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Actin Polymerization

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Kathleen G Morgan – One of the best experts on this subject based on the ideXlab platform.

  • Actin Polymerization in differentiated vascular smooth muscle cells requires vasodilator stimulated phosphoprotein
    American Journal of Physiology-cell Physiology, 2010
    Co-Authors: Philip Graceffa, Kathleen G Morgan, Francois Ferron, Cynthia Gallant, Malgorzata Boczkowska, Roberto Dominguez

    Abstract:

    Our group has previously shown that vasoconstrictors increase net Actin Polymerization in differentiated vascular smooth muscle cells (dVSMC) and that increased Actin Polymerization is linked to co…

Evelyne Friederich – One of the best experts on this subject based on the ideXlab platform.

  • acta and human zyxin harbour arp2 3 independent Actin Polymerization activity
    Nature Cell Biology, 2001
    Co-Authors: Julie Fradelizi, Daniel Louvard, Cécile Sykes, Evelyne Friederich, Vincent Noireaux, Julie Plastino, Bernadette Menichi, Roy M Golsteyn

    Abstract:

    The Actin cytoskeleton is a dynamic network that is composed of a variety of F-Actin structures. To understand how these structures are produced, we tested the capacity of proteins to direct Actin Polymerization in a bead assay in vitro and in a mitochondrial-targeting assay in cells. We found that human zyxin and the related protein ActA of Listeria monocytogenes can generate new Actin structures in a vasodilator-stimulated phosphoprotein-dependent (VASP) manner, but independently of the Arp2/3 complex. These results are consistent with the concept that there are multiple ActinPolymerization machines in cells. With these simple tests it is possible to probe the specific function of proteins or identify novel molecules that act upon cellular Actin Polymerization.

  • ActA and human zyxin harbour Arp2/3-independent ActinPolymerization activity
    Nature cell biology, 2001
    Co-Authors: Julie Fradelizi, Daniel Louvard, Cécile Sykes, Vincent Noireaux, Julie Plastino, Bernadette Menichi, Roy M Golsteyn, Evelyne Friederich

    Abstract:

    The Actin cytoskeleton is a dynamic network that is composed of a variety of F-Actin structures. To understand how these structures are produced, we tested the capacity of proteins to direct Actin Polymerization in a bead assay in vitro and in a mitochondrial-targeting assay in cells. We found that human zyxin and the related protein ActA of Listeria monocytogenes can generate new Actin structures in a vasodilator-stimulated phosphoprotein-dependent (VASP) manner, but independently of the Arp2/3 complex. These results are consistent with the concept that there are multiple ActinPolymerization machines in cells. With these simple tests it is possible to probe the specific function of proteins or identify novel molecules that act upon cellular Actin Polymerization.

Timothy J Mitchison – One of the best experts on this subject based on the ideXlab platform.

  • spatial control of Actin Polymerization during neutrophil chemotaxis
    Nature Cell Biology, 1999
    Co-Authors: Orion D Weiner, Matthew D Welch, Timothy J Mitchison, Guy Servant, John W Sedat, Henry R Bourne

    Abstract:

    Neutrophils respond to chemotactic stimuli by increasing the nucleation and Polymerization of Actin filaments, but the location and regulation of these processes are not well understood. Here, using a permeabilized-cell assay, we show that chemotactic stimuli cause neutrophils to organize many discrete sites of Actin Polymerization, the distribution of which is biased by external chemotactic gradients. Furthermore, the Arp2/3 complex, which can nucleate Actin Polymerization, dynamically redistributes to the region of living neutrophils that receives maximal chemotactic stimulation, and the least-extractable pool of the Arp2/3 complex co-localizes with sites of Actin Polymerization. Our observations indicate that chemoattractant-stimulated neutrophils may establish discrete foci of Actin Polymerization that are similar to those generated at the posterior surface of the intracellular bacterium Listeria monocytogenes. We propose that asymmetrical establishment and/or maintenance of sites of Actin Polymerization produces directional migration of neutrophils in response to chemotactic gradients.

  • Actin Polymerization is induced by arp 2 3 protein complex at the surface of listeria monocytogenes
    Nature, 1997
    Co-Authors: Matthew D Welch, Akihiro Iwamatsu, Timothy J Mitchison

    Abstract:

    The pathogenic bacterium Listeria monocytogenes is capable of directed movement within the cytoplasm of infected host cells. Propulsion is thought to be driven by Actin Polymerization at the bacterial cell surface1,2, and moving bacteria leave in their wake a tail of Actin filaments3. Determining the mechanism by which L. monocytogenes polymerizes Actin may aid the understanding of how Actin Polymerization is controlled in the cell. Actin assembly by L. monocytogenes requires the bacterial surface protein ActA4,5 and protein components present in host cell cytoplasm. We have purified an eight-polypeptide complex that possesses the properties of the host-cell Actin Polymerization factor. The pure complex is sufficient to initiate ActA-dependent Actin Polymerization at the surface of L. monocytogenes, and is required to mediate Actin tail formation and motility. Two subunits of this protein complex are Actin-related proteins (ARPs) belonging to the Arp2 and Arp3 subfamilies. The Arp3 subunit localizes to the surface of stationary bacteria and the tails of motile bacteria in tissue culture cells infected with L. monocytogenes; this is consistent with a role for the complex in promoting Actin assembly in vivo. The activity and subunit composition of the Arp2/3 complex suggests that it forms a template that nucleates Actin Polymerization.

  • Actin Polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes.
    Nature, 1997
    Co-Authors: Matthew D Welch, Akihiro Iwamatsu, Timothy J Mitchison

    Abstract:

    The pathogenic bacterium Listeria monocytogenes is capable of directed movement within the cytoplasm of infected host cells. Propulsion is thought to be driven by Actin Polymerization at the bacterial cell surface, and moving bacteria leave in their wake a tail of Actin filaments. Determining the mechanism by which L. monocytogenes polymerizes Actin may aid the understanding of how Actin Polymerization is controlled in the cell. Actin assembly by L. monocytogenes requires the bacterial surface protein ActA and protein components present in host cell cytoplasm. We have purified an eight-polypeptide complex that possesses the properties of the host-cell Actin Polymerization factor. The pure complex is sufficient to initiate ActA-dependent Actin Polymerization at the surface of L. monocytogenes, and is required to mediate Actin tail formation and motility. Two subunits of this protein complex are Actin-related proteins (ARPs) belonging to the Arp2 and Arp3 subfamilies. The Arp3 subunit localizes to the surface of stationary bacteria and the tails of motile bacteria in tissue culture cells infected with L. monocytogenes; this is consistent with a role for the complex in promoting Actin assembly in vivo. The activity and subunit composition of the Arp2/3 complex suggests that it forms a template that nucleates Actin Polymerization.