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Two Dictyostelium tyrosine kinase-like kinases function in parallel, stress-induced STAT activation pathways.

Araki T, Vu LH, Sasaki N, Kawata T, Eichinger L, Williams JG - Mol. Biol. Cell (2014)

Bottom Line: The site(s) that are generated bind the SH2 domain of STATc, and then STATc becomes the target of further kinase action.The latter functions, like the JH2 domain of metazoan JAKs, as a negative regulator of the kinase domain.The fact that two differently regulated kinases catalyze the same phosphorylation event may facilitate specific targeting because under stress, Pyk3 and Pyk2 accumulate in different parts of the cell; Pyk3 moves from the cytosol to the cortex, whereas Pyk2 accumulates in cytosolic granules that colocalize with PTP3.

View Article: PubMed Central - PubMed

Affiliation: College of Life Sciences, Welcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, United Kingdom.

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Transcriptional regulation of STATc target genes and STATc pathway genes. Real-time PCR analysis of selected STATc-dependent genes was carried out with cDNAs from Ax2 wild-type, pyk2−, pyk3−, pyk2−/pyk3−, and STATc− cells either treated for 15 min with 200 mM sorbitol or left untreated. (A) Differential expression of STATc target genes rtoA, sigG , and DDB_G0277667. (B) Differential expression of STATc pathway genes dstc, ptpC, pyk2, and pyk3. The data are expressed as means of fold change in comparison to untreated cells. Fold changes and SEM of three independent experiments with three measurements each. N/A, not applicable. Unpaired t test: *p < 0.05; **p < 0.01; ***p < 0.001; NS, not significant. Statistical significance as compared with expression values in Ax2 cells is indicated.
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Figure 4: Transcriptional regulation of STATc target genes and STATc pathway genes. Real-time PCR analysis of selected STATc-dependent genes was carried out with cDNAs from Ax2 wild-type, pyk2−, pyk3−, pyk2−/pyk3−, and STATc− cells either treated for 15 min with 200 mM sorbitol or left untreated. (A) Differential expression of STATc target genes rtoA, sigG , and DDB_G0277667. (B) Differential expression of STATc pathway genes dstc, ptpC, pyk2, and pyk3. The data are expressed as means of fold change in comparison to untreated cells. Fold changes and SEM of three independent experiments with three measurements each. N/A, not applicable. Unpaired t test: *p < 0.05; **p < 0.01; ***p < 0.001; NS, not significant. Statistical significance as compared with expression values in Ax2 cells is indicated.

Mentions: To determine the effects of the various mutations on specific gene expression, we analyzed, by quantitative real-time PCR (qPCR), the sorbitol induction of three genes known to require STATc for their optimal inducibility: rtoA, sigG, and an uncharacterized gene (Dictybase ID DDB_G0277667). The three genes are maximally induced in the parental (Ax2) strain and somewhat less well induced in the pyk2− or pyk3− strain (Figure 4A). In the double- strain, and as expected in the STATc- strain, sorbitol inducibility is abolished and there is even, perhaps, slight repression of gene expression by sorbitol.


Two Dictyostelium tyrosine kinase-like kinases function in parallel, stress-induced STAT activation pathways.

Araki T, Vu LH, Sasaki N, Kawata T, Eichinger L, Williams JG - Mol. Biol. Cell (2014)

Transcriptional regulation of STATc target genes and STATc pathway genes. Real-time PCR analysis of selected STATc-dependent genes was carried out with cDNAs from Ax2 wild-type, pyk2−, pyk3−, pyk2−/pyk3−, and STATc− cells either treated for 15 min with 200 mM sorbitol or left untreated. (A) Differential expression of STATc target genes rtoA, sigG , and DDB_G0277667. (B) Differential expression of STATc pathway genes dstc, ptpC, pyk2, and pyk3. The data are expressed as means of fold change in comparison to untreated cells. Fold changes and SEM of three independent experiments with three measurements each. N/A, not applicable. Unpaired t test: *p < 0.05; **p < 0.01; ***p < 0.001; NS, not significant. Statistical significance as compared with expression values in Ax2 cells is indicated.
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Figure 4: Transcriptional regulation of STATc target genes and STATc pathway genes. Real-time PCR analysis of selected STATc-dependent genes was carried out with cDNAs from Ax2 wild-type, pyk2−, pyk3−, pyk2−/pyk3−, and STATc− cells either treated for 15 min with 200 mM sorbitol or left untreated. (A) Differential expression of STATc target genes rtoA, sigG , and DDB_G0277667. (B) Differential expression of STATc pathway genes dstc, ptpC, pyk2, and pyk3. The data are expressed as means of fold change in comparison to untreated cells. Fold changes and SEM of three independent experiments with three measurements each. N/A, not applicable. Unpaired t test: *p < 0.05; **p < 0.01; ***p < 0.001; NS, not significant. Statistical significance as compared with expression values in Ax2 cells is indicated.
Mentions: To determine the effects of the various mutations on specific gene expression, we analyzed, by quantitative real-time PCR (qPCR), the sorbitol induction of three genes known to require STATc for their optimal inducibility: rtoA, sigG, and an uncharacterized gene (Dictybase ID DDB_G0277667). The three genes are maximally induced in the parental (Ax2) strain and somewhat less well induced in the pyk2− or pyk3− strain (Figure 4A). In the double- strain, and as expected in the STATc- strain, sorbitol inducibility is abolished and there is even, perhaps, slight repression of gene expression by sorbitol.

Bottom Line: The site(s) that are generated bind the SH2 domain of STATc, and then STATc becomes the target of further kinase action.The latter functions, like the JH2 domain of metazoan JAKs, as a negative regulator of the kinase domain.The fact that two differently regulated kinases catalyze the same phosphorylation event may facilitate specific targeting because under stress, Pyk3 and Pyk2 accumulate in different parts of the cell; Pyk3 moves from the cytosol to the cortex, whereas Pyk2 accumulates in cytosolic granules that colocalize with PTP3.

View Article: PubMed Central - PubMed

Affiliation: College of Life Sciences, Welcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, United Kingdom.

Show MeSH