A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation

Article Abstract:

Pyk2 acts with the epidermal growth factor (EGF) receptor Src to link G(sub 1)- and G(sub q)-coupled receptors with Grb2 and Sos to activate the MAP kinase signalling pathway in PC12 cells. Lysophosphatidic acid and bradykinin were shown to induce tyrosine phosphorylation of Pyk2 and complex formation between Pyk2 and activated Src. Tyrosine phosphorylation of Pyk2 also leads to binding of the SH2 domain of Src to tyrosine 402 of Pyk2 and activation of Src. LPA- or bradykinin-induced activation of MAP kinase is reduced by transient overexpression of a dominant interfering mutant of Pyk2.

Analysis, Signal peptides, Linkage (Genetics)

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Interaction of a G-protein beta-subunit with a conserved sequence in Ste20/PAK family protein kinases

Article Abstract:

It has been possible to identify a binding site for the G-protein beta-subunit (G-beta) in the non-catalytic carboxy-terminal regions of Ste20 and its mammalian homologues, the p21-activated protein kinases (PAKs). The results of this research offer a possible model for a role of these kinases in G-beta-gamma-mediated signal transduction in many different organisms. The transmission of the pheromone signal was found to involve the regulated interaction between the mating-response G-protein beta-subunit and a conserved sequence in the Ste20 protein kinase.

Protein metabolism

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A non-enzymatic p21 protein inhibitor of stress-activated protein kinases

Article Abstract:

The inhibiting influence of the recombinant protein, p21, on the stress-activated protein kinases (SAPKs) represents a novel biochemical step towards identification of the first non-enzymatic inhibitory protein for SAPK. p21's inhibiting character may be useful in regulating stress-activated signalling cascades in cells. The inhibition process is studied through SAPK phosphorylation of a fusion protein substrate, glutathione-S-tranferase-c-Jun. SAPKs resemble c-Jun amino-terminal kinases and are activated due to cellular stresses, including DNA damage.

DNA damage, Recombinant proteins

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