Although MTA-2 has zinc finger domains similar to the GATA family of proteins, experimental evidence in support of direct DNA-binding activity of MTA proteins is lacking.18,21 It therefore remains to study the detailed molecular mechanism of MTA-2 and GATA-3 interaction in the regulation of il4 and ifng gene expression, in particular whether MTA-2 binds directly to DNA. Previous studies have shown that GATA-1, the founding member of the GATA family, directly interacts with FOG-1,32,33 and that FOG-1 recruits the NuRD complex, which includes MTA-2, to GATA-1/FOG-1 target

genes through binding of N-terminal regions of FOG-1.24,34,35 GATA-3 has also been shown to interact with FOG-1,27 so there is a possibility that the interaction of GATA-3 with MTA-2 is also mediated by FOG-1. It will be interesting SCH 900776 solubility dmso to study the involvement of FOG-1 in this interaction. In conclusion,

this study discovered that GATA-3 interacts buy GSK126 with MTA-2, a chromatin remodelling factor, to regulate Th2 cytokine and ifng loci. This study describes a fundamental molecular mechanism of Th2 cell differentiation, and will provide valuable insight for finding strategies to treat Th2-related diseases such as allergy and asthma. This work was supported partly by a National Research Foundation of Korea (NRF) grant funded by Korean government (2009-0052965), partly by the Korea Research Foundation Grant (MOEHRD, Basic Research Promotion Fund) (KRF-2006-331-C00214), partly by the Research Program for New Drug Target Discovery through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2009-0083358), and by a 2006 intramural grant funded by Sogang University (20061018). S.S. Hwang is a fellow of Seoul Scholarship. The authors have no potential conflicts of interest. Figure S1. Effects of the acetylation of GATA-3 on the interaction between GATA-3 and MTA2. Please note: Wiley-Blackwell are not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries

(other than missing material) should be directed Dimethyl sulfoxide to the corresponding author for the article. “
“School of General Studies, GIST College, Gwangju Institute of Science and Technology, Gwangju, Korea Platelet-activating factor (PAF) promotes tumour metastasis via activation of the transcription factor nuclear factor-κB (NF-κB). We here investigated the role of the protein kinase CK2 (formerly Casein Kinase 2 or II) in PAF-induced NF-κB activation and tumour metastasis, given that PAF has been reported to increase CK2 activity, and that CK2 plays a key role in NF-κB activation. PAF increased CK2 activity, phosphorylation and protein expression in vivo as well as in vitro. CK2 inhibitors inhibited the PAF-mediated NF-κB activation and expression of NF-κB-dependent pro-inflammatory cytokines and anti-apoptotic factors.