Search

Your search keyword '"Cho, Seung-Ju"' showing total 26 results
Start Over Author "Cho, Seung-Ju"
26 results on '"Cho, Seung-Ju"'

9. Protein kinase C‐δ interacts with and phosphorylates ARD1.

Author

Chun, Kwang‐Hoon, Cho, Seung‐Ju, Lee, Ji‐Won, Seo, Ji Hae, Kim, Kyu‐Won, and Lee, Seung‐Ki

Subjects
*PROTEIN kinases, *CELL communication, *AMINO acid sequence, *MASS spectrometry, *APOPTOSIS, *GLUTATHIONE transferase
Abstract

Protein kinase C‐δ (PKCδ) is a diacylglycerol‐dependent, calcium‐independent novel PKC isoform that is engaged in various cell signaling pathways, such as cell proliferation, apoptosis, inflammation, and oxidative stress. In this study, we searched for proteins that bind PKCδ using a yeast two‐hybrid assay and identified murine arrest‐defective 1 (mARD1) as a binding partner. The interaction between PKCδ and mARD1 was confirmed by glutathione S‐transferase pull‐down and co‐immunoprecipitation assays. Furthermore, recombinant PKCδ phosphorylated full‐length mARD1 protein. The NetPhos online prediction tool suggested PKCδ phosphorylates Ser80, Ser108, and Ser114 residues of mARD1 with the highest probability. Based on these results, we synthesized peptides containing these sites and examined their phosphorylations using recombinant PKCδ. Autoradiography confirmed these sites were efficiently phosphorylated. Consequent mass spectrometry and peptide sequencing in combination with MALDI‐TOF MS/MS confirmed that Ser80 and Ser108 were major phosphorylation sites. The alanine mutations of Ser80 and Ser108 abolished the phosphorylation of mARD1 by PKCδ in 293T cells supporting these observations. In addition, kinase assays using various PKC isotypes showed that Ser80 of ARD1 was phosphorylated by PKCβI and PKCζ isotypes with the highest selectivity, while Ser108 and/or Ser114 were phosphorylated by PKCγ with activities comparable to that of the PKCδ isoform. Overall, these results suggest the possibility that PKCδ transduces signals by regulating phosphorylation of ARD1. [ABSTRACT FROM AUTHOR]

Published
2021
Full Text
View/download PDF

18. Black Raspberry-Derived Anthocyanins Demethylate Tumor Suppressor Genes Through the Inhibition of DNMT1 and DNMT3B in Colon Cancer Cells

Author

Wang, Li-Shu, primary, Kuo, Chieh-Ti, additional, Cho, Seung-Ju, additional, Seguin, Claire, additional, Siddiqui, Jibran, additional, Stoner, Kristen, additional, Weng, Yu-I, additional, Huang, Tim H.-M., additional, Tichelaar, Jay, additional, Yearsley, Martha, additional, Stoner, Gary D., additional, and Huang, Yi-Wen, additional

Published
2013
Full Text
View/download PDF

26. Differential regulation of splicing, localization and stability of mammalian ARD1235 and ARD1225 isoforms

Author

Chun, Kwang-Hoon, Cho, Seung-Ju, Choi, Joon-Seok, Kim, Se-Hee, Kim, Kyu-Won, and Lee, Seung-Ki

Subjects
*CELL nuclei, *APOPTOSIS, *CYTOPLASM, *LEAVENING agents
Abstract

Abstract: ARD1 protein is a mammalian gene product homologous to a yeast Ard1p (Arrest defective 1 protein) acetyltransferase. Although two alternative splicing products of ARD1, ARD1235 and ARD1225, were reported in mouse, only ARD1235 orthologue was reported in humans. Here we show that ARD1225 is not expressed in humans, suggesting that factors regulating alternative splicing of ARD1 may have evolved differently between species. In human cells, hARD1235 is shown to be present in both nucleus and cytoplasm. However, in mouse cells, mARD1235 and mARD1225 proteins are localized to the nucleus and cytoplasm, respectively. Moreover, during apoptosis, ARD1235 and ARD1225 isoforms are destabilized by different mechanisms in a species-specific manner and dependent on destabilizing reagents. These results indicate that ARD1235 and ARD1225 isoforms may have different activities and function in different subcellular compartments of mammalian cells. [Copyright &y& Elsevier]

Published
2007
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results