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CDK16 negatively modulates p53 signaling pathway to promote radioresistance in lung cancer cells.
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CDK16 is significantly up-regulated in non-small cell lung cancer tumor tissue and plays a role in promoting cell proliferation.
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Authors provided the first evidence that CDK16 is an bona fide oncogene in HCC, and multiple activating mechanisms at transcriptional and posttranscriptional levels together contributes to CDK16 up-regulation in HCC.
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PCTAIRE1 has a role in regulating p27, c-Myc levels and tumor growth in cutaneous cutaneous squamous cell carcinoma cells
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CDK-16 upregulation in serous EOC cells may represent a negative feedback loop to promote ovarian cell differentiation in malignantly-transformed serous epithelial ovarian cancer cells
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GALNT7 and CDK16 were confirmed to be the direct targets of miR-494. These results suggested that miR-494 play an inhibitory role in the tumorigenesis of NPC
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Activation of PCTAIRE-1 is mediated through interaction with the phosphorylated form of cyclin Y in complex with 14-3-3.
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PCTK1 in the proliferation and survival of medulloblastoma characterized by cMYC amplification
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PCTK1 regulates spindle orientation through phosphorylation of Ser83 on KAP0, a regulatory subunit of protein kinase A.
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An unexpected role for PCTAIRE1 in regulating p27 stability, mitosis, and tumor growth.
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Dysfunction of MKL2 and its transcriptional coactivation partner, serum response factor (SRF), was supported by a decrease in gene and protein expression of PCTAIRE1, a downstream target of MKL2:SRF heterodimer transcriptional activation
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Pctaire1 exerts promyogenic effects by regulating myoblast migration and process formation during skeletal myogenesis
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a novel function of BRSK2 in the regulation of GSIS in beta-cells via a PCTAIRE1-dependent mechanism and suggest that BRSK2 is an attractive target for developing novel diabetic drugs.
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CCNY binding to CDK16 required a region upstream of the kinase domain and was found to be inhibited by phosphorylation of serine 153, a potential PKA phosphorylation site.
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Cdk5-dependent phosphorylation of Pctaire1 at Ser95 plays an important role in dendrite development
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Data show that various forms of PCTAIRE-1 transfected into neuroblastoma cell lines could either promote or inhibit neurite outgrowth, suggesting a potential role for the PCTAIRE-1 gene product in the control of neurite outgrowth.
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Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein
