Actin-based Motility: Cellular, Molecular and Physical by J. Victor Small, Klemens Rottner (auth.), Marie-France

By J. Victor Small, Klemens Rottner (auth.), Marie-France Carlier (eds.)

This booklet provides the mobile, molecular and actual points of strength and circulation by means of the self-assembly of actin, probably the most plentiful proteins present in cells, into cytoskeletal filaments. « Actin-based motile tactics » are chargeable for a wide number of motile actions corresponding to chemotactic locomotion, embryonic and metastatic mobilephone migration, wound therapeutic, eukaryotic cytokinesis and bacterial plasmid segregation, endocytic and phagocytic actions, in addition to morphogenetic tactics together with, axis patterning in early embryos, axonal development in mind improvement, and the immune reaction and synaptic plasticity methods on the foundation of studying and reminiscence. The ebook describes how the lately undertaken multidisciplinary and multiscale techniques have explored the molecular and actual mechanisms on the beginning of strength and move produced by way of actin self-assembly. the selected issues convey how advances were made within the box of telephone motility as a result growth in dwell cellphone imaging, mild microscopy, better solution within the constitution of enormous protein assemblies, the biochemical research and mathematical modeling of actin meeting dynamics and the advance of nanotechnologies permitting us to degree forces within the diversity of pico- to nano-newtons produced via actin assemblies.

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Extra info for Actin-based Motility: Cellular, Molecular and Physical Aspects

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The contractile bundle around the periphery of the trailing part of the cell is formed via prior ruffling activity at those locations. Actin filaments are in green, myosin filaments in blue (Fig. 8). , 2008), it is not directly dependent on myosin II. We should not be left with the misconception that filaments generated at the front of a moving cell end up at the rear. It is the prehistory of protrusion, substrate adhesion and contractile activity at specific regions of the cell periphery that determines the local organization of the actin cytoskeleton.

B. M. G. Borisy. 2004. Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell. 118:363–73. , B. M. Kessels, and W. Almers. 2004. Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrinmediated endocytosis in cultured fibroblasts. Eur J Cell Biol. 83:13–8. , and M. Kirschner. 1988. Cytoskeletal dynamics and nerve growth. Neuron. 1: 761–72. , H. Miki, H. He, H. Maruta, and T. Takenawa. 2002.

Wehland, and R. Kuhn. 2001. Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2:850–57. H. Insall. 1998. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr Biol. 8:1347–56. D. Pollard. 2008. Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry. 47:6460–67. D. Pollard.

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