Sumoylated proteins

Sumoylated proteins are proteins modified post-translationally with small (~12 kDa) ubiquitin-like proteins called SUMOs. Sumoylated proteins are involved in various cellular processes, such as nucleocytoplasmic transport, transcriptional regulation, apoptosis and regulation of cell cycle proteins.

Latest Research and Reviews

  • Research | | open

    The NLRP3 inflammasome is an important component of inflammatory responses, but how it is negatively regulated is still unclear. Here the authors show that post-translational modification of NLRP3 by sumoylation suppresses inflammasome activity, and that desumoylation of NLRP3 by the SENP6 and SENP7 proteases promotes NLRP3 activation.

    • Rachael Barry
    • , Sidonie Wicky John
    • , Gianmaria Liccardi
    • , Tencho Tenev
    • , Isabel Jaco
    • , Chih-Hong Chen
    • , Justin Choi
    • , Paulina Kasperkiewicz
    • , Teresa Fernandes-Alnemri
    • , Emad Alnemri
    • , Marcin Drag
    • , Yuan Chen
    •  & Pascal Meier
  • Research | | open

    Ubiquitylation and SUMOylation are two important related post-translational modifications. Here the authors present an approach for the simultaneous identification and quantification of protein-wide SUMO and ubiquitin sites from a single sample, uncovering widespread crosstalk between the two modifications.

    • Frédéric Lamoliatte
    • , Francis P. McManus
    • , Ghizlane Maarifi
    • , Mounira K. Chelbi-Alix
    •  & Pierre Thibault
  • Research | | open

    Gephyrin is a cytoplasmic scaffolding protein that selectively forms postsynaptic scaffolds at GABAergic and glycinergic synapses. Here the authors characterize regulatory mechanisms determining gephyrin scaffolding and GABAA receptor synaptic transmission that involve acetylation, SUMOylation and phosphorylation.

    • Himanish Ghosh
    • , Luca Auguadri
    • , Sereina Battaglia
    • , Zahra Simone Thirouin
    • , Khaled Zemoura
    • , Simon Messner
    • , Mario A. Acuña
    • , Hendrik Wildner
    • , Gonzalo E. Yévenes
    • , Andrea Dieter
    • , Hiroshi Kawasaki
    • , Michael O. Hottiger
    • , Hanns Ulrich Zeilhofer
    • , Jean-Marc Fritschy
    •  & Shiva K. Tyagarajan
  • Research |

    Analysis of the available human small ubiquitin-like modifier (SUMO) proteomics data provided evidence for the sumoylation of thousands of proteins and residues, and clustered the sumoylated proteins into functional networks. Sumoylation is a frequent modification, occurring mostly on nuclear proteins, with functions including transcription, mRNA processing and the DNA-damage response.

    • Ivo A. Hendriks
    •  & Alfred C. O. Vertegaal
  • Protocols |

    This is a mass spectrometry–based biochemical assay to identify the site of SUMOylation on recombinant proteins from in vitro reactions. SUMO site identification is achieved using mutant SUMOs that release five amino acid remnants upon tryptic cleavage.

    • Francis P McManus
    • , Christine Desroches Altamirano
    •  & Pierre Thibault
    Nature Protocols 11, 387-397