Proteases are enzymes that catalyse hydrolysis of the peptide and isopeptide bonds that join amino acids within proteins (known as proteolysis). Proteases can also remove protein post-translational modifications. Exopeptidases remove the terminal amino acids from the protein chain and endopeptidases attack an internal peptide bond, as in trypsin, chymotrypsin, pepsin, elastase and papain.

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News and Comment

  • News & Views |

    Chemoproteomics reveals a cysteine oxidation event that inhibits the maturation process of a lysosomal protease, enabling its secretion into the extracellular space during infection-induced tumorigenesis. A recent study offers a new mechanistic paradigm for redox-dependent regulation of protein trafficking.

    • Jing Yang
  • News & Views |

    Inflammasomes are cytosolic immune complexes that initiate inflammatory signaling upon pathogen recognition. A new paper reveals that inhibition of M24B aminopeptidases drives the selective activation of the CARD8 inflammasome, providing new insights into its regulation.

    • Jessie Kulsuptrakul
    •  & Patrick S. Mitchell
  • News & Views |

    LYTACs induce selective degradation of extracellular proteins by recruiting them to cellular receptors that mediate delivery to the lysosome. Recent development of GalNAc-LYTACs and MoDE-As targeting the liver-specific ASGPR enables cell-type-restricted lysosomal protein degradation and reveals new LYTAC design principles.

    • Joshiawa Paulk