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Showing 1–9 of 9 results
Advanced filters: Author: Dorothee Dormann Clear advanced filters

  • Here, the authors present the crystal structure of Transportin 3 (TNPO3) bound to its cargo cold-inducible RNA-binding protein (CIRBP), uncovering a distinct mechanism of protein nuclear import regulation independent of phosphorylation.

    • Qishun Zhou
    • Theo Sagmeister
    • Tobias Madl
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • TDP-43 aggregates are a hallmark of neurodegeneration. Wagner et al. show that SUMOylation/ubiquitylation of TDP-43, mediated by its recruitment to the promyelocytic leukemia protein nuclear bodies, prevents its aggregation under proteotoxic stresses.

    • Kristina Wagner
    • Jan Keiten-Schmitz
    • Stefan Müller
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 21, P: 1408-1419

  • Repeat-associated non-AUG (RAN) translation generates toxic repeat proteins from pathological repeat expansions found in certain neurodegenerative disorders, including amyotrophic lateral sclerosis and frontotemporal dementia. How to suppress RAN translation has so far been unknown. A new study now reports a selective regulator of RAN translation identified in a genetic screen in yeast.

    • Saskia Hutten
    • Dorothee Dormann
    News & Views
    Nature Neuroscience
    Volume: 22, P: 1379-1380

  • Processing bodies (P-bodies) are non-membrane-bound protein/RNA granules in the cytosol. Here the authors combine bioinformatics, NMR and cell based assays and find that lysine is enriched in the disordered regions of P-body-associated proteins and show that lysine-rich polypeptides form highly dynamic lysine/RNA-coacervates and lysine acetylation reverses liquid-liquid phase separation.

    • Tina Ukmar-Godec
    • Saskia Hutten
    • Markus Zweckstetter
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-15

  • Biological clocks can be used to evaluate the age of a cell or organisms. This Perspective proposes the concept of an intrinsically disordered protein (IDP) clock, whereby the aggregation state of an IDP encodes for a biological ageing signature.

    • Dorothee Dormann
    • Edward Anton Lemke
    Reviews
    Nature Cell Biology
    Volume: 26, P: 851-858

  • The realization that the cell is abundantly compartmentalized into biomolecular condensates has opened new opportunities for understanding the physics and chemistry underlying many cellular processes1, fundamentally changing the study of biology2. The term biomolecular condensate refers to non-stoichiometric assemblies that are composed of multiple types of macromolecules in cells, occur through phase transitions, and can be investigated by using concepts from soft matter physics3. As such, they are intimately related to aqueous two-phase systems4 and water-in-water emulsions5. Condensates possess tunable emergent properties such as interfaces, interfacial tension, viscoelasticity, network structure, dielectric permittivity, and sometimes interphase pH gradients and electric potentials6–14. They can form spontaneously in response to specific cellular conditions or to active processes, and cells appear to have mechanisms to control their size and location15–17. Importantly, in contrast to membrane-enclosed organelles such as mitochondria or peroxisomes, condensates do not require the presence of a surrounding membrane.

    • Simon Alberti
    • Paolo Arosio
    • Tanja Mittag
    Comments & OpinionOpen Access
    Nature Communications
    Volume: 16, P: 1-14