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10.1038/s41467-018-03918-1 http://scihub22266oqcxt.onion/10.1038/s41467-018-03918-1 C5915599!5915599 !29691404     free     free     free       Nat+Commun 2018 ; 9 (1 ): 1630 Nephropedia Template TP {{tp|p=29691404 |t=2018. Capping protein-controlled actin polymerization shapes lipid membranes |pdf=|usr=}}{{29691404 }} gab.com Text Capping protein-controlled actin polymerization shapes lipid membranes JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29691404 #FOAvip 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. Twit Text FOAVip Capping protein-controlled actin polymerization shapes lipid membranes ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29691404 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29691404 #FOAvip English Wikipedia <ref>{{Cite pmid|29691404 }}</ref> Capping protein-controlled actin polymerization shapes lipid membranes #MMPMID29691404 Dürre K ; Keber FC ; Bleicher P ; Brauns F ; Cyron CJ ; Faix J ; Bausch AR Nat Commun 2018[Apr]; 9 (1 ): 1630 PMID29691404 show ga 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. |Actin Capping Proteins/*metabolism [MESH] |Actin-Related Protein 2-3 Complex/genetics/metabolism [MESH] |Actins/chemistry/*metabolism [MESH] |Animals [MESH] |Cell Line, Tumor [MESH] |Cytoskeleton/genetics/metabolism [MESH] |Mice [MESH] |Myosin Type II/genetics/metabolism [MESH] |Polymerization [MESH] |Rabbits [MESH]Capping protein-controlled actin polymerization shapes lipid membranes(epmc).pdf DeepDyve Pubget Overpricing