Abstract
PKCα is a member of a large family of serine/threonine kinases that is involved in diverse cellular signaling pathways. The primary mode of PKCα regulation involves the C2 subunit docking with the cell membrane; however the molecular mechanisms of these interactions are poorly understood. Therefore, we used atomistic molecular dynamics simulations to systematically investigate the interaction between PKCα-C2 domains and lipid bilayers. In this study, three lipid bilayers with different compositions (pure POPC, POPC/POPS/PIP2 and POPC/POPS/PIP2/POG) were used to study the effects of POPC, PIP2, and POG on PKCα-C2 docking to the lipid bilayer. In the absence of POPS and PIP2, our results show that the PKCα-C2 domain does not interact with the bilayer surface. In contrast, in the presence of POPS and PIP2, the domain strongly docked to lipid bilayers. Furthermore, the results show that POG alters hydrogen bonding patterns between PKCa-C2 and PIP2 molecules. We hypothesize that POG facilitates the docking of PKCα-C2 domain to the bilayer by modifying the bilayer headgroup region.
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