Intracellular signalling peptides and proteins articles within Nature

Featured

  • Article
    | Open Access

    Structural insights into the poly-ADP-ribosyltransferase tankyrase reveal its filamentous architecture and illustrate how assembly controls catalytic and non-catalytic functions.

    • Nisha Pillay
    • , Laura Mariotti
    •  & Sebastian Guettler

  • Letter |

    Cell death by apoptosis is crucial for tissue development and function, and occurs throughout life. Apoptotic cells must be cleared by phagocytic cells, but the mechanisms that regulate cell clearance in vivo remain unclear. Here, a conserved engulfment protein, ELMO1, is shown to be required for the phagocytic clearance of apoptotic germ cells by Sertoli cells in mouse testes. The findings make a compelling case for the relationship between engulfment and tissue homeostasis in vivo.

    • Michael R. Elliott
    • , Shuqiu Zheng
    •  & Kodi S. Ravichandran

  • Letter |

    Before mating, a yeast cell must detect a partner cell that is close enough and expresses sufficiently large amounts of a sex pheromone. The mating decision is an all-or-none, switch-like response to pheromone concentration. It is now shown that this decision involves the competition of one kinase and one phosphatase enzyme for multiple phosphorylation sites on a 'scaffold' protein. The results should prompt a re-evaluation of the role of related signalling molecules that have been implicated in cancer.

    • Mohan K. Malleshaiah
    • , Vahid Shahrezaei
    •  & Stephen W. Michnick

  • Letter |

    Fibrillar deposits of tau protein (neurofibrillary tangles) are thought to cause neuronal death in patients with Alzheimer's disease, and tau-related frontotemporal dementia. Here, however, the opposite has been found: the activation of executioner caspase enzymes occurs first, preceding tangle formation by hours to days. Tangle-bearing neurons seem to be long-lived, indicating that tangles might be 'off pathway' to acute neuronal death.

    • Alix de Calignon
    • , Leora M. Fox
    •  & Bradley T. Hyman

  • Letter |

    Ca2+ channels and calmodulin (CaM) are two prominent hubs of biological signalling networks, affecting functions such as cardiac excitability and gene transcription. The prevailing view has been that the ultrastrong affinity of channels for the Ca2+-free form of calmodulin (apoCaM) ensures their saturation with CaM and yields a form of concentration independence between Ca2+ channels and CaM. Here, however, significant exceptions to this autonomy are shown to exist.

    • Xiaodong Liu
    • , Philemon S. Yang
    •  & David T. Yue

Browse broader subjects

Browse Intracellular signalling peptides and proteins across other nature.com journals