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Showing 1–12 of 12 results
Advanced filters: Author: Frauke Melchior Clear advanced filters

  • A protein called small ubiquitin-related modifier (SUMO) can be coupled to other proteins to control their function. This SUMOylation has been implicated in the regulation of a host of cellular processes, and is essential for the health, and even the survival, of most organisms.

    • Erik Meulmeester
    • Frauke Melchior
    Comments & Opinion
    Nature
    Volume: 452, P: 709-711

  • Cortical actin is implicated in cell shape regulation during mitosis. Melchior and colleagues reveal that SCFFbxw5-mediated ubiquitylation and degradation of the actin remodeller Eps8 is required for timely cell rounding and progression into metaphase, whereas the capping activity of Eps8 is needed for mitotic exit.

    • Achim Werner
    • Andrea Disanza
    • Frauke Melchior
    Research
    Nature Cell Biology
    Volume: 15, P: 179-188

  • SUMO (small ubiquitin-related modifier) is a reversible post-translational protein modifier that causes molecular alterations in sumoylated target proteins, leading to changes in localization, activity and stability. In the past 10 years, mechanisms and principles that govern sumoylation have been elucidated.

    • Ruth Geiss-Friedlander
    • Frauke Melchior
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 8, P: 947-956

  • FAT10 is an ubiquitin-like modifier that targets proteins to proteasomal degradation. Here, the authors show that FAT10 also regulates SUMO activation in vitro and in cells, providing evidence for functional crosstalk between two ubiquitin-like modifiers.

    • Annette Aichem
    • Carolin Sailer
    • Marcus Groettrup
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-17

  • The bicyclic disulfide–containing compound thiolutin has broad antimicrobial activity and targets the essential proteasomal deubiquitinase Rpn11 and other metalloproteases, leading to inhibition of enzymatic activity through a mechanism involving zinc chelation.

    • Linda Lauinger
    • Jing Li
    • Axel Diernfellner
    Research
    Nature Chemical Biology
    Volume: 13, P: 709-714

  • Covalent modification of the oncogene product Mdm2 by the ubiquitin-related protein SUMO1 protects it from ubiquitination and enhances its E3 ligase activity towards p53 in vitro. Disappearance of SUMO-modified Mdm2, which is observed upon radiation, may thus be a prerequisite for DNA-damage-induced accumulation of p53.

    • Frauke Melchior
    • Ludger Hengst
    News & Views
    Nature Cell Biology
    Volume: 2, P: E161-E163

  • SUMOylation is a dynamic protein post-translational modification that regulates many eukaryotic proteins. Now a methodology using commercially available monoclonal antibodies coupled to MS analysis leads to the enrichment and identification of endogenous targets for SUMO1 and for SUMO2/3 in HeLa cells and mouse liver. This protocol can be adapted for other tissues and organs.

    • Janina Becker
    • Sina V Barysch
    • Frauke Melchior
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 525-531