By J. Victor Small, Klemens Rottner (auth.), Marie-France Carlier (eds.)
This booklet offers the mobile, molecular and actual facets of strength and circulation through the self-assembly of actin, probably the most ample proteins present in cells, into cytoskeletal filaments. « Actin-based motile approaches » are accountable for a wide number of motile actions corresponding to chemotactic locomotion, embryonic and metastatic telephone migration, wound therapeutic, eukaryotic cytokinesis and bacterial plasmid segregation, endocytic and phagocytic actions, in addition to morphogenetic methods together with, axis patterning in early embryos, axonal progress in mind improvement, and the immune reaction and synaptic plasticity tactics on the beginning of studying and reminiscence. The booklet describes how the lately undertaken multidisciplinary and multiscale techniques have explored the molecular and actual mechanisms on the foundation of strength and move produced by means of actin self-assembly. the selected themes express how advances were made within the box of cellphone motility as a result growth in stay phone imaging, mild microscopy, enhanced solution within the constitution of enormous protein assemblies, the biochemical research and mathematical modeling of actin meeting dynamics and the advance of nanotechnologies allowing us to degree forces within the variety of pico- to nano-newtons produced by way of actin assemblies.
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Extra resources for Actin-based Motility: Cellular, Molecular and Physical Aspects
101:597–602. , A. C. D. Salmon. 1998. Fluorescent speckle microscopy, a method to visualize the dynamics of protein assemblies in living cells. Curr Biol. 8:1227–30. Wegner, A. 1976. Head to tail polymerization of actin. J Mol Biol. 108:139–50. A. F. J. W. Kirschner. 2007. An actinbased wave generator organizes cell motility. PLoS Biol. 5:e221. P. Newsome, S. Schleich, and M. Way. 2009. The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility. Nature. 458: 87–91.
Membrane Deformation by the BAR and EFC/F-BAR Domains . . . . . The BAR and EFC/F-BAR Domain-Containing Proteins are Connected to the actin Cytoskeleton Through N-WASP . . . . . . 5 IMD/I-Bar Domain Induces Outward Protrusions . . . . . . . . 6 Direction of Actin Polymerization Beneath the Membrane . . . . . . 7 Membrane Curvature-Dependent Actin Polymerization . . . . . . . 8 Conclusions: Activation of Signal Transduction Cascades by Membrane Curvature .
Holt, J. Y. Soong, C. A. Dunn. 2003. Rapid actin transport during cell protrusion. Science. 300:142–45. , K. Meerschaert, G. Reekmans, I. V. Small, J. Vandekerckhove, G. David, and J. Gettemans. 2002. PIP(2)-PDZ domain binding controls the association of syntenin with the plasma membrane. Mol Cell. 9:1215–25. S. E. B. D. Mullins. 2009. p53-cofactor JMY is a multifunctional actin nucleation factor. Nat Cell Biol. 11:451–59. Chapter 2 Coupling Membrane Dynamics to Actin Polymerization Shiro Suetsugu and Tadaomi Takenawa Abstract WASP/WAVE family proteins are important regulators of the Arp2/3 complex, which causes exponential growth of actin filaments.
Actin-based Motility: Cellular, Molecular and Physical Aspects by J. Victor Small, Klemens Rottner (auth.), Marie-France Carlier (eds.)