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. [BMB reports 2010; 43(1): 17-22].
journal_name
BMB Repjournal_title
BMB reportsauthors
Hu J,Yuan W,Tang M,Wang Y,Fan X,Mo X,Li Y,Ying Z,Wan Y,Ocorr K,Bodmer R,Deng Y,Wu Xdoi
10.5483/bmbrep.2010.43.1.017subject
Has Abstractpub_date
2010-01-01 00:00:00pages
17-22issue
1eissn
1976-6696issn
1976-670Xjournal_volume
43pub_type
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