Human cullin-RING ligases are buffered to a much greater extent than had been previously appreciated, and the roles of ubiquitin chain extension enzymes are far more nuanced at physiological concentrations.
Genetic code expansion (GCE) enables site-specific labeling and visualization of Salmonella secreted effectors, secretion system components and provides a viable alternative for labeling proteins that do not tolerate N- or C-terminal tags.
Reconstructing ancestral enzymes has revealed that a switch in kinase substrate preference evolved via an expanded specificity intermediate that is tolerated in vivo, thus providing a path for kinase diversification.
A high-throughput comparison of substrate specificities of the Src-family kinases Lck and c-Src against a library of proteome-derived phosphorylation sites reveals that Lck has evolved divergent electrostatic features reflecting its involvement in T-cell signaling.
The threonine kinase controls maternal mRNA translation phosphorylate components of the translational machinery, including translational repressors, which appear to inactivate to promote the oocyte-to-embryo transition.