Molecular motors work with protein scaffolds to drive fission of membrane tubules.

Simunovic, Mijo;Manneville, Jean-Baptiste;Renard, Henri-François;Johannes, Ludger;Bassereau, Patricia;et.al.
(2015) EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS

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Authors
  • Simunovic, MijoThe University of Chicago, USA
    Author
  • Manneville, Jean-BaptisteInstitut Curie, France
    Author
  • Renard, Henri-FrançoisUCLouvain
    Author
  • Johannes, LudgerInstitut Curie, France
    Author
  • Bassereau, PatriciaInstitut Curie, France
    Author
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Abstract
Lipid membranes mediate the interaction of cells with the external environment. A number of proteins alter its shape, facilitating key cellular phenomena such as endocytosis, the formation of organelles, infection, etc. The most notable membrane sculptors are proteins that contain an intrinsically curved BAR domain. These proteins have frequently been associated with endocytosis, a process by which cells regulate the uptake of external material, however their precise role has remained elusive. By using quantitative fluorescence microscopy on model membranes and on cells, we show a new role of a BAR protein endophilin and demonstrate that it can drive its own clathrin-independent endocytic pathway. Surprisingly, we uncover a dynamic interplay between BAR proteins and molecular motors. By constructing a minimal experimental model, we demonstrate that molecular motors dynamically function with scaffolds formed by BAR proteins to cut the membrane tubules, an event that separates the endocytic vesicle from the plasma membrane. Our work elucidates the physics underlying an endocytic pathway used by the cells to internalize various signaling proteins and bacterial toxins.
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Citations

Simunovic, M., Manneville, J.-B., Renard, H.-F., Johannes, L., Evergren, E., McMahon, H., Callan-Jones, A., Prost, J., Voth, G. A., & Bassereau, P. (2015). Molecular motors work with protein scaffolds to drive fission of membrane tubules. European Biophysics Journal, 44(Suppl 1), S97. https://doi.org/10.1007/s00249-015-1045-6 (Original work published 2015)