Actin articles within Nature

Featured

  • Article |

    Using micropipette aspiration on donated human embryos, cell surface tensions during compaction were mapped, indicating a role for defective cell contractility in poor quality embryos.

    • Julie Firmin
    • , Nicolas Ecker
    •  & Jean-Léon Maître

  • Article |

    Functional mutations identified in patients with androgen insensitivity syndrome, in the formin and actin nucleator DAAM2, uncover signal-regulated nuclear actin assembly at a steroid hormone receptor necessary for transcription.

    • Julian Knerr
    • , Ralf Werner
    •  & Nadine C. Hornig

  • Article |

    Mechanical load-sharing enables the long-range cooperative uptake of apoptotic cells by multiple epithelial cells; and clearance of these apoptotic cells facilitates error correction, which is necessary for developmental robustness and survival of the embryo.

    • Esteban Hoijman
    • , Hanna-Maria Häkkinen
    •  & Verena Ruprecht

  • Article |

    Glycolysis in normal epithelial cells responds to microenvironmental mechanics via the modulation of actin bundles that sequester the phosphofructokinase-targeting ubiquitin ligase TRIM21, a process superseded by persistent actin bundles in cancer cells.

    • Jin Suk Park
    • , Christoph J. Burckhardt
    •  & Gaudenz Danuser

  • Article |

    The cryo-EM structure of the γ-tubulin ring complex (γ-TuRC) from Xenopus laevis provides insights into the molecular organization of the complex, and shows that actin is a structural component that is functionally relevant to microtubule nucleation.

    • Peng Liu
    • , Erik Zupa
    •  & Elmar Schiebel

  • Letter |

    Electron cryomicroscopy reveals the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å; the stabilizing interactions and the effects of disease-causing mutants are also investigated.

    • Julian von der Ecken
    • , Mirco Müller
    •  & Stefan Raunser

  • Letter |

    A new protein, Arpin, is identified that inhibits the Arp2/3 complex and controls cell migration by decreasing cell speed and the directional persistence of migration; this inhibitory circuit is under the control of the small GTPase Rac1, and Arpin depletion causes faster lamellipodia protrusion and increased cell migration.

    • Irene Dang
    • , Roman Gorelik
    •  & Alexis Gautreau

  • News & Views |

    Recognition of aberrant cell death is a crucial function of the immune system. It seems that one way in which immune cells identify damage is by sensing actin, an abundant intracellular protein.

    • Gordon D. Brown

  • Article |

    In cells, WAVE protein, a central regulator of actin dynamics during cell motility, is constitutively incorporated into WAVE regulatory complex (WRC), is normally present in an inactive state and can be activated by a number of inputs. These authors present the structure and mechanistic analysis of WRC. The combined data reveal how the WAVE protein is inhibited within the WRC complex and provide mechanisms for WRC activation at the plasma membrane.

    • Zhucheng Chen
    • , Dominika Borek
    •  & Michael K. Rosen

  • Letter |

    The formation of filamentous F-actin, through polymerization of globular G-actin, is essential for processes such as cell motility and muscle contraction. These authors report the structure of F-actin as visualized by electron cryomicroscopy, and build a complete atomic model of F-actin. This new structure will improve our understanding of the mechanism of actin assembly and disassembly.

    • Takashi Fujii
    • , Atsuko H. Iwane
    •  & Keiichi Namba

  • News & Views |

    The front of motile cells is thought to be pushed out by branched filaments of actin protein abutting the cell membrane. New work challenges this textbook view, showing that actin branches grow away from, or obliquely to, a surface.

    • Cécile Sykes
    •  & Julie Plastino

  • Letter |

    Semaphorins and their receptors, plexins, relay guidance information to neurons during development and regulate actin dynamics through an unknown mechanism. Recently, proteins of the Mical family of enzymes have been found to associate with plexins; here, Mical is reported to directly link semaphorins and their plexin receptors to the precise control of actin filament dynamics.

    • Ruei-Jiun Hung
    • , Umar Yazdani
    •  & Jonathan R. Terman

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