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- W2034173988 abstract "A major aim of our work is to understand the mechanisms behind dynamic organization of the cellular plasma membrane, especially local heterogeneities such as nanometer sized lipid domains (Mayor and Rao, 2004). As reported previously, glycosyl-phosphatidylinositol-anchored protein (GPI-AP) organization in nano-clusters in the plasma membrane is driven by the activity of cortical actin (Goswami et al., 2008).A recent theoretical framework and its experimental verification suggests that the engagement of short actin filaments together with myosin-motor like activity at the inner leaflet is sufficient to explain all the unusual features of GPI-AP organization at the outer leaflet (Gowrishankar et al., 2012).Here, we present a strategy to reconstitute cortical actin dynamics in vitro on supported lipid bi-layers. This allows us to explore the role of proteins thought to be involved in actin cluster formation and to test predictions of the theoretical model. In a first step, we investigate how the diffusion of membrane bound actin binding proteins is affected by actin filaments of varying lengths. Then, we increase the complexity of the system including myosin motors, and actin modifying proteins, and identify conditions under which actin remodeling, i.e. transient formation of actin asters, occurs. As suggested by observation in cells and by the theoretical framework, short actin filaments (< 1 μm) are the main source of fast remodeling events whereas longer filaments create a more static meshwork, which can confine membrane bound particles. In summary, we introduce a new kind of minimal dynamic actin cortex, and show how dynamic short actin filaments can drive the organization of membrane components." @default.
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- W2034173988 date "2014-01-01" @default.
- W2034173988 modified "2023-09-28" @default.
- W2034173988 title "In Vitro Reconstitution of Remodeling Actin Asters - Steps towards a Minimal Active Actomyosin Cortex" @default.
- W2034173988 doi "https://doi.org/10.1016/j.bpj.2013.11.964" @default.
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