What are the implications of changes in lipid membrane curvature induced by beta Arrestins?
beta-Arrestins are proteins thought to turn off GPCR receptor signaling by assisting the recruitment of Clathrin leading to endocytosis of GPCRs, where the receptor is removed from the plasma membrane and the activating extracellular ligands. Our recent fluorescence microscopy studies suggest that beta-Arrestins may have a so far unknown function in nature: to induce changes in the bilayer membrane that would aid the endocytosis of the GPCR receptors. In order to determine how beta-Arrestin induces such distortion of the lipid bilayer we need to use Neutron Reflection to monitor the binding of beta-Arrestins to supported lipid bilayers and thus determine not only the positioning of beta-Arrestin within the bilayer but also the level of perturbation it induces to the lipid bilayer structure. This will be achieved by a careful study in which the protein concentration and the supported bilayer composition will be varied, and proper contrast matching. The results here obtained will permit us to identify the mechanism of interaction of beta-Arrestins with lipid bilayers and thus confirm a new biological function of this protein.
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NYLANDER Tommy; BARKER Robert; CARDENAS; Tania Kjellerup Lind; MORTENSEN Kell; NZULUMIKE Achebe and STAMOU Dimitrios. (2012). What are the implications of changes in lipid membrane curvature induced by beta Arrestins?. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-453
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