Proteasome articles within Nature

Featured

  • Article |

    Hyperosmotic stress leads to a phase separation of the proteasome, triggered by interactions between RAD23B and ubiquitylated proteins, which bring together p97 and proteasome-associated proteins into nuclear proteolytic foci.

    • Sayaka Yasuda
    • , Hikaru Tsuchiya
    •  & Yasushi Saeki

  • Article |

    Cryo-electron microscopy structures and dynamics of a substrate-engaged human 26S proteasome reveal in atomic detail three principal modes of coordinated ATP hydrolysis that regulate different steps in the degradation of a ubiquitylated protein.

    • Yuanchen Dong
    • , Shuwen Zhang
    •  & Youdong Mao

  • Article |

    Proteasome abundance is crucial for cell survival, but how cells maintain adequate amounts of proteasome is unclear; an analysis in yeast identifies TORC1 and Mpk1 as central components of a pathway regulating proteasome homeostasis through the coordinated regulation of regulatory particle assembly chaperones and proteasome subunits—this pathway is evolutionarily conserved with mTOR and ERK5 regulating proteasome abundance in mammals.

    • Adrien Rousseau
    •  & Anne Bertolotti

  • Letter |

    The proteasome-associated enzyme USP14 regulates protein degradation by removing ubiquitin from proteins; here it is shown that USP14 removes ubiquitin chains from in vitro generated cyclin B conjugates en bloc and within milliseconds, before the proteasome has a chance to initiate degradation, and proceeds until a single chain remains.

    • Byung-Hoon Lee
    • , Ying Lu
    •  & Daniel Finley

  • Letter |

    Human embryonic stem cells (hESCs) are shown to have high 26S/30S proteasome activity owing to increased expression of the 19S proteasome subunit PSMD11; FOXO4 regulates proteasome activity in hESCs by modulating PSMD11 expression, and the high proteasome activity decreases after induced differentiation.

    • David Vilchez
    • , Leah Boyer
    •  & Andrew Dillin

  • Article |

    This study shows that nematodes without a germ line re-allocate resources to the soma, resulting in elevated proteasome activity, clearance of damaged proteins and increased longevity; this activity is associated with the increased expression of rpn-6 mediated by the transcription factor DAF-16.

    • David Vilchez
    • , Ianessa Morantte
    •  & Andrew Dillin

  • News & Views |

    Correctly dismantling a structure can be as challenging as assembling it. The architecture of the yeast proteasome reveals this enzyme's intricate machinery for protein degradation. See Article p.186

    • Geng Tian
    •  & Daniel Finley

  • Article |

    Regulated proteolysis by ATP-dependent proteases have a crucial role in protein quality control in cells. The Clp/Hsp100 proteins of the AAA+ superfamily of ATP-dependent chaperones unfold and translocate proteins into the proteolytic chamber of protease complexes. ClpC requires the adaptor protein MecA for activation and substrate targetting to the ClpCP protease complex. Here, a structural and biochemical analysis is presented of the MecA–ClpC complex revealing organizational principles and providing mechanistic insights into this complex molecular machine.

    • Feng Wang
    • , Ziqing Mei
    •  & Yigong Shi

  • Letter |

    The proteasome is a multi-protein complex that enzymatically degrades proteins. Proteolysis occurs in a barrel-shaped 20S core particle comprising three interconnected cavities, including a pair of antechambers in which substrates are held before degradation. These authors demonstrate that substrates interact actively with the antechamber walls and that the environment in this compartment is optimized to maintain the substrates in unfolded states so as to be accessible for hydrolysis.

    • Amy M. Ruschak
    • , Tomasz L. Religa
    •  & Lewis E. Kay

  • Article |

    In the ubiquitin–proteasome system, substrates destined for destruction are modified with ubiquitin chains and then degraded by the proteasome. These authors reveal a regulatory mechanism in which proteasomal activity is modulated by the length of ubiquitin chains in human cells. They find that deubiquitinating enzyme USP14 can inhibit the degradation of ubiquitin-conjugated substrates by trimming ubiquitin chains, and that stimulation of proteasome activity may be used to reduce the levels of toxic proteins in cells.

    • Byung-Hoon Lee
    • , Min Jae Lee
    •  & Daniel Finley

  • Article |

    Although Archaea encode proteasomes highly related to those of eukaryotes, archaeal ubiquitin-like proteins are less conserved and not known to function in protein conjugation, complicating our understanding of the origins of ubiquitination. Two small archaeal modifier proteins, SAMP1 and SAMP2, structurally similar to ubiquitin, are now reported to form protein conjugates in the archaeon Haloferax volcanii.

    • Matthew A. Humbard
    • , Hugo V. Miranda
    •  & Julie A. Maupin-Furlow

Browse broader subjects

Browse Proteasome across other nature.com journals