Identification of novel phosphatidic acid-binding proteins in the rat brain

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...

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Bibliographic Details
Published in:Neuroscience letters 2015-05, Vol.595, p.108-113
Main Authors: Park, ChiHu, Kang, Du-Seock, Shin, Geon-Hoon, Seo, Jeongkon, Kim, Hyein, Suh, Pann-Ghill, Bae, Chang-Dae, Shin, Joo-Ho
Format: Article
Language:English
Subjects:
Animals
Brain - metabolism
Carrier Proteins - metabolism
Guanine Nucleotide Dissociation Inhibitors - metabolism
Intercellular Signaling Peptides and Proteins - metabolism
Intracellular Signaling Peptides and Proteins - metabolism
Male
Membrane Proteins - metabolism
Myristoylated Alanine-Rich C Kinase Substrate
Nerve Tissue Proteins - metabolism
Phosphatidic Acids - metabolism
Protein Binding
Protein Kinase C - metabolism
Rats
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Summary: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.
ISSN:0304-3940
1872-7972
DOI:10.1016/j.neulet.2015.04.012