Ubiquitins

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.

Latest Research and Reviews

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