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Sestrin as a Feedback Inhibitor of TOR That Prevents Age-Related Pathologies
Lee, J. H.,Budanov, A. V.,Park, E. J.,Birse, R.,Kim, T. E.,Perkins, G. A.,Ocorr, K.,Ellisman, M. H.,Bodmer, R.,Bier, E.,Karin, M. American Association for the Advancement of Scienc 2010 Science Vol.327 No.5970
<P>Sestrins are conserved proteins that accumulate in cells exposed to stress, potentiate adenosine monophosphate-activated protein kinase (AMPK), and inhibit activation of target of rapamycin (TOR). We show that the abundance of Drosophila sestrin (dSesn) is increased upon chronic TOR activation through accumulation of reactive oxygen species that cause activation of c-Jun amino-terminal kinase and transcription factor Forkhead box O (FoxO). Loss of dSesn resulted in age-associated pathologies including triglyceride accumulation, mitochondrial dysfunction, muscle degeneration, and cardiac malfunction, which were prevented by pharmacological activation of AMPK or inhibition of TOR. Hence, dSesn appears to be a negative feedback regulator of TOR that integrates metabolic and stress inputs and prevents pathologies caused by chronic TOR activation that may result from diminished autophagic clearance of damaged mitochondria, protein aggregates, or lipids.</P>
( Na Luo ),( Guan Li ),( Yong Qing Li ),( Xiong Wei Fan ),( Yue Qun Wang ),( Xiang Li Ye ),( Xiao Yan Mo ),( Jun Mei Zhou ),( Wu Zhou Yuan ),( Ming Tan ),( Hua Ping Xie ),( Karen Ocorr ),( Rolf Bodmer 생화학분자생물학회 (구 한국생화학분자생물학회) 2010 BMB Reports Vol.43 No.5
The sterile alpha motif (SAM) is a putative protein interaction domain involved in a wide variety of biological processes. Here we report the identification and characterization of a novel gene, SAMD4B, which encodes a putative protein of 694 amino acids with a SAM domain. Northern blot and RT-PCR analysis showed that SAMD4B is widely expressed in human embryonic and adult tissues. Transcriptional activity assays show SAMD4B suppresses transcriptional activity of L8G5-luciferase. Over-expression of SAMD4B in mammalian cells inhibited the transcriptional activities of activator protein-1 (AP-1), p53 and p21, and the inhibitory effects can be relieved by siRNA. Deletion analysis indicates that the SAM domain is the main region for transcriptional suppression. The results suggest that SAMD4B is a widely expressed gene involved in AP-1-, p53-and p21-mediated transcriptional signaling activity. [BMB reports 2010; 43(5): 355-361]
KBTBD7, a novel human BTB-kelch protein, activates transcriptional activities of SRE and AP-1
( Jun Jian Hu ),( Wu Zhou Yuan ),( Ming Tang ),( Yue Qun Wang ),( Xiong Wei Fan ),( Xiao Yang Mo ),( Yong Qing Li ),( Zao Chu Ying ),( Yong Qi Wan ),( Karen Ocorr ),( Rolf Bodmer ),( Yun Deng ),( Xiu 생화학분자생물학회 2010 BMB Reports Vol.43 No.1
Weishi Yu,Yuequn Wang,Yongqing Li,Yun Deng,Zequn Wang,Wuzhou Yuan,Dali Li,Chuanbing Zhu,Xueying Zhao,Xiaoyang Mo,Wen Huang,Na Luo,Yan Yan,Karen Ocorr,Rolf Bodmer,Xiushan Wu 한국분자세포생물학회 2008 Molecules and cells Vol.26 No.5
The Bric-a-brac, Tramtrack, Broad-complex (BTB) domain is a protein-protein interaction domain that is found in many zinc finger transcription factors. BTB containing proteins play important roles in a variety of cellular functions including regulation of transcription, regulation of the cytoskeleton, protein ubiquitination, angiogenesis, and apoptosis. Here, we report the cloning and characterization of a novel human gene, KLHL31, from a human embryonic heart cDNA library. The cDNA of KLHL31 is 5743 bp long, encoding a protein product of 634 amino acids containing a BTB domain. The protein is highly conserved across different species. Western blot analysis indicates that the KLHL31 protein is abundantly expressed in both embryonic skeletal and heart tissue. In COS-7 cells, KLHL31 proteins are localized to both the nucleus and the cytoplasm. In primary cultures of nascent mouse cardiomyocytes, the majority of endogenous KLHL31 proteins are localized to the cytoplasm. KLHL31 acts as a transcription repressor when fused to GAL4 DNA-binding domain and deletion analysis indicates that the BTB domain is the main region responsible for this repression. Overexpression of KLHL31 in COS-7 cells inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE). KLHL31 also significantly reduces JNK activation leading to decreased phosphorylation and protein levels of the JNK target c-Jun in both COS-7 and Hela cells. These results suggest that KLHL31 protein may act as a new transcriptional repressor in MAPK/JNK signaling pathway to regulate cellular functions.