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Actin, a Central Player in Cell Shape and Movement
Comparisons of quantitative measurements of reactions in live cells with computer simulations of mathematical models will help generate meaningful insights and present a summary of the key questions in the field.
Effects of cytochalasin and phalloidin on actin
  • J. Cooper
  • Biology, Medicine
    The Journal of cell biology
  • 1 October 1987
A review briefly summarizes older studies and concentrates on recent studies on the mechanisms of action of cytochalasin and phalloidin.
Antagonism between Ena/VASP Proteins and Actin Filament Capping Regulates Fibroblast Motility
It is concluded that Ena/VASP regulates cell motility by controlling the geometry of actin filament networks within lamellipodia.
Cortactin promotes and stabilizes Arp2/3-induced actin filament network formation
These results support a model in which cortactin modulates actin filament dendritic nucleation by two mechanisms, (1) direct activation of Arp2/3 complex and (2) stabilization of newly generated filament branch points.
The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast
During mitosis in Saccharomyces cerevisiae, the mitotic spindle moves into the mother–bud neck via dynein-dependent sliding of cytoplasmic microtubules along the cortex of the bud via Dynein/dynactin pathway, and Pac1 plays a key role in this process.
Microtubule Interactions with the Cell Cortex Causing Nuclear Movements in Saccharomyces cerevisiae
Video analysis of GFP-labeled microtubules in wild-type cells and in EB1 and Arp1 mutants, which are defective in the first and second steps, finds that nuclear movement to the neck is largely mediated by the capture of microtubule ends at one cortical region at the incipient bud site or bud tip, followed by micro tubule depolymerization.
Cortactin Localization to Sites of Actin Assembly in Lamellipodia Requires Interactions with F-Actin and the Arp2/3 Complex
Cortactin is an actin-binding protein that is enriched within the lamellipodia of motile cells and in neuronal growth cones. Here, we report that cortactin is localized with the actin-related protein
Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin
The dynactin complex visualized by deepetch electron microscopy appears as a short filament 37-nm in length, which resembles F-actin, plus a thinner, laterally oriented filament that terminates in two globular heads, suggesting that the dynactIn polypeptide comprises at least part of the sidearm structure.
Actin and actin-binding proteins. A critical evaluation of mechanisms and functions.
The present study focuses on the development of binding proteins that bind to the sides of ACTIN FILAMENTS and their applications in the context of nanofiltration.
The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling
This review focuses on the recent convergence of cell biology and immunology studies to explain the role of the actin cytoskeleton in creating the molecular basis for immunological synapse formation and T cell signaling.