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Showing 1–8 of 8 results
Advanced filters: Author: Vivian Pogenberg Clear advanced filters

  • During infection, the Legionella effector Lem3 removes a phosphocholine moiety from the human protein Rab1. Here, the authors present the crystal structure of the stabilised Lem3:Rab1b complex, revealing the catalytic mechanism and substrate recognition of PPM phosphatases shaped Lem3.

    • Marietta S. Kaspers
    • Vivian Pogenberg
    • Aymelt Itzen
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • The microphthalmia-associated transcription factor MITF is a lineage-survival oncogene that plays a crucial role in melanocyte development and melanoma. Here, the authors reveal that MITF has a very long chromatin-bound half-life, and that MITF target selectivity is regulated by K206 acetylation, a residue linked to Waardenburg syndrome.

    • Pakavarin Louphrasitthiphol
    • Alessia Loffreda
    • Colin R. Goding
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • The ER chaperone BiP is critical for the unfolded protein response and tightly regulated through reversible AMPylation by FICD, but the structural basis is unknown. Here the authors use thiol-reactive nucleotide derivatives to stabilize the transient FICD:BiP complex and determine its crystal structure.

    • Joel Fauser
    • Burak Gulen
    • Aymelt Itzen
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • Many bacterial pathogens release effector enzymes belonging to the large Fic family, which modify host targets with nucleotide monophosphates. Now, recombinantly produced Fic enzymes have been equipped with synthetic thiol-reactive nucleotide derivatives to make covalent binary probes. The reaction of modified Fic enzymes with their targets permits covalent substrate capture and the structural determination of low-affinity ternary enzyme–nucleotide–substrate complexes.

    • Burak Gulen
    • Marie Rosselin
    • Aymelt Itzen
    Research
    Nature Chemistry
    Volume: 12, P: 732-739

  • Oct4 cannot be replaced by other members of the same family of transcription factors to induce reprogramming. By comparing the structure of the POU family domain of Oct4 complexed to DNA with that of others, Schöler and colleagues identify an α-helix that is exposed on the surface of Oct4 and provides an interaction platform to recruit epigenetic modifiers to Oct4 targets. Mutations abolishing this helix suppress the reprogramming properties of Oct4.

    • Daniel Esch
    • Juha Vahokoski
    • Hans R. Schöler
    Research
    Nature Cell Biology
    Volume: 15, P: 295-301