Affiliation: Kyoto University
Miyata Y, Nishida E. CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol Cell Biol. 2004;24:4065-74 pubmed
Miyata Y, Nishida E. Evaluating CK2 activity with the antibody specific for the CK2-phosphorylated form of a kinase-targeting cochaperone Cdc37. Mol Cell Biochem. 2008;316:127-34 pubmed publisher
..These results show that the anti-[pSer13]-Cdc37 antibody can be a promising new tool to evaluate in vivo CK2 activity. ..
Miyata Y, Nakamoto H, Neckers L. The therapeutic target Hsp90 and cancer hallmarks. Curr Pharm Des. 2013;19:347-65 pubmed
..Finally, we discuss the "Hsp90-addiction" of cancer cells, and suggest a role for Hsp90 in tumor evolution. ..
Miyata Y. Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery. Cell Mol Life Sci. 2009;66:1840-9 pubmed publisher
..The tumor kinome appears to become addicted to the Hsp90-Cdc37 chaperone system, thus, targeting Hsp90, Cdc37, and CK2 is a promising strategy for cancer treatment. ..
Miyata Y, Yoneda Y, Yahara I. Stimulation of CK2-dependent Grp94 phosphorylation by the nuclear localization signal peptide. Mol Cell Biochem. 2011;356:191-200 pubmed publisher
..We suggest a possible general role for CK2-catalyzed phosphorylation in the regulation of NLS-dependent protein nuclear translocation. ..
Miyata Y, Shibata T, Aoshima M, Tsubata T, Nishida E. The molecular chaperone TRiC/CCT binds to the Trp-Asp 40 (WD40) repeat protein WDR68 and promotes its folding, protein kinase DYRK1A binding, and nuclear accumulation. J Biol Chem. 2014;289:33320-32 pubmed publisher
..Altogether, our results demonstrate that the molecular chaperone TRiC/CCT is essential for correct protein folding, DYRK1A binding, and nuclear accumulation of WDR68. ..
Miyata Y, Nishida E. CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone. Mol Cell Biochem. 2005;274:171-9 pubmed
..The structure of Cdc37 and physiological importance of the CK2-Cdc37 interaction are discussed. ..
Miyata Y, Nishida E. DYRK1A binds to an evolutionarily conserved WD40-repeat protein WDR68 and induces its nuclear translocation. Biochim Biophys Acta. 2011;1813:1728-39 pubmed publisher
..Taken together, these results suggest that DYRK1A binds specifically to WDR68 in cells, and that the binding, but not the phosphorylation event, induces the nuclear translocation of WDR68. ..