Bernd J. Pulverer

TL;DR: Evidence is presented that mitogen-activated protein-serine (MAP) kinases (pp54 and pp42/44) specifically phosphorylate these sites and that their phosphorylation positively regulates the transacting activity of c-jun.

TL;DR: Study of GSK-3 had an inauspicious beginning rooted in intermediary metabolism, however, owing to the fortuitous convergence of several disparate areas of biology, the enzyme now offers unique opportunities for study of the control of a variety cellular processes.

TL;DR: Data suggest acute, post-translational modulation of Myc via phosphorylation of a conserved region previously implicated in transactivation, transformation and autorepression.

TL;DR: A protein kinase activity is detectable in extracts of phorbol ester-treated U937 cells that specifically targets these two serines located within the A1 transactivation domain of c-Jun that have been shown to positively regulate activity.

TL;DR: A rapid purification scheme has been developed yielding essentially pure GSK-3 beta protein in three chromatographic steps, and it is likely that the Drosophila zw3sgg protein kinase has a similar specificity for such transcription factors which may underlie the pleiotropic phenotypes observed when the Dosophila homologue is mutationally inactivated.