Regulation of tyrosine hydroxylase by stress-activated protein kinases

Stress-activated protein kinases: activation, regulation and function.

The response of cells to extracellular stimuli is mediated in part by a number of intracellular kinase and phosphatase enzymes. Within this area of research the activation of the p42 and p44 isoforms of mitogen-activated protein (MAP) kinases have been extensively described and characterised as central components of the signal transduction pathways stimulated by both growth factors and G-protei...

Regulation of tyrosine hydroxylase by protein phosphatase 2A

Tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis, is stimulated by N-terminal phosphorylation on its regulatory domain and inhibited by protein serine/threonine phosphatase 2A (PP2A). PP2A comprising of an AC core dimer composed of catalytic (C) and scaffolding (A) subunit is complexed to a variable regulatory subunit derived from three gene families (B, B’, B”). M...

Multilayered control of gene expression by stress-activated protein kinases.

Stress-activated protein kinases (SAPKs) are key elements for intracellular signalling networks that serve to respond and adapt to extracellular changes. Exposure of yeast to high osmolarity results in the activation of p38-related SAPK, Hog1, which is essential for reprogramming the gene expression capacity of the cell by regulation of several steps of the transcription process. At initiation,...

Regulation of receptor tyrosine kinases by Ubiquilin1

Stress-activated protein kinases are negatively regulated by cell density.

Stimulation by UV irradiation, TNFalpha, as well as PDGF or EGF activates the JNK/SAPK signalling pathway in mouse fibroblasts. This results in the phosphorylation of the N-terminal domain of c-Jun, increasing its transactivation potency. Using an antibody that specifically recognizes c-Jun phosphorylated at Ser63, we show that culture confluency drastically inhibited c-Jun N-terminal phosphory...