Autocatalytic dual specificity of kinase IKK2/β, a Serine/Threonine kinase, is important for its substrate phosphorylation activity through an uncommon phosphorelay mechanism.
Roman O Fedoryshchak, Karim El-Bouri ... Richard Treisman
Proteomics with PP1-Neurabin fusion proteins identify the 4E-BP proteins as novel Neurabin/PP1 substrates, and interaction with the Neurabin PDZ domain shown to be the major determinant of Neurabin/PP1 substrate specificity.
A high-throughput chemical screen identifies ligands of the Kelch domain of E3 ligase KLHDC2 capable of being modified as proteolysis-targeting chimeras.
A coiled-coil-based transduction mechanism is identified for a serine/threonine phosphatase that controls a bacterial stress response, suggesting that phosphatases are part of a modularly exchangeable toolkit for bacterial signaling.
The drug-phospholipid interaction is fully elucidated at molecular level as an important part of the mode of action of daptomycin and the mechanism of its resistance in bacterial pathogens.
