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KMID : 0624620100430010017
BMB Reports
2010 Volume.43 No. 1 p.17 ~ p.22
KBTBD7, a novel human BTB-kelch protein, activates transcriptional activities of SRE and AP-1
Hu Jun-jian

Yuan Wu-Zhou
Tang Ming
Wang Yue-Qun
Fan Xiong-Wei
Mo Xiao-Yan
Li Yong-Qing
Ying Zaochu
Wan Yongqi
Ocorr Karen
Bodmer Rolf
Deng Yun
Wu Xiu-Shan
Abstract
In this study, a novel member of BTB-kelch proteins, named KBTBD7, was cloned from a human embryonic heart cDNA library. The cDNA of KBTBD7 is 3,008 bp long and encodes a protein product of 684 amino acids (77.2 kD). This protein is highly conserved in evolution across different species. Western blot analysis indicates that a 77 kD protein specific for KBTBD7 is wildly expressed in all embryonic tissues examined. In COS-7 cells, KBTBD7 proteins are localized to the cytoplasm. KBTBD7 is a transcription activator when fused to GAL4 DNA-binding domain. Deletion analysis indicates that the BTB domain and kelch repeat motif are main regions for transcriptional activation. Overexpression of KBTBD7 in MCF-7 cells activates the transcriptional activities of activator protein-1 (AP-1) and serum response element (SRE), which can be relieved by siRNA. These results suggest that KBTBD7 proteins may act as a new transcriptional activator in mitogen-activated protein kinase (MAPK) signaling.
KEYWORD
AP-1, BTB-kelch¡¯KBTBD7, SRE, Transcriptional activator
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