The Experts below are selected from a list of 2163 Experts worldwide ranked by ideXlab platform
Youming Lu - One of the best experts on this subject based on the ideXlab platform.
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degradation of caytaxin causes learning and memory deficits via activation of DAPK1 in aging
Molecular Neurobiology, 2019Co-Authors: Hao Li, Xiao Ke, Manfei Deng, Zhuoze Wu, Henok Kessete Afewerky, Xiaoan Zhang, Youming LuAbstract:Loss of memory is an inevitable clinic sign in aging, but its underlying mechanisms remain unclear. Here we show that death-associated protein kinase (DAPK1) is involved in the decays of learning and memory in aging via degradation of Caytaxin, a brain-specific member of BNIP-2. DAPK1 becomes activated in the hippocampus of mice during aging. Activation of DAPK1 is closely associated with degradation of Caytaxin protein. Silencing Caytaxin by the expression of small interfering RNA (siRNA) that targets specifically to Caytaxin in the hippocampus of adult mice impairs the learning and memory. Genetic inactivation of DAPK1 by deletion of DAPK1 kinase domain prevents the degradation of Caytaxin and protects against learning and memory declines. Thus, activation of DAPK1 impairs learning and memory by degrading Caytaxin during aging.
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DAPK1 signaling pathways in stroke from mechanisms to therapies
Molecular Neurobiology, 2017Co-Authors: Shan Wang, Hao Li, Pei Pang, Huiyong Shen, Youming LuAbstract:Death-associated protein kinase 1 (DAPK1), a Ca2+/calmodulin (CaM)-dependent serine/threonine protein kinase, plays important roles in diverse apoptosis pathways not only in tumor suppression but also in neuronal cell death. The requirement of DAPK1 catalytic activity for its proposed cell functions and the elevation of catalytic activity of DAPK1 in injured neurons in models of neurological diseases, such as ischemia and epilepsy, validate that DAPK1 can be taken as a potential therapeutic target in these diseases. Recent studies show that DAPK1-NR2B, DAPK1-DANGER, DAPK1-p53, and DAPK1-Tau are currently known pathways in stroke-induced cell death, and blocking these cascades in an acute treatment effectively reduces neuronal loss. In this review, we focus on the role of DAPK1 in neuronal cell death after stroke. We hope to provide exhaustive summaries of relevant studies on DAPK1 signals involved in stroke damage. Therefore, disrupting DAPK1-relevant cell death pathway could be considered as a promising therapeutic approach in stroke.
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selective degeneration of entorhinal ca1 synapses in alzheimer s disease via activation of DAPK1
The Journal of Neuroscience, 2016Co-Authors: Na Tang, Hao Li, Qing Tian, Wenting Chen, Xinyan Li, Yangling Mu, Youming LuAbstract:Excitatory pyramidal neurons in the entorhinal cortical layer II region (ECIIPN) form functional excitatory synapses with CA1 parvalbumin inhibitory neurons (CA1PV) and undergo selective degeneration in the early stages of Alzheimer9s disease (AD). Here, we show that death-associated protein kinase 1 (DAPK1) is selectively activated in ECIIPN of AD mice. Inhibition of DAPK1 by deleting a catalytic domain or a death domain of DAPK1 rescues the ECIIPN-CA1PV synaptic loss and improves spatial learning and memory in AD mice. This study demonstrates that activation of DAPK1 in ECIIPN contributes to a memory loss in AD and hence warrants a promising target for the treatment of AD. SIGNIFICANCE STATEMENT Our recent study reported that excitatory pyramidal neurons in the entorhinal cortical layer II region (ECIIPN) target to CA1 parvalbumin-type inhibitory neurons (CA1PV) at a direct pathway and are one of the most vulnerable brain cells that are selectively degenerated in the early stage of Alzheimer9s disease (AD). Our present study shows that death-associated protein kinase 1 (DAPK1) is selectively activated in ECIIPN of AD mice. Inhibition of DAPK1 by deleting a catalytic domain or a death domain of DAPK1 rescues the ECIIPN-CA1PV synaptic loss and improves spatial learning and memory in the early stage of AD. These data not only demonstrate a crucial molecular event for synaptic degeneration but also provide a therapeutic target for the treatment of AD.
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DAPK1 p53 interaction converges necrotic and apoptotic pathways of ischemic neuronal death
The Journal of Neuroscience, 2014Co-Authors: You Shang, Shan Wang, Yan Wu, Xiaoxi Wang, Youming LuAbstract:Necrosis and apoptosis are two distinct types of mechanisms that mediate ischemic injury. But a signaling point of convergence between them has yet to be identified. Here, we show that activated death-associated protein kinase 1 (DAPK1), phosphorylates p53 at serine-23 (pS23) via a direct binding of DAPK1 death domain (DAPK1DD) to the DNA binding motif of p53 (p53DM). We uncover that the pS23 acts as a functional version of p53 and mediates necrotic and apoptotic neuronal death; in the nucleus, pS23 induces the expression of proapoptotic genes, such as Bax, whereas in the mitochondrial matrix, pS23 triggers necrosis via interaction with cyclophilin D (CypD) in cultured cortical neurons from mice. Deletion of DAPK1DD (DAPK1DDΔ) or application of Tat-p53DM that interrupts DAPK1–p53 interaction blocks these dual pathways of pS23 actions in mouse cortical neurons. Thus, the DAPK1–p53 interaction is a signaling point of convergence of necrotic and apoptotic pathways and is a desirable target for the treatment of ischemic insults.
Wenzheng Yuan - One of the best experts on this subject based on the ideXlab platform.
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downregulation of DAPK1 promotes the stemness of cancer stem cells and emt process by activating zeb1 in colorectal cancer
Journal of Molecular Medicine, 2019Co-Authors: Wenzheng Yuan, Jintong Ji, Jinhuang Chen, Liang Wu, Zili Zhou, Qiang Tang, Xudan ZhangAbstract:: Cancer stem cells (CSCs) and epithelial-mesenchymal transition (EMT) play an important role in the metastasis and chemoresistance in the context of colorectal cancer (CRC). Downregulation of death associated protein kinase 1 (DAPK1) may promote metastasis and chemoresistance of cancer cells through various mechanisms. However, the association between DAPK1 and CSCs or EMT has not been explored. In this study, we demonstrated that DAPK1 was associated with elevated stemness of CSCs in patients with CRC. Silencing of DAPK1 in CRC cell lines promoted the metastasis and chemoresistance due to increased stemness of CSCs and enhanced mesenchymal phenotype, an effect that was mediated via activation of the transcription factor, zinc finger E-box binding homeobox 1 (ZEB1). Blockade of this signaling pathway attenuated the stemness of CSCs and rescued the EMT process. DAPK1-ZEB1 may lie at the interface of TGF-β and WNT pathways and participate in both CSCs and EMT process. Targeted therapies aimed at DAPK1-ZEB1 pathway may inhibit the chemoresistance and metastasis of CRC. KEY MESSAGES: Downregulation of DAPK1 promotes chemoresistance and metastasis of CRC. Inhibition of DAPK1 promotes the stemness of cancer stem cells and EMT process. DAPK1-ZEB1 may lie at the interface of TGF-β and WNT pathways. DAPK1-ZEB1 participates in both CSCs and EMT process.
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correlation of DAPK1 methylation and the risk of gastrointestinal cancer a systematic review and meta analysis
PLOS ONE, 2017Co-Authors: Wenzheng Yuan, Jintong Ji, Jinhuang Chen, Liang Wu, Zili Zhou, Qiang Tang, Yifeng Cheng, Bin JiangAbstract:Objective One of the critical mechanisms of gastrointestinal cancer pathogenesis is the silencing of death associated protein kinase 1 (DAPK1), which could be caused by aberrant methylation of the promoter. However, the relationship between DAPK1 methylation and the risk of gastrointestinal cancer is still controversial. Hence, we conducted this study to determine the potential correlation. Methods Eligible publications were searched in the Pubmed, Embase, and Cochrane Library through November 2016 according to the inclusion criteria and exclusion criteria. Revman 5.3 and Stata 12.0 software were used to analyze the relevant data regarding the association between the frequency of DAPK1 methylation and gastrointestinal cancer. Results A total of 22 studies with 2406 patients were included in this meta analysis. Methylation of DAPK1 was positively related with the risk of gastrointestinal cancer (odds ratio [OR] = 5.35, 95% confidence interval [CI]: 2.76–10.38, P<0.00001, random effects model). The source of heterogeneity was analyzed by sensitivity analysis and subgroup analysis. After omitting one heterogeneous study, the I2 decreased and the OR increased in pooled analysis. Also, the heterogeneity decreased most significantly in the subgroup of studies that had a sample size of less than 60 cases. Then, the correlations between DAPK1 methylation and clinicopathological features of gastrointestinal cancer were assessed. DAPK1 methylation was positively correlated with the lymph node (N) stage (positive vs. negative, OR = 1.45, 95%CI: 1.01–2.06, P = 0.04, fixed effects model) and poor differentiation (OR = 1.55, 95%CI: 1.02–2.35, P = 0.04, fixed effects model) in gastric cancer, and the association was significant among Asian patients. However, among cases of gastrointestinal cancer, the association between DAPK1 methylation and tumor (T) stage, N stage, distant metastasis (M) stage, and cancer differentiation were not statistically significant. Conclusions DAPK1 methylation is a potential biomarker for the early diagnosis of gastrointestinal cancer. Further analysis of the clinicopathological features indicated that aberrant methylation of DAPK1 is positively associated with the tumorigenesis of gastrointestinal cancer, and metastasis of gastric cancer.
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Correlation of DAPK1 methylation and the risk of gastrointestinal cancer: A systematic review and meta-analysis.
PLOS ONE, 2017Co-Authors: Wenzheng Yuan, Jintong Ji, Jinhuang Chen, Liang Wu, Zili Zhou, Qiang Tang, Yifeng ChengAbstract:Objective One of the critical mechanisms of gastrointestinal cancer pathogenesis is the silencing of death associated protein kinase 1 (DAPK1), which could be caused by aberrant methylation of the promoter. However, the relationship between DAPK1 methylation and the risk of gastrointestinal cancer is still controversial. Hence, we conducted this study to determine the potential correlation. Methods Eligible publications were searched in the Pubmed, Embase, and Cochrane Library through November 2016 according to the inclusion criteria and exclusion criteria. Revman 5.3 and Stata 12.0 software were used to analyze the relevant data regarding the association between the frequency of DAPK1 methylation and gastrointestinal cancer. Results A total of 22 studies with 2406 patients were included in this meta analysis. Methylation of DAPK1 was positively related with the risk of gastrointestinal cancer (odds ratio [OR] = 5.35, 95% confidence interval [CI]: 2.76–10.38, P
Shan Wang - One of the best experts on this subject based on the ideXlab platform.
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presynaptic caytaxin prevents apoptosis via deactivating DAPK1 in the acute phase of cerebral ischemic stroke
Experimental Neurology, 2020Co-Authors: Shan Wang, Keng Chen, Jia Yu, Xiaojiao Wang, Qiang Li, Fei Lv, Huiyong ShenAbstract:Abstract Death-associated protein kinase 1 (DAPK1) is a key protein that mediates neuronal death in ischemic stroke. Although the substrates of DAPK1 and molecular signal in stroke have been gradually discovered, the modulation of DAPK1 itself is still unclear. Here we first reveal that Caytaxin, a brain-specific member of BCL2/adenovirus E1B -interacting protein (BNIP-2), increases and interacts with DAPK1 as early as 2 h after middle cerebral artery occlusion (MCAO) in the penumbra area of mouse brain. Furthermore, Caytaxin binds to DAPK1 at the presynaptic site and inhibits DAPK1 catalytic activity. Silencing Caytaxin by Caytaxin shRNA (Sh-Caytaxin) enhances DAPK1 activity, deteriorates neuronal apoptosis and brain injuries both in vivo and in vitro. Thus, elevating presynaptic Caytaxin could prevent neuronal apoptosis by inhibiting DAPK1 activation in the acute stage of ischemic stroke. Caytaxin may physiologically protect neuronal cells and represent a potential prevention and therapeutic target in the early phase of cerebral ischemic stroke.
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DAPK1 signaling pathways in stroke from mechanisms to therapies
Molecular Neurobiology, 2017Co-Authors: Shan Wang, Hao Li, Pei Pang, Huiyong Shen, Youming LuAbstract:Death-associated protein kinase 1 (DAPK1), a Ca2+/calmodulin (CaM)-dependent serine/threonine protein kinase, plays important roles in diverse apoptosis pathways not only in tumor suppression but also in neuronal cell death. The requirement of DAPK1 catalytic activity for its proposed cell functions and the elevation of catalytic activity of DAPK1 in injured neurons in models of neurological diseases, such as ischemia and epilepsy, validate that DAPK1 can be taken as a potential therapeutic target in these diseases. Recent studies show that DAPK1-NR2B, DAPK1-DANGER, DAPK1-p53, and DAPK1-Tau are currently known pathways in stroke-induced cell death, and blocking these cascades in an acute treatment effectively reduces neuronal loss. In this review, we focus on the role of DAPK1 in neuronal cell death after stroke. We hope to provide exhaustive summaries of relevant studies on DAPK1 signals involved in stroke damage. Therefore, disrupting DAPK1-relevant cell death pathway could be considered as a promising therapeutic approach in stroke.
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a novel mechanism of spine damages in stroke via DAPK1 and tau
Cerebral Cortex, 2015Co-Authors: Shan Wang, Hao Li, Pei Pang, Linlin Bi, Xin Yang, Mengmeng Xu, Jianhua Wu, Tian Tian, Qing Tian, You ShangAbstract:Abstract Synaptic spine loss is one of the major preceding consequences of stroke damages, but its underlying molecular mechanisms remain unknown. Here, we report that a direct interaction of DAPK1 with Tau causes spine loss and subsequently neuronal death in a mouse model with stroke. We found that DAPK1 phosphorylates Tau protein at Ser262 (pS(262)) in cortical neurons of stroke mice. Either genetic deletion of DAPK1 kinase domain (KD) in mice (DAPK1-KD(-/-)) or blocking DAPK1-Tau interaction by systematic application of a membrane permeable peptide protects spine damages and improves neurological functions against stroke insults. Thus, disruption of DAPK1-Tau interaction is a promising strategy in clinical management of stroke.
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DAPK1 p53 interaction converges necrotic and apoptotic pathways of ischemic neuronal death
The Journal of Neuroscience, 2014Co-Authors: You Shang, Shan Wang, Yan Wu, Xiaoxi Wang, Youming LuAbstract:Necrosis and apoptosis are two distinct types of mechanisms that mediate ischemic injury. But a signaling point of convergence between them has yet to be identified. Here, we show that activated death-associated protein kinase 1 (DAPK1), phosphorylates p53 at serine-23 (pS23) via a direct binding of DAPK1 death domain (DAPK1DD) to the DNA binding motif of p53 (p53DM). We uncover that the pS23 acts as a functional version of p53 and mediates necrotic and apoptotic neuronal death; in the nucleus, pS23 induces the expression of proapoptotic genes, such as Bax, whereas in the mitochondrial matrix, pS23 triggers necrosis via interaction with cyclophilin D (CypD) in cultured cortical neurons from mice. Deletion of DAPK1DD (DAPK1DDΔ) or application of Tat-p53DM that interrupts DAPK1–p53 interaction blocks these dual pathways of pS23 actions in mouse cortical neurons. Thus, the DAPK1–p53 interaction is a signaling point of convergence of necrotic and apoptotic pathways and is a desirable target for the treatment of ischemic insults.
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DAPK1–p53 Interaction Converges Necrotic and Apoptotic Pathways of Ischemic Neuronal Death
The Journal of Neuroscience, 2014Co-Authors: You Shang, Shan Wang, Yan Wu, Xiaoxi WangAbstract:Necrosis and apoptosis are two distinct types of mechanisms that mediate ischemic injury. But a signaling point of convergence between them has yet to be identified. Here, we show that activated death-associated protein kinase 1 (DAPK1), phosphorylates p53 at serine-23 (pS23) via a direct binding of DAPK1 death domain (DAPK1DD) to the DNA binding motif of p53 (p53DM). We uncover that the pS23 acts as a functional version of p53 and mediates necrotic and apoptotic neuronal death; in the nucleus, pS23 induces the expression of proapoptotic genes, such as Bax, whereas in the mitochondrial matrix, pS23 triggers necrosis via interaction with cyclophilin D (CypD) in cultured cortical neurons from mice. Deletion of DAPK1DD (DAPK1DDΔ) or application of Tat-p53DM that interrupts DAPK1–p53 interaction blocks these dual pathways of pS23 actions in mouse cortical neurons. Thus, the DAPK1–p53 interaction is a signaling point of convergence of necrotic and apoptotic pathways and is a desirable target for the treatment of ischemic insults.
Xilong Xiao - One of the best experts on this subject based on the ideXlab platform.
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quinocetone triggered er stress induced autophagy via atf6 DAPK1 modulated matg9a trafficking
Cell Biology and Toxicology, 2016Co-Authors: Yan Zhou, Shen Zhang, Shusheng Tang, Xiayun Yang, Daowen Li, Kena Zhao, Xilong XiaoAbstract:The present study is undertaken to explore quinocetone-induced autophagy and its possible mechanism. Western blotting and green fluorescence protein (GFP)-LC3 vector transfection were performed to determine the ratio of LC3 conversion and its subcellular localization. Results revealed that the quinocetone induced autophagy in time- and dose-dependent manners. Besides, we tested the expressions of immunoglobulin heavy chain binding protein (BiP) and C/EBP homologous protein (CHOP) and the transcription of BiP, HerpUD, and sec24D by western blotting and RT-PCR, respectively. Results showed that quinocetone also induced endoplasmic reticulum (ER) stress during quinocetone-induced autophagy. Furthermore, we observed the cleavage of ATF6, the phosphorylation of MRLC, and the expression of death-associated protein kinase (DAPK1) by western blotting; the transcription of DAPK1 by RT-PCR; and the subcellular localization of ATF6 and mAtg9 by immunofluorescence. These results suggest that quinocetone stimulates the MRLC-mediated mAtg9 trafficking, which is critical for autophagosome formation, via the ATF6 upregulated expression of DAPK1. Last, we generated ATF6 and DAPK1 stable knockdown HepG2 cell lines and found that the conversion ratios of LC3 were decreased upon the treatment of quinocetone. Together, we propose that quinocetone induces autophagy through ER stress signaling pathway-induced cytoskeleton activation.
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Quinocetone triggered ER stress-induced autophagy via ATF6/DAPK1-modulated mAtg9a trafficking
Cell Biology and Toxicology, 2016Co-Authors: Yan Zhou, Shen Zhang, Shusheng Tang, Xiayun Yang, Daowen Li, Kena Zhao, Xilong XiaoAbstract:The present study is undertaken to explore quinocetone-induced autophagy and its possible mechanism. Western blotting and green fluorescence protein (GFP)-LC3 vector transfection were performed to determine the ratio of LC3 conversion and its subcellular localization. Results revealed that the quinocetone induced autophagy in time- and dose-dependent manners. Besides, we tested the expressions of immunoglobulin heavy chain binding protein (BiP) and C/EBP homologous protein (CHOP) and the transcription of BiP, HerpUD, and sec24D by western blotting and RT-PCR, respectively. Results showed that quinocetone also induced endoplasmic reticulum (ER) stress during quinocetone-induced autophagy. Furthermore, we observed the cleavage of ATF6, the phosphorylation of MRLC, and the expression of death-associated protein kinase (DAPK1) by western blotting; the transcription of DAPK1 by RT-PCR; and the subcellular localization of ATF6 and mAtg9 by immunofluorescence. These results suggest that quinocetone stimulates the MRLC-mediated mAtg9 trafficking, which is critical for autophagosome formation, via the ATF6 upregulated expression of DAPK1. Last, we generated ATF6 and DAPK1 stable knockdown HepG2 cell lines and found that the conversion ratios of LC3 were decreased upon the treatment of quinocetone. Together, we propose that quinocetone induces autophagy through ER stress signaling pathway-induced cytoskeleton activation.
Christopher C Oakes - One of the best experts on this subject based on the ideXlab platform.
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germline allele specific expression of DAPK1 in chronic lymphocytic leukemia
PLOS ONE, 2013Co-Authors: Rainer Claus, Thomas Hielscher, Daniel Mertens, Aparna Raval, Christopher C Oakes, Stephan M Tanner, Albert De La Chapelle, John C ByrdAbstract:We previously reported a rare germline variant (c.1-6531) that resulted in allele–specific expression (ASE) of death-associated protein kinase 1 (DAPK1) and predisposition to chronic lymphocytic leukemia (CLL). We investigated a cohort of CLL patients lacking this mutation for the presence of ASE of DAPK1. We developed a novel strategy that combines single-nucleotide primer extension (SNuPE) with MALDI-TOF mass spectrometry, and detected germline DAPK1 ASE in 17 out of 120 (14.2%) CLL patients associated with a trend towards younger age at diagnosis. ASE was absent in 63 healthy controls. Germline cells of CLL patients with ASE showed increased levels of DNA methylation in the promoter region, however, neither genetic nor further epigenetic aberrations could be identified in the DAPK1 5′ upstream regulatory region, within distinct exons or in the 3′-UTR. We identified B-lymphoid malignancy related cell line models harboring allelic imbalance and found that allele-specific methylation in DAPK1 is associated with ASE. Our data indicate that ASE at the DAPK1 gene locus is a recurrent event, mediated by epigenetic mechanisms and potentially predisposing to CLL.
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abstract b6 revealing DAPK1 transcriptional regulation by rna interference screening with an integrated bac reporter system
Cancer Research, 2009Co-Authors: Christopher C Oakes, Yoon Jung Park, Michael Boutros, Christoph PlassAbstract:High‐throughput RNA interference screening has been used successfully to reveal novel gene function. Currently used expression reporter systems employ small constructs of synthetic or endogenous sequences containing pathway‐specific response elements. The use of these small reporter systems does not allow for the recapitulation of the regulatory complexity that controls an individual gene of interest. Death‐associated protein kinase 1 (DAPK1) is a tumor suppressor gene that is silenced in a broad variety of cancers. Specifically, we have previously found DAPK1 to be silenced in virtually all cases of chronic lymphocytic leukemia and silencing is associated with promoter DNA methylation. Although epigenetic silencing is indicative of a transcriptional defect, the basis for this silencing is unknown. Here, we have employed a novel approach to elucidate genes involved in the transcriptional regulation of DAPK1. Using BAC recombineering and stable transgene integration, we have engineered human cells to express a DAPK1‐luciferase reporter under the control of approximately 180 Kb of sequence surrounding the DAPK1 transcriptional start site. By performing genome‐wide siRNA high‐throughout screening, we have been able to determine candidate genes involved in DAPK1 regulation. We have also performed screens in parallel using small, plasmid‐based promoter reporter constructs by transient transfection and stable integration. Evaluation of these reporter systems has revealed significant drawbacks of plasmid‐based reporters which include nonspecific effects arising from proximal vector backbone sequences. In conclusion, an integrated BAC‐reporter system is useful for the assessment of gene‐specific transcriptional regulation. Future work will involve determining the disease‐specific roles for novel DAPK1 regulatory genes. Citation Information: Cancer Res 2009;69(23 Suppl):B6.
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Abstract B6: Revealing DAPK1 transcriptional regulation by RNA interference screening with an integrated BAC‐reporter system
Cancer Research, 2009Co-Authors: Christopher C Oakes, Yoon Jung Park, Michael Boutros, Christoph PlassAbstract:High‐throughput RNA interference screening has been used successfully to reveal novel gene function. Currently used expression reporter systems employ small constructs of synthetic or endogenous sequences containing pathway‐specific response elements. The use of these small reporter systems does not allow for the recapitulation of the regulatory complexity that controls an individual gene of interest. Death‐associated protein kinase 1 (DAPK1) is a tumor suppressor gene that is silenced in a broad variety of cancers. Specifically, we have previously found DAPK1 to be silenced in virtually all cases of chronic lymphocytic leukemia and silencing is associated with promoter DNA methylation. Although epigenetic silencing is indicative of a transcriptional defect, the basis for this silencing is unknown. Here, we have employed a novel approach to elucidate genes involved in the transcriptional regulation of DAPK1. Using BAC recombineering and stable transgene integration, we have engineered human cells to express a DAPK1‐luciferase reporter under the control of approximately 180 Kb of sequence surrounding the DAPK1 transcriptional start site. By performing genome‐wide siRNA high‐throughout screening, we have been able to determine candidate genes involved in DAPK1 regulation. We have also performed screens in parallel using small, plasmid‐based promoter reporter constructs by transient transfection and stable integration. Evaluation of these reporter systems has revealed significant drawbacks of plasmid‐based reporters which include nonspecific effects arising from proximal vector backbone sequences. In conclusion, an integrated BAC‐reporter system is useful for the assessment of gene‐specific transcriptional regulation. Future work will involve determining the disease‐specific roles for novel DAPK1 regulatory genes. Citation Information: Cancer Res 2009;69(23 Suppl):B6.
