proteins / metabolism*
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Phosphatidic Acids / metabolism*
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Protein Binding
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Protein Kinase C / metabolism*
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Rats
Substances
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Carrier Proteins
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Cytoskeletal Proteins
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GDP dissociation inhibitor 1
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Guanine Nucleotide Dissociation Inhibitors
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Intercellular Signaling Peptides and Proteins
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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Nerve Tissue Proteins
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Pacsin1 protein, rat
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Phosphatidic Acids
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collapsin response mediator protein-2
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Myristoylated Alanine-Rich C Kinase Substrate
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Protein Kinase C