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.
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.
Global phosphoproteomic analysis in nerve terminal during exocytosis reveals 252 uniquely regulated phosphosites, highlighting complex regulation of active zone proteins at multiple sites and the role of specific kinases/phosphatases.
A deubiquitinase antagonizes the activity of an associated E3 ligase to prevent uncontrolled ubiquitination of a degradation machinery protein and thus maintain its functionality in protein quality control at the endoplasmic reticulum.