Protein quality control

Protein quality control is the mechanism by which a cell monitors proteins to ensure that they are appropriately folded. Protein quality control takes place predominantly in the endoplasmic reticulum, and can redeliver damaged proteins to the biosynthetic machinery or, failing correction, can deliver them to the ubiquitin–proteasome system for degradation.

Latest Research and Reviews

News and Comment

  • News & Views |

    Mitochondrial-derived vesicles (MDVs) transfer mitochondrial content to lysosomes and peroxisomes. A study now reveals that MDVs deliver β-barrel proteins and fully assembled mitochondrial complexes for lysosomal degradation, establishing an important role for MDVs in mitochondrial protein quality control.

    • Dominic Winter
    •  & Thomas Becker
    Nature Cell Biology 23, 1216-1217
  • News & Views |

    Neuronal mitochondria perturbation elicits a mitochondrial unfolded protein response (UPRmt) in peripheral tissues cell non-autonomously, dependent on the Wnt signalling pathway. A study now reveals that a Wnt-mediated increase in maternally inherited mitochondria DNA is responsible for transgenerational UPRmt induced by neuronal mitochondria perturbation.

    • Mooncheol Park
    •  & Meng C. Wang
    Nature Cell Biology 23, 820-821
  • News & Views |

    The ‘N-end rule’ correlates the identity of the N-terminal residue of a protein to its in vivo half-life. A study has now shown that an N-terminal glycine can serve as a potent degradation signal, which reveals a novel branch of N terminus–dependent protein degradation.

    • Mohamed Eldeeb
    • , Mansoore Esmaili
    •  & Richard Fahlman
  • News & Views |

    In the ribosome-associated quality control (RQC) pathway, stalled ribosomes are ubiquitinated and dissociated into subunits. The nascent protein chain associated with the 60S ribosomal subunit is ubiquitinated by the E3 ligase Listerin (Ltn1) and is released from tRNA by ANKZF1 (Vms1) for proteasomal degradation. Shao and colleagues now report that ANKZF1 (Vms1)-cleaved tRNAs are recycled via a two-step process that requires the removal of a terminal 2′,3′-cyclic phosphate and the addition of CCA by TRNT1.

    • Toshifumi Inada