1 Biocomplexity, The Niels Bohr Institute, Faculty of Science, Københavns Universitet2 Administration, Department of Chemistry, Faculty of Science, Københavns Universitet3 Niels Bohr Institutet4 Institute for Advanced Studies in Basic Sciences (IASBS)5 Biocomplexity, The Niels Bohr Institute, Faculty of Science, Københavns Universitet6 Administration, Department of Chemistry, Faculty of Science, Københavns Universitet
Syndapin 1 FBAR, a member of the Bin-amphiphysin-Rvs (BAR) domain protein family, is known to induce membrane curvature and is an essential component in biological processes like endocytosis and formation and growth of neurites. We quantify the curvature sensing of FBAR on reconstituted porcine brain lipid vesicles and show that it senses membrane curvature at low density whereas it induces and reinforces tube stiffness at higher density. FBAR strongly up-concentrates on the high curvature tubes pulled out of Giant Unilamellar lipid Vesicles (GUVs), this sorting behavior is strongly amplified at low protein densities. Interestingly, FBAR from syndapin 1 has a large affinity for tubular membranes with curvatures larger than its own intrinsic concave curvature. Finally, we studied the effect of FBAR on membrane relaxation kinetics with high temporal resolution and found that the protein increases relaxation time of the tube holding force in a density-dependent fashion.