Activation-loop autophosphorylation is mediated by a novel transitional intermediate form of DYRKs

Article Abstract:

The molecular mechanism by which the autophosphorylation of a critical residue takes place was addressed for two dual-specificity tyrosine-phosphorylation-regulation protein kinases (DYRKs), as they autophosphorylate their substrates on serine and threonine. Demonstrations reveal that autophosphorylation of a critical activation-loop tyrosine is intramolecular and mediated by the nascent kinase passing through a transitory intermediate form.

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cPLA2 is phosphorylated and activated by MAP kinase

Article Abstract:

The role of phosphorylation of cytosolic phospholipase A2 (cPLA2) in the activation process was investigated by examining the protein kinases that directly phosphorylate and activate cPLA2. The findings indicate that cPLA2 is a substrate for mitogen-activated protein (MAP) kinase. Moreover, it is reported that MAP kinase-mediated cPLA2 phosphorylation is essential for the full activation of cPLA2 in response to various stimuli.

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Proteins kinases: Chromatin-associated enzymes?

Article Abstract:

New insights gleaned from studies showing that protein kinases associate with the entire transcribed region of target genes and might also play a more general role as chromatin-associated enzymes are presented. The data indicate that marked differences in gene targeting by protein kinases exist and that individual members of a closely related protein kinases family might exhibit functional differences in gene regulation.

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