@article{8d84d993a43048eba50f15058075a806,
title = "Friction Mediates Scission of Tubular Membranes Scaffolded by BAR Proteins",
abstract = "Membrane scission is essential for intracellular trafficking. While BAR domain proteins such as endophilin have been reported in dynamin-independent scission of tubular membrane necks, the cutting mechanism has yet to be deciphered. Here, we combine a theoretical model, in vitro, and in vivo experiments revealing how protein scaffolds may cut tubular membranes. We demonstrate that the protein scaffold bound to the underlying tube creates a frictional barrier for lipid diffusion; tube elongation thus builds local membrane tension until the membrane undergoes scission through lysis. We call this mechanism friction-driven scission (FDS). In cells, motors pull tubes, particularly during endocytosis. Through reconstitution, we show that motors not only can pull out and extend protein-scaffolded tubes but also can cut them by FDS. FDS is generic, operating even in the absence of amphipathic helices in the BAR domain, and could in principle apply to any high-friction protein and membrane assembly.",
keywords = "BAR domain, diffusion barrier, endocytosis, endophilin, friction-driven scission, in vitro reconstitution, membrane scission, membrane tube, molecular motors, scaffold, Acyltransferases/chemistry, Humans, Rats, Lipid Metabolism, Biomechanical Phenomena, Endocytosis, Animals, Membrane Proteins/chemistry, Friction, Protein Domains",
author = "Mijo Simunovic and Manneville, {Jean Baptiste} and Renard, {Henri Fran{\c c}ois} and Emma Evergren and Krishnan Raghunathan and Dhiraj Bhatia and Kenworthy, {Anne K.} and Voth, {Gregory A.} and Jacques Prost and McMahon, {Harvey T.} and Ludger Johannes and Patricia Bassereau and Andrew Callan-Jones",
note = "Funding Information: We thank Laura Picas and Marta Bally for assistance in membrane sheet and supported bilayer experiments. M.S. and G.A.V. acknowledge the support of the National Institute of General Medical Sciences of the National Institutes of Health (award number R01GM063796). P.B. and L.J. acknowledge the support of the Agence Nationale pour la Recherche (ANR-11BSV201403 to P.B. and ANR-16-CE23-0005-02 to L.J.), L.J. acknowledges the support of the European Research Council advanced grant (project 340485), E.E. and H.T.M. acknowledge the support of the Medical Research Council UK (grant U105178795), and A.K.K. acknowledges the support of the NIH (grant R01 GM106720). M.S. was funded in part by the Chateaubriand fellowship and the France and Chicago Collaborating in the Sciences grant (both through the University of Chicago) and received support from the University Paris Diderot. The P.B. group belongs to the CNRS consortium CellTiss; the P.B., J.P., and L.J. groups belong to Labex CelTisPhyBio (ANR-11-LABX0038) and to Paris Sciences et Lettres (ANR-10-IDEX-0001-02). Publisher Copyright: {\textcopyright} 2017 Elsevier Inc. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",
year = "2017",
month = jun,
day = "29",
doi = "10.1016/j.cell.2017.05.047",
language = "English",
volume = "170",
pages = "172--184.e11",
journal = "Cell Cycle",
issn = "1538-4101",
publisher = "Landes Bioscience",
number = "1",
}