CK1ε is a member of the CK1 family of serine/threonine protein kinases which play an important role in diverse cell processes, including DNA replication and repair. CK1ε is a regulator of Yes-associated protein (YAP) transcription coactivator which is a key regulator of organ size and a candidate human oncogene. CK1ε is activated by CCK2R and this then phosphorylates PKD2 at Ser244. Phosphorylation of PKD2 leads to its nuclear accumulation and efficient phosphorylation of nuclear PKD2 substrates in human gastric cancer cells. CKIε can phosphorylate topoisomerase (topo) IIalpha at serine-1106 and this regulates the enzyme activity and sensitivity to topo II-targeted drugs.
We previously reported that phosphorylation of topoisomerase (topo) IIalpha at serine-1106 (Ser-1106) regulates enzyme activity and sensitivity to topo II-targeted drugs. In this study we demonstrate that phosphorylation of Ser-1106, which is flanked by acidic amino acids, is regulated in
Protein kinase D2 (PKD2), a member of the PKD family of serine/threonine kinases, is localized in various subcellular compartments including the nucleus where the kinase accumulates upon activation of G-protein-coupled receptors. We define three critical post-translational modifications required for nuclear
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