Ubiquitin ligases

Ubiquitin ligases are enzymes involved in the ligation step of ubiquitylation. Ubiquitin ligases bind the substrate protein and catalyse the transfer of ubiquitin from the cysteine of ubiquitin-conjugating enzymes to a lysine residue on the substrate protein.

Latest Research and Reviews

News and Comment

  • News and Views |

    Piwi proteins are aberrantly induced in human tumours, but their function in cancer has been poorly understood. A study now shows that in the absence of piRNA loading, human PIWIL1 promotes pancreatic cancer metastasis by acting as a co-activator of the anaphase-promoting complex/cyclosome (APC/C) to degrade the cell-adhesion protein Pinin.

    • Fan Yao
    •  & Li Ma
    Nature Cell Biology 22, 359-360
  • News and Views |

    The ‘N-end rule’ correlates the identity of the N-terminal residue of a protein to its in vivo half-life. A study has now shown that an N-terminal glycine can serve as a potent degradation signal, which reveals a novel branch of N terminus–dependent protein degradation.

    • Mohamed Eldeeb
    • , Mansoore Esmaili
    •  & Richard Fahlman
  • News and Views |

    Loss-of-function mutations in the ubiquitin ligase Parkin are a cause of Parkinson’s disease. Parkin also has tumour-suppressor activity, although how Parkin prevents cancer is unclear. Unexpectedly, Parkin is found to suppress cancer by inhibiting an inflammatory type of cell death called necroptosis.

    • Kai Cao
    •  & Stephen W. G. Tait
    Nature Cell Biology 21, 915-916
  • Research Highlights |

    The ABC family member ABCF1 has E2 ubiquitin-conjugating activity and regulates Toll-like receptor signalling and macrophage polarization to protect against lethal septic shock.

    • Lucy Bird