Protein quality control articles within Nature

Featured

  • Article |

    Structural studies of the dimerization quality control E3 ubiquitin ligase SCF–FBXL17 indicate that its selectivity for aberrant complex formation is based on recognizing both shape and complementarity of interacting domains.

    • Elijah L. Mena
    • , Predrag Jevtić
    •  & Michael Rape

  • Article |

    During nutrient stress, ribosomal protein abundance is regulated primarily by translational and non-autophagic degradative mechanisms, but ribosome density per cell is largely maintained by reductions in cell volume and rates of cell division.

    • Heeseon An
    • , Alban Ordureau
    •  & J. Wade Harper

  • Article |

    In Saccharomyces cerevisiae, Ubx2 promotes clearing trapped precursor proteins from the channel of the translocase of the outer membrane, in a translocation-associated degradation pathway that maintains the protein import capacity of mitochondria.

    • Christoph U. Mårtensson
    • , Chantal Priesnitz
    •  & Thomas Becker

  • 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 |

    A protein degradation pathway is found at the inner nuclear membrane that is distinct from, but complementary to, endoplasmic-reticulum-associated protein degradation, and which is mediated by the Asi protein complex; a genome-wide library screening of yeast identifies more than 20 substrates of this pathway, which is shown to target mislocalized integral membrane proteins for degradation.

    • Anton Khmelinskii
    • , Ewa Blaszczak
    •  & Michael Knop

  • Letter |

    The translation of messenger RNA that lacks stop codons results in the production of aberrant proteins, which may have harmful effects on the cell. It is unclear how eukaryotic cells eliminate these 'non-stop' proteins. Here it is shown that, in Saccharomyces cerevisiae, an E3 ubiquitin ligase called Ltn1 acts in the quality-control pathway. It associates with ribosomes and marks non-stop proteins with ubiquitin, which targets the proteins for degradation.

    • Mario H. Bengtson
    •  & Claudio A. P. Joazeiro

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