Proteasome articles within Nature Cell Biology

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  • Article
    | Open Access

    Williams et al. report that, upon TORC1 inhibition in yeast, mRNA of the chaperone protein ADC17 is localized to cortical actin patches where its translation is enhanced upon stress.

    • Thomas David Williams
    • , Roberta Cacioppo
    •  & Adrien Rousseau

  • News & Views |

    Overload of proteasomal clearance triggers formation of a large protein inclusion called the aggresome, which shares similarities with protein aggregates seen in neurodegenerative diseases such as Huntington’s. A new study uncovers how centrosome and centriolar satellite components facilitate stepwise assembly of aggresomes.

    • Elisa Vitiello
    •  & Fanni Gergely

  • Letter |

    Lee et al. show that, after nitrogen starvation and genetic interference with the architecture of nuclear pore complexes, nucleoporins are degraded by autophagy, constituting a quality-control step at the nuclear envelope.

    • Chia-Wei Lee
    • , Florian Wilfling
    •  & Boris Pfander

  • News & Views |

    p53 mutations occur very frequently in human cancer. Besides abrogating the tumour suppressive functions of wild-type p53, many of those mutations also acquire oncogenic gain-of-function activities. Augmentation of proteasome activity is now reported as a common gain-of-function mechanism shared by different p53 mutants, which promotes cancer resistance to proteasome inhibitors.

    • Moshe Oren
    •  & Eran Kotler

  • News & Views |

    Clearing misfolded proteins from the cytoplasm is essential to maintain cellular homeostasis. Now, a parallel clearance system is described that uses the deubiquitylase USP19 to enable secretion of misfolded cytoplasmic proteins when conventional proteasomal degradation is compromised. Misfolding-associated protein secretion (MAPS) has important implications for protein quality control and prion-like transmission.

    • Norbert Volkmar
    • , Emma Fenech
    •  & John C. Christianson

  • News & Views |

    The control of proteasome-mediated protein degradation is thought to occur mainly at the level of polyubiquitylation of the substrate. However, the proteasome can also be regulated directly, as now demonstrated by a study in which DYRK2-mediated phosphorylation of the 19S subunit Rpt3 is found to increase proteasome activity.

    • Jon M. Huibregtse
    •  & Andreas Matouschek

  • Article |

    The mTORC1 complex promotes protein translation and cell growth, whereas mTORC2 promotes survival. The Tel2 and Tt1 proteins belong to both complexes. Bassermann and colleagues demonstrate that following growth-factor deprivation, casein kinase 2 mediates phosphorylation of Tel2 and Tt1, specifically in the mTORC1 complex, to target them for degradation by the SCFFbxo9 ubiquitin ligase. This mechanism inactivates mTORC1 and activates mTORC2 and Akt signalling to promote survival of multiple myeloma cells.

    • Vanesa Fernández-Sáiz
    • , Bianca-Sabrina Targosz
    •  & Florian Bassermann

  • Article |

    The SCF ubiquitin ligase subunit Fbxw7 is a tumour suppressor that is mutated in many cancers. Pagano and colleagues now show that in multiple myeloma, Fbxw7α instead functions as a pro-survival factor by activating the NF-κB pathway through the ubiquitin-mediated degradation of p100, an NF-κB pathway inhibitor.

    • Luca Busino
    • , Scott E. Millman
    •  & Michele Pagano

  • Article |

    Wallerian degeneration occurs in axons following cutting or crush injuries; however, the molecular mechanisms that regulate this process remain elusive. Araki and colleagues find that the ubiquitin ligase ZNRF1 promotes Wallerian degeneration by ubiquitylating AKT, which leads to increased GSK3B activity and subsequent inhibition of the tubulin-binding protein CRMP2.

    • Shuji Wakatsuki
    • , Fuminori Saitoh
    •  & Toshiyuki Araki

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