Mycobacterium tuberculosis (Mtb), effectors secreted through SecA2 pathway cause double strand breaks (DSBs) in the host DNA, which in turn activates ATM kinase to gain survival advantages, through Akt.
The kinase that controls maternal mRNA translation is regulated by phosphorylation of its activating subunit to restrict kinase activity to the developmental window between meiosis completion and early embryogenesis.
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.
The poorly characterized BTB-protein SPOPL is required to maintain the function of the late endosomal system and the endocytic adaptor EPS15 is therein targeted by the SPOPL/Cullin-3 ubiquitin ligase complex for degradation.
A rationally designed small molecule ATP-mimetic activates IRE1 and PERK signaling in cells by inducing conformational changes that template the assembly of higher-order enzymatically active structures.
An atomic model of the bacterial chemosensory array obtained through the synthesis of cryo-electron tomography and large-scale molecular-dynamics simulations reveals a new kinase conformation during signaling events.