Ubiquitins are small proteins (~8 kDa) that post-translationally modify proteins on lysine residues through formation of an isopeptide bond between the carboxylic acid group of the ubiquitin's glycine and the epsilon amino group of the substrate's lysine.

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News and Comment

  • Research Highlights |

    Recently, a Legionella pneumophila effector protein was shown to have an unprecedented ATP-independent ubiquitin ligase activity that couples phosphoribosylated ubiquitin (PR-Ub) to serine residues of host proteins. A new study published in Cell Research by Qiu et al. reveals that another Legionella effector protein, SidJ, catalyzes deubiquitination of PR-Ub by cleavage of the substrate-linked phosphodiester bond.

    • Judith A Ronau
    •  & Mark Hochstrasser
    Cell Research 27, 845-846
  • News |

    A “simple but a bit crazy idea” to tag ubiquitin and practice multilingual, multidisciplinary proteomics.

    • Vivien Marx
    Nature Methods 14, 459
  • Research Highlights |

    Ubiquitin chains assembled via the N-terminal methionine (Met1 or linear ubiquitin), conjugated by the linear ubiquitin chain assembly complex (LUBAC), participate in NF-κΒ-dependent inflammatory signaling and immune responses. A recent report in Cell finds that OTULIN, a deubiquitinase that selectively cleaves Met1-linked ubiquitin chains, is essential for restraining inflammation in vivo.

    • Berthe Katrine Fiil
    •  & Mads Gyrd-Hansen
    Cell Research 26, 1176-1177