Mesoscale simulations of curvature-inducing protein partitioning on lipid bilayer membranes in the presence of mean curvature fields

摘要

The membrane-surface migration of curvature-inducing proteins in response to membrane curvature gradients has been investigated using Monte Carlo simulations of a curvilinear membrane model based on the Helfrich Hamiltonian. Consistent with theoretical and experimental data, we find the proteins that generate curvature can also sense the background membrane curvature, wherein they preferentially partition to the high curvature regions. The partitioning strength depends linearly on local membrane curvature and the slope (or the coupling constant) of the partitioning probability versus mean curvature depends on the membrane bending rigidity and instantaneous curvature field caused by different proteins. Our simulation study allows us to quantitatively characterize and identify the important factors affecting the coupling constant (slope), which may be difficult to determine in experiments. Furthermore, the membrane model is used to study budding of vesicles where it is found that in order to stabilize a mature vesicle with a stable ‘neck-region’ (or stable membrane overhangs), the area (extent) of the intrinsic curvature region needs to exceed a threshold-critical value. The migration and partitioning of curvature-inducing proteins in a budding vesicle with a stable neck (with a characteristic negative value of the Gaussian curvature) is investigated.View full textDownload full textKeywordsMonte Carlo simulations, Helfrich Hamiltonian, curvilinear model, curvature inducing proteins, clathrin-mediated endocytosis (CME), epsin N-terminal homology (ENTH) domain proteins, Bin Amphysin Rvs (BAR) domain proteinsRelated var addthis_config = { ui_cobrand: "Taylor & Francis Online", services_compact: "citeulike,netvibes,twitter,technorati,delicious,linkedin,facebook,stumbleupon,digg,google,more", pubid: "ra-4dff56cd6bb1830b" }; Add to shortlist Link Permalink http://dx.doi.org/10.1080/00268976.2012.664661