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Phospholipase activity is modulated by c‐Fos through substrate expansion and hyperpolarization
Author(s) -
Borioli Graciela A,
Caputto Beatriz L,
Maggio Bruno
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.06.033
Subject(s) - phospholipase c , endoplasmic reticulum , phospholipase , phospholipid , biophysics , hyperpolarization (physics) , phospholipase a2 , chemistry , phosphatidylcholine , biochemistry , membrane , microbiology and biotechnology , phosphoinositide phospholipase c , enzyme , biology , stereochemistry , nuclear magnetic resonance spectroscopy
c‐Fos, a component of AP‐1 transcription factors, has been shown to have marked amphitropic properties and to regulate phospholipase activity against lipid monolayers. In agreement with its high surface activity, it has also been found to associate to membranes of the endoplasmic reticulum and to activate phospholipid metabolism in vivo. All these findings point to an involvement of this oncoprotein within a membrane environment. We have previously shown that c‐Fos modulates in different manners the activity of phospholipase A 2 and phospholipase C against monolayers of dilauroylphosphatidylcholine (PC). In this work, we have studied the possible molecular mechanism underlying the phosphohydrolytic modulation. Our results show that c‐Fos expands and hyperpolarizes PC, indicating that its effects on these enzymatic activities are due to the changes it induces on the interfacial organization of the substrate.