Cytoskeleton

The cytoskeleton is a network of filamentous and tubular protein structures that support cell shape, intracellular compartmentalisation and trafficking, cell migration and cell division. The key constituents of the cytoskeleton are actin filaments, microtubules and intermediate filaments.

Latest Research and Reviews

News and Comment

  • News and Views |

    Assembly of the mitotic spindle requires timely separation of the centrosomes. Their movement apart is driven by the plus-end-directed kinesin Eg5. A new study demonstrates that the kinesin KIFC3 provides an opposing microtubule-based cohesive force that modulates centrosome separation and ensures accurate chromosome segregation.

    • Ciaran G. Morrison
    Nature Cell Biology 21, 1057-1059
  • News and Views |

    Researchers have sought to understand the function and regulation of the motor protein dynein since its discovery more than 50 years ago1. Dynein-2 is one of the motors that move the intraflagellar transport (IFT) trains ― large protein complexes that are needed for the assembly and function of eukaryotic cilia and flagella. Toropova et al. report the single-particle cryo-EM structure of the human dynein-2 complex2, which unexpectedly reveals two different conformations of the motor subunit tails. One tail forms a zigzag that matches the periodicity of the IFT trains, which reinforces the auto-inhibition of dynein motor activity and the binding of multiple dynein-2 complexes along the train during anterograde transport.

    • Susan K. Dutcher
  • Research Highlights |

    In zebrafish, pioneer axons of the dorsal root ganglia require the release of synaptic-like vesicles to enter the spinal cord, suggesting that synaptic vesicles have a role in circuit formation ahead of synaptogenesis.

    • Katharine H. Wrighton
  • News and Views |

    The ‘tubulin code’, a set of post-translational modifications to the microtubule cytoskeleton that include removal of the C-terminal Tyr of α-tubulin, regulates the biological function of the polymer. Three studies now report structures of VASH1–SVBP and VASH2–SVBP heterodimers and provide insights into how these proteases recognize and cleave the terminal Tyr of α-tubulin.

    • Kevin C. Slep