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.
The determination of GAGases structure facilitates the elucidation of the catalytic mechanism of PL35 family lyases and provides potential evidence for the hypothesis that GAG lyase evolved from alginate lyase.
