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

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

This e-book provides the mobile, molecular and actual points of strength and flow via the self-assembly of actin, essentially the most considerable proteins present in cells, into cytoskeletal filaments. « Actin-based motile procedures » are accountable for a wide number of motile actions akin to chemotactic locomotion, embryonic and metastatic mobilephone migration, wound therapeutic, eukaryotic cytokinesis and bacterial plasmid segregation, endocytic and phagocytic actions, in addition to morphogenetic strategies together with, axis patterning in early embryos, axonal development in mind improvement, and the immune reaction and synaptic plasticity approaches on the starting place of studying and reminiscence. The ebook describes how the lately undertaken multidisciplinary and multiscale techniques have explored the molecular and actual mechanisms on the starting place of strength and circulation produced via actin self-assembly. the selected themes exhibit how advances were made within the box of telephone motility as a result of development in dwell 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 improvement of nanotechnologies permitting 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

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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. WASP/WAVE proteins mediate actin polymerization for both cellular protrusions, such as filopodia and lamellipodia, and invaginations, such as coated pits for endocytosis.

D. Welch. 2008. WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport. Cell. 134:148–61. , S. Wiesner, C. Le Clainche, and D. Pantaloni. 2003. Actin-based motility as a selforganized system: mechanism and reconstitution in vitro. C R Biol. 326:161–70. , and E. Paluch. 2008. Blebs lead the way: How to migrate without lamellipodia. Nat Rev Mol Cell Biol. 9:730–36. L. Goode. 2009. Actin nucleation and elongation factors: mechanisms and interplay. Curr Opin Cell Biol.

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.

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