Deubiquitylating enzymes articles within Nature Cell Biology

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  • News & Views |

    There are many challenges in finding an effective, long-lasting and universal cure for the whole cohort of patients with Duchenne muscular dystrophy (DMD). The discovery of H19 lncRNA as a stabiliser of dystrophin may prove to be the missing link to the success of various rescue therapies proposed for treating DMD.

    • Morten Ritso
    •  & Michael A. Rudnicki

  • Article |

    The stability of the PTEN tumour suppressor protein is regulated by polyubiquitylation. Ma and colleagues identify USP13 as an enzyme reversing polyubiquitylation of PTEN, leading to PTEN stabilization and tumour suppression.

    • Jinsong Zhang
    • , Peijing Zhang
    •  & Li Ma

  • Article |

    The RAS-like GTPase RALB mediates cellular responses to nutrient availability or viral infection by engaging two distinct exocyst complex proteins: EXO84 to modulate autophagy and SEC5 to regulate innate immune signalling. Sablina and colleagues find that whereas ubiquitylation of RALB at K47 promotes its interaction with SEC5, the de-ubiquitylase USP33 switches RALB to the EXO84–beclin complex to promote autophagy during nutrient starvation.

    • Michal Simicek
    • , Sam Lievens
    •  & Anna A. Sablina

  • News & Views |

    The transforming growth factor (TGF-β) pathway is regulated by ubiquitin-mediated proteolysis at different levels. Two studies now identify deubiquitinating enzymes (DUBs) for the TGF-β type I receptor. Both ubiquitin-specific peptidase-4 (USP4) and -15 (USP15) extend the life of activated receptors against the negative pressure of receptor-ubiquitinating complexes, but through distinct modes of action.

    • Kamna Aggarwal
    •  & Joan Massagué

  • Letter |

    In the TGFβ pathway, receptor-activated SMADs (R-SMADs) associate with SMAD4 to regulate transcription. Piccolo and colleagues reveal that the deubiquitylase USP15 is required for TGFβ responses by reversing R-SMAD ubiquitylation and thereby promoting the retention of the SMAD complex at promoters.

    • Masafumi Inui
    • , Andrea Manfrin
    •  & Stefano Piccolo

  • Article |

    REST transcription factor is a master regulator of neural stem and progenitor cells, which is subjected to ubiquitylation-mediated proteasomal degradation during differentiation. In progenitor cells, degradation is inhibited by the action of the deubiquitylase enzyme HAUSP to prevent untimely neuronal differentiation.

    • Zhi Huang
    • , Qiulian Wu
    •  & Shideng Bao

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