Protease-Activatable Scaffold Proteins as Versatile Molecular Hubs in Synthetic Signaling Networks.

ABSTRACT: Protease signaling and scaffold-induced control of protein-protein interactions represent two important mechanisms for intracellular signaling. Here we report a generic and modular approach to control the activity of scaffolding proteins by protease activity, creating versatile molecular platforms to construct synthetic signaling networks. Using 14-3-3 proteins as a structurally well-characterized and important class of scaffold proteins, three different architectures were explored to achieve optimal protease-mediated control of scaffold activity, fusing either one or two monovalent inhibitory ExoS peptides or a single bivalent ExoS peptide to T14-3-3 using protease-cleavable linkers. Analysis of scaffolding activity before and after protease-induced cleavage revealed optimal control of 14

SUBMITTER: Aper SJA 

PROVIDER: S-EPMC6154215 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature