Intramembrane proteases identify target proteins in a different way from other proteases.

Cleavage of a membrane-bound transcription factor by the chemotherapeutic reagent doxorubicin can block the proliferation of tumor cells.

The enzyme p97/VCP regulates the activity of the transcription factor Nrf1 to promote increased transcription of genes that encode proteasome subunits following inhibition of the proteasome.

Genetic rescue experiments reveal that γ-secretase enzymes containing Aph1b subunits control signalling by type III neuregulin 1, with implications for schizophrenia.

Parallel horizontal gene transfer has spread a bacteriolytic gene family to all domains of life, and has bestowed a niche-transcending adaptation in recipients that must deploy antibacterial molecules to survive in a bacterial world.

Mutational analysis and biochemical experiments suggest that the conserved β-hairpin-like membrane-reentrant loop of RseP - an S2P family intramembrane cleaving protease - helps to discriminate substrates by directly interacting with their transmembrane segments.

The metalloprotease ADAM10 modulates axon and synapse function by cleaving numerous synaptic and axonal membrane proteins in the central nervous system.

The protease γ-secretase generates amyloid-beta peptides using a mechanism that is driven by the stabilization of an enzyme-substrate scisson complex.

Feedback mechanisms that contribute to the deactivation of the unfolded protein response lead to the dysregulation of mRNA expression during chronic stress in the liver, including that of the critical endoplasmic reticulum chaperone BiP.