Unmyristoylated MARCKS-related protein (MRP) binds to supported planar phosphatidylcholine membranes.
We have recently shown that unmyristoylated MARCKS-related protein (MRP) does not bind to neutral phospholipid vesicles, unless negatively charged phospholipids are present. Similar behaviour has also been reported for MARCKS itself. Here we have compared the binding of MRP to neutral and negatively charged supported planar lipid bilayer membranes (SPLM) using two-mode waveguide spectroscopy. We find appreciable binding of unmyristoylated MRP to neutral SPLM. We propose that hydrophobic residues in the effector domain constitute an additional factor capable of mediating MRP-membrane interaction.
Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland.
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Michielin
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Ramsden
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Vergères
D000818:Animals; D002148:Calmodulin-Binding Proteins; D004926:Escherichia coli; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins / Q000737:chemistry*; D008567:Membranes, Artificial; D051379:Mice; D008840:Microfilament Proteins; D010713:Phosphatidylcholines / Q000737:chemistry*; D011485:Protein Binding; D017510:Protein Folding
D002148:Calmodulin-Binding Proteins; D047908:Intracellular Signaling Peptides and Proteins; C512945:Marcksl1 protein, mouse; D008565:Membrane Proteins; D008567:Membranes, Artificial; D008840:Microfilament Proteins; D010713:Phosphatidylcholines