Proteolysis of lipidated N-terminal peptides that tether Hedgehog morphogens to the surface of source cells is absolutely required for their coupled release and bioactivation in vivo in Drosophila melanogaster.
Selective APC/C-mediated proteolysis of cyclin B drives progression through the metaphase-anaphase transition whilst wide-spread waves of dephosphorylation co-ordinate the subsequent events of mitotic exit.
Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.
Kif26b, a new component of the evolutionarily conserved Wnt5a-Ror signaling pathway, is controlled by regulated proteolysis and plays crucial roles in mediating vertebrate embryonic tissue morphogenesis.
The modularity and unequivocal input/response of Notch signaling are harnessed to measure cell-surface shedding of diverse transmembrane receptors to identify new proteolytic switches and detect modulation of proteolysis by therapeutics.
Crosslinking the AAA+ protease interface does not abolish protein degradation by ClpAP, establishing that rotation of the AAA+ unfoldase with respect to its partner peptidase is not essential for activity.