Polymorphism of Cross-Linked Actin Networks in Giant Vesicles

Limozin, Laurent; Sackmann, E.

doi:10.1103/physrevlett.89.168103

Cited by 136 publications

(130 citation statements)

References 27 publications

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“…Because highly bent microtubules in very small droplets are expected to be strongly pressed against the boundary, the microtubules might rather align instead of crossing each other (39,40). Such an organization of confined filaments into rings has been observed previously for cross-linked actin filaments in liposomes (41).…”

Section: Discussionmentioning

confidence: 92%

Motor-mediated Cortical versus Astral Microtubule Organization in Lipid-monolayered Droplets

Baumann

Surrey

2014

Journal of Biological Chemistry

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Background: How cytoskeleton architecture is established within the confining boundary of the cell membrane is not understood. Results: Together, spatial constraints and cross-linking motor activities determine distinct motor/microtubule organizations in a biomimetic system. Conclusion: Characteristic microtubule architectures result from basic design principles. Significance: Spatial confinement plays an important role in cytoskeleton organization.

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Section: Discussionmentioning

confidence: 92%

Motor-mediated Cortical versus Astral Microtubule Organization in Lipid-monolayered Droplets

Baumann

Surrey

2014

Journal of Biological Chemistry

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“…Interestingly, for the case of ␣-actinin, both bundle and network-like structures have been reported (28,29). This behavior would indicate that the binding energy of ␣-actinin to actin should be unusually low, so that ␣-actinin might be described by Fig.…”

Section: Discussionmentioning

confidence: 99%

Structural polymorphism of the cytoskeleton: A model of linker-assisted filament aggregation

Borukhov

Bruinsma

Gelbart

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

105

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The phase behavior of charged rods in the presence of interrod linkers is studied theoretically as a model for the equilibrium behavior underlying the organization of actin filaments by linker proteins in the cytoskeleton. The presence of linkers in the solution modifies the effective interrod interaction and can lead to interfilament attraction. Depending on the composition and physical properties of the system, such as linker-binding energies, filaments will orient either perpendicular or parallel to each other, leading to network-like or bundled structures. We show that such a system can have one of three generic phase diagrams, one dominated by bundles, another by networks, and the third containing both bundle and network-like phases. The first two diagrams can be found over a wide range of interaction energies, whereas the third diagram occurs only for a narrow range. These results provide theoretical understanding of the classification of linker proteins as bundling proteins or crosslinking proteins. In addition, they suggest possible mechanisms by which the cell may control cytoskeletal morphology.actin ͉ bundle ͉ liquid crystal ͉ network F ilamentous actin (F-actin) is a highly charged, stiff biopolymer that is abundant in the cell and a key component of the cellular cytoskeleton. A cell controls the assembly of actin filaments into structures ranging from dilute networks, where filaments cross at large angles, to dense bundles, where filaments are closely packed and nearly parallel to one another (1). This structural polymorphism of actin filaments is crucial to cell function because different structures have different roles. Actin bundles have a key role during cell locomotion and cell adhesion (1). However, actin networks near the periphery of an animal cell form the cell cortex, which controls the mechanical properties of the cell surface. To exploit the functional differences between bundles and networks, cells switch between formation of these two structures during cell crawling and cell division (2, 3).Regulation of actin architecture requires control of both the kinetics of assembly and disassembly and of the morphology of actin aggregates. The assembly and disassembly of actin structures are carefully regulated by a number of specific actinbinding proteins, such as branching, capping, and severing proteins (1). However, the morphology, structure, and stability of actin aggregates are controlled by linker proteins, architectural proteins that can bind two filaments together (see refs. 4 and 5 and references therein). These linker proteins are typically classified into bundling proteins, primarily found in bundles, and crosslinking proteins, primarily found in networks. In addition, multivalent cationic species such as Ca 2ϩ , Mg 2ϩ , and spermine can control the morphology of actin aggregation and, therefore, should also be regarded as linkers.In this article, we focus on the equilibrium phase behavior of actin͞linker systems, with a view toward understanding structural polymorphism in the cytosk...

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“…[3] it is found that F-actin filaments form rings with several kinks-regions with strong variation of the tangent angle to the bundle. Such kinks are not observed for actin filament rings formed by the addition of actin crosslinking proteins [9]. We demonstrate in Fig.…”

mentioning

confidence: 57%

Counterion-Mediated Attraction and Kinks on Loops of Semiflexible Polyelectrolyte Bundles

2006

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Polymorphism of Cross-Linked Actin Networks in Giant Vesicles

Cited by 136 publications

References 27 publications

Motor-mediated Cortical versus Astral Microtubule Organization in Lipid-monolayered Droplets

Motor-mediated Cortical versus Astral Microtubule Organization in Lipid-monolayered Droplets

Structural polymorphism of the cytoskeleton: A model of linker-assisted filament aggregation

Counterion-Mediated Attraction and Kinks on Loops of Semiflexible Polyelectrolyte Bundles

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