 |
Center for Nonlinear Studies |
Membranes serve as a framework to organize proteins and lipids into signaling platforms. Many peripheral signaling proteins are targeted to membranes via lipid-based motifs, which are generated by the post-translational modification of glycine or cysteine residues by acyl and prenyl groups. The quintessential example of lipid-anchored proteins is the guanine triphosphate (GTP) hydrolyzing Ras superfamily of small GTPases. Compared to protein-based membrane targeting motifs such as the C1, C2 and PH domains, much less is known about the structural and biophysical basis of membrane targeting by the intrinsically disordered lipid-based membrane targeting motifs. Using molecular dynamics simulations and experiments, we have begun to gain insights into the capacity of these short peptide segments in encoding binding specificity for specific acyl chains and lipid headgroups, which allow differential responses to biophysical perturbations that may have biological and signaling consequences for lipid-anchored small GTPases.
Host: Angel Garcia