Proteolysis is the enzymatic process by which proteins are degraded into their component polypeptide or amino acid parts. This generally occurs through protease-mediated hydrolysis of peptide bonds, but can also occur through non-enzymatic methods such as by action of mineral acids and heat.


Latest Research and Reviews

  • Research |

    Olfactory food perception is known to extend lifespan in C. elegans. Here the authors demonstrate food-odour-dependent brain-to-gut communication that extends lifespan in worms. Food odour downregulates tir-1 mRNA in AWC neurons, in a manner dependent on the miRNA miR-71, which triggers downstream effects in the gut, due to neuropeptide secretion, that promote proteostasis and longevity.

    • Fabian Finger
    • , Franziska Ottens
    • , Alexander Springhorn
    • , Tanja Drexel
    • , Lucie Proksch
    • , Sophia Metz
    • , Luisa Cochella
    •  & Thorsten Hoppe
  • Research | | open

    Ubiquitination may control protein stability or function. Here the authors show that an ubiquitination enzyme, Hectd3, ubiquitinates Stat3 and Malt1 to modulate their function but not degradation in T cells, and thereby promoting the differentiation of pathogenic Th17 cells and susceptibility to a mouse model of multiple sclerosis.

    • Jonathan J. Cho
    • , Zhiwei Xu
    • , Upasana Parthasarathy
    • , Theodore T. Drashansky
    • , Eric Y. Helm
    • , Ashley N. Zuniga
    • , Kyle J. Lorentsen
    • , Samira Mansouri
    • , Joshua Y. Cho
    • , Mariola J. Edelmann
    • , Duc M. Duong
    • , Torben Gehring
    • , Thomas Seeholzer
    • , Daniel Krappmann
    • , Mohammad N. Uddin
    • , Danielle Califano
    • , Rejean L. Wang
    • , Lei Jin
    • , Hongmin Li
    • , Dongwen Lv
    • , Daohong Zhou
    • , Liang Zhou
    •  & Dorina Avram
  • Reviews |

    By opposing protein ubiquitylation, deubiquitylating enzymes (DUBs) regulate various cellular processes, including protein degradation, the DNA damage response, cell signalling and autophagy. Many DUBs show high specificity for ubiquitin chain architecture and/or the protein substrate that they recognize, and have emerged as exciting therapeutic targets within the field of proteostasis.

    • Michael J. Clague
    • , Sylvie Urbé
    •  & David Komander
  • Reviews |

    Misfolded proteins have a high propensity to form potentially toxic aggregates. Cells employ a complex network of processes, involving chaperones and proteolytic machineries that ensure proper protein folding and remodel or degrade misfolded species and aggregates. This proteostasis network declines with age, which can be linked to human degenerative diseases.

    • Mark S. Hipp
    • , Prasad Kasturi
    •  & F. Ulrich Hartl

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