Volume 18 Issue 2, February 2017

Volume 18 Issue 2

'Variations on histones' by Vicky Summersby, inspired by the Review on p115.

Research Highlights

Reviews

  • Review Article |

    Nuclear pore complexes (NPCs) are large protein assemblies that form channels in the nuclear envelope and constitute major routes for nucleocytoplasmic communication. Insights into the complex structure of NPCs provide the basis for understanding their functions and reveal how the dysfunction of their structural components, nucleoporins, contributes to human disease.

    • Martin Beck
    •  & Ed Hurt
  • Review Article |

    In addition to acetylation, eight types of structurally and functionally different short-chain acylations have recently been identified as important histone Lys modifications: propionylation, butyrylation, 2-hydroxyisobutyrylation, succinylation, malonylation, glutarylation, crotonylation and β-hydroxybutyrylation. These modifications are regulated by enzymatic and metabolic mechanisms and have physiological functions, which include signal-dependent gene activation and metabolic stress.

    • Benjamin R. Sabari
    • , Di Zhang
    • , C. David Allis
    •  & Yingming Zhao
  • Review Article |

    Histone variants are typically incorporated into chromatin independently of DNA replication and modify chromatin properties. Recent studies have elucidated how particular histone variants are substrates of histone chaperones, chromatin remodellers and histone-modifying enzymes, thereby modifying DNA replication and repair, transcription and chromatin packaging.

    • Paul B. Talbert
    •  & Steven Henikoff

Perspectives

    Timeline

  • Timeline |

    Several years after the characterization of the role of receptor-interacting serine/threonine protein kinase 1 (RIPK1) in cell survival, inflammation and disease, RIPK1 was implicated in the regulation of a newly identified type of cell death known as necroptosis. This Timeline article describes the discoveries that shed light on the roles of RIPK1, RIPK3, mixed-lineage kinase domain-like protein (MLKL) and other regulators of necroptosis in controlling cell fate.

    • Ricardo Weinlich
    • , Andrew Oberst
    • , Helen M. Beere
    •  & Douglas R. Green