Capping protein-controlled actin polymerization shapes lipid membranes
| Autor: | Fridtjof Brauns, Felix C. Keber, Andreas R. Bausch, Jan Faix, Philip Bleicher, Katharina Dürre, Christian J. Cyron |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Swine Actin Capping Proteins Science General Physics and Astronomy Article Actin-Related Protein 2-3 Complex General Biochemistry Genetics and Molecular Biology Polymerization Mice 03 medical and health sciences Cell Line Tumor Myosin Animals lcsh:Science Cytoskeleton Technik [600] Actin Myosin Type II Multidisciplinary Chemistry Vesicle General Chemistry Actins ddc 030104 developmental biology Endocytic vesicle Membrane Biophysics lcsh:Q Rabbits ddc:600 Membrane biophysics |
| Zdroj: | Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018) Nature Communications 9 (1): 1630 (2018-12) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | Arp2/3 complex-mediated actin assembly at cell membranes drives the formation of protrusions or endocytic vesicles. To identify the mechanism by which different membrane deformations can be achieved, we reconstitute the basic membrane deformation modes of inward and outward bending in a confined geometry by encapsulating a minimal set of cytoskeletal proteins into giant unilamellar vesicles. Formation of membrane protrusions is favoured at low capping protein (CP) concentrations, whereas the formation of negatively bent domains is promoted at high CP concentrations. Addition of non-muscle myosin II results in full fission events in the vesicle system. The different deformation modes are rationalized by simulations of the underlying transient nature of the reaction kinetics. The relevance of the regulatory mechanism is supported by CP overexpression in mouse melanoma B16-F1 cells and therefore demonstrates the importance of the quantitative understanding of microscopic kinetic balances to address the diverse functionality of the cytoskeleton. Cell membrane protrusions and invaginations are both driven by actin assembly but the mechanism leading to different membrane shapes is unknown. Using a minimal system and modelling the authors reconstitute the deformation modes and identify capping protein as a regulator of both deformation types. |
| Databáze: | OpenAIRE |
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