Anita Alexa

TL;DR: This work claims that this is the first kinetically correct determination of the rate constant of autolysis of mu-calpain, and it cannot exclude the possibility that the activation process involves other mechanistic steps, e.g. the rapid dissociation of the mu-Calpain heterodimer.

TL;DR: It is proposed that short MAPK‐binding stretches are created in disordered protein segments through a variety of ways and they represent a major resource for ancient signaling enzymes to acquire new regulatory roles.

TL;DR: Although S100B-RSK1 and the calmodulin-CAMKII system are clearly distinct functionally, they demonstrate how unrelated intracellular Ca2+-binding proteins could influence the activity of the CaMK domain-containing protein kinases.

TL;DR: It is demonstrated that protection is biphasically dependent on the degree of phosphorylation, and that stripping of native MAP2 from its phosphate content enhances calpainolysis 3.6‐fold.

TL;DR: The crystal structure of an RSK1 construct in complex with its activator kinase captures the kinase–kinase complex in a precatalytic state where the activation loop of the downstream kinase (RSK1) faces the enzyme's (ERK2) catalytic site.