title: External push and internal pull forces recruit curvature-sensing N-BAR domain proteins to the plasma membrane.
abstract: Many of the more than 20 mammalian proteins with N-BAR domains control cell architecture and endocytosis by associating with curved sections of the plasma membrane. It is not well understood whether N-BAR proteins are recruited directly by processes that mechanically curve the plasma membrane or indirectly by plasma-membrane-associated adaptor proteins that recruit proteins with N-BAR domains that then induce membrane curvature. Here, we show that externally induced inward deformation of the plasma membrane by cone-shaped nanostructures (nanocones) and internally induced inward deformation by contracting actin cables both trigger recruitment of isolated N-BAR domains to the curved plasma membrane. Markedly, live-cell imaging in adherent cells showed selective recruitment of full-length N-BAR proteins and isolated N-BAR domains to plasma membrane sub-regions above nanocone stripes. Electron microscopy confirmed that N-BAR domains are recruited to local membrane sites curved by nanocones. We further showed that N-BAR domains are periodically recruited to curved plasma membrane sites during local lamellipodia retraction in the front of migrating cells. Recruitment required myosin-II-generated force applied to plasma-membrane-connected actin cables. Together, our results show that N-BAR domains can be directly recruited to the plasma membrane by external push or internal pull forces that locally curve the plasma membrane.
authors: Department of Chemical and Systems Biology, Stanford University, 318 Campus Drive, Clark Building W200, Stanford, California 94305, USA. milos@stanford.edu
authors: Milos
authors: M
authors: Galic
authors: Sangmoo
authors: S
authors: Jeong
authors: Feng-Chiao
authors: FC
authors: Tsai
authors: Lydia-Marie
authors: LM
authors: Joubert
authors: Yi I
authors: YI
authors: Wu
authors: Klaus M
authors: KM
authors: Hahn
authors: Yi
authors: Y
authors: Cui
authors: Tobias
authors: T
authors: Meyer
mesh_terms: D016475:3T3 Cells; D000199:Actins / Q000502:physiology*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D055595:Mechanical Phenomena; D051379:Mice; D008855:Microscopy, Electron, Scanning; D049329:Nanostructures; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism; D054730:Protein Interaction Domains and Motifs / Q000502:physiology*
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; C075637:amphiphysin