Arginine methylation of FOXO transcription factors inhibits their phosphorylation by Akt.
- K. Yamagata, H. Daitoku, A. Fukamizu
- Biology, ChemistryMolecules and Cells
- 24 October 2008
Mitogen-activated protein kinases, Erk and p38, phosphorylate and regulate Foxo1.
- S. Asada, H. Daitoku, A. Fukamizu
- BiologyCellular Signalling
- 1 March 2007
Multitissue Circadian Expression of Rat periodHomolog (rPer2) mRNA Is Governed by the Mammalian Circadian Clock, the Suprachiasmatic Nucleus in the Brain*
- K. Sakamoto, Takahiro Nagase, N. Ishida
- BiologyJournal of Biological Chemistry
- 16 October 1998
It is suggested that the multitissue circadian expression of rPer2 mRNA was governed by the mammalian brain clock SCN and also suggest that the r per2 gene was involved in the circadian rhythm of locomotor behavior in mammals.
Mammalian Copper Chaperone Cox17p Has an Essential Role in Activation of Cytochrome c Oxidase and Embryonic Development
- Yoshinori Takahashi, K. Kako, E. Munekata
- BiologyMolecular and Cellular Biology
- 1 November 2002
It was found that the activity of lactate dehydrogenase was also normal in E6.5 embryos, implying that the activation of CCO by Cox17p may not be essential to the progress of embryogenesis before gastrulation.
Estrogen Regulates Tumor Growth Through a Nonclassical Pathway that Includes the Transcription Factors ERβ and KLF5
- Y. Nakajima, K. Akaogi, J. Yanagisawa
- Biology, ChemistryScience Signaling
- 12 April 2011
It is demonstrated that the estrogen receptor β (ERβ) mediates inhibition by the antiestrogen ICI 182,780 (ICI) and its enhancement by estrogen, and affects prostate tumor growth through ERβ-mediated regulation of KLF5.
The localization of the site of arylalkylamine N-acetyltransferase circadian expression in the photoreceptor cells of mammalian retina.
The temporal mRNA expression pattern of arylalkylamine (serotonin) N-acetyltransferase (AA-NAT) is examined, the first report to localize the site of AA-NAT mRNA circadian expression in mammalian photoreceptor cells.
Transcriptional down-regulation through nuclear exclusion of EWS methylated by PRMT1.
EWS is a substrate of type I protein arginine methyltransferase, PRMT8.
- Jun-Dal Kim, K. Kako, M. Kakiuchi, G. Park, A. Fukamizu
- BiologyInternational Journal of Molecular Medicine
EWS, a pro-oncoprotein which is encoded by the Ewing sarcoma (EWS) gene, contains arginine-glycine-glycine repeats (RGG box) in its COOH-terminus. We previously found that the RGG box of EWS is a…
PRMT8 as a phospholipase regulates Purkinje cell dendritic arborization and motor coordination
- Jun-Dal Kim, Kyung-Eui Park, A. Fukamizu
- Biology, ChemistryScience Advances
- 1 December 2015
It is shown that protein arginine methyltransferase 8 (PRMT8) acts as a phospholipase that directly hydrolyzes PC, generating choline and phosphatidic acid, and suggests that PRMT8 acts both as an arginin methyl transferase and as a PC-hydrolyzing PLD that is essential for proper neurological functions.