12 results on '"Keunhee Seo"'
Search Results
2. MON-2, a Golgi protein, mediates autophagy-dependent longevity in Caenorhabditis elegans
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Dongyeop Lee, Hyun-Jun Nam, Chanhee Kang, Jooyeon Sohn, Malene Hansen, Linnea M Adams, Yujin Lee, Eun Ji Kim, Seung-Yeol Park, Murat Artan, Dae-Eun Jeong, Dong Jin Moon, Wooseon Hwang, Seung-Jae Lee, Joo-Yeon Yoo, Mihwa Seo, Jeonghun Yeom, Yoonji Jung, Ozlem Altintas, Youngjae Ryu, Sang Ki Park, Cheolju Lee, Keunhee Seo, Sanguk Kim, Chang Man Ha, Seong Kyu Han, Nari Kim, Ara B. Hwang, and Sungeun Ju
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Multidisciplinary ,Physiology ,media_common.quotation_subject ,Autophagy ,Longevity ,SciAdv r-articles ,Life Sciences ,Biology ,biology.organism_classification ,Cell biology ,Biomedicine and Life Sciences ,Golgi protein ,Caenorhabditis elegans ,Research Article ,media_common - Abstract
Description, MON-2, which mediates Golgi-endosome trafficking, mediates mitochondrial inhibition–induced longevity by enhancing autophagy., The Golgi apparatus plays a central role in trafficking cargoes such as proteins and lipids. Defects in the Golgi apparatus lead to various diseases, but its role in organismal longevity is largely unknown. Using a quantitative proteomic approach, we found that a Golgi protein, MON-2, was up-regulated in long-lived Caenorhabditis elegans mutants with mitochondrial respiration defects and was required for their longevity. Similarly, we showed that DOP1/PAD-1, which acts with MON-2 to traffic macromolecules between the Golgi and endosome, contributed to the longevity of respiration mutants. Furthermore, we demonstrated that MON-2 was required for up-regulation of autophagy, a longevity-associated recycling process, by activating the Atg8 ortholog GABARAP/LGG-1 in C. elegans. Consistently, we showed that mammalian MON2 activated GABARAPL2 through physical interaction, which increased autophagic flux in mammalian cells. Thus, the evolutionarily conserved role of MON2 in trafficking between the Golgi and endosome is an integral part of autophagy-mediated longevity.
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- 2021
3. Prefoldin 6 mediates longevity response from heat shock factor 1 to FOXO in C. elegans
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Haeshim Baek, Eunseok Choi, Mihwa Seo, Chang Man Ha, Tae-Young Roh, Ao Lin Hsu, Sung Key Jang, Youngjae Ryu, Seon Woo A. An, Seokjin Ham, Seung-Jae Lee, Keunhee Seo, Yujin Lee, Heehwa G. Son, Eunju Kim, and Sangsoon Park
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Transcriptional Activation ,0301 basic medicine ,endocrine system ,media_common.quotation_subject ,Longevity ,03 medical and health sciences ,Subcutaneous Tissue ,0302 clinical medicine ,Heat shock protein ,Genetics ,Daf-16 ,Animals ,Insulin ,Insulin-Like Growth Factor I ,Caenorhabditis elegans ,Caenorhabditis elegans Proteins ,HSF1 ,Transcription factor ,media_common ,biology ,Forkhead Transcription Factors ,Prefoldin ,Cell biology ,Intestines ,030104 developmental biology ,Chaperone (protein) ,biology.protein ,Chaperone complex ,030217 neurology & neurosurgery ,Research Paper ,Molecular Chaperones ,Protein Binding ,Signal Transduction ,Transcription Factors ,Developmental Biology - Abstract
Heat shock factor 1 (HSF-1) and forkhead box O (FOXO) are key transcription factors that protect cells from various stresses. In Caenorhabditis elegans, HSF-1 and FOXO together promote a long life span when insulin/IGF-1 signaling (IIS) is reduced. However, it remains poorly understood how HSF-1 and FOXO cooperate to confer IIS-mediated longevity. Here, we show that prefoldin 6 (PFD-6), a component of the molecular chaperone prefoldin-like complex, relays longevity response from HSF-1 to FOXO under reduced IIS. We found that PFD-6 was specifically required for reduced IIS-mediated longevity by acting in the intestine and hypodermis. We showed that HSF-1 increased the levels of PFD-6 proteins, which in turn directly bound FOXO and enhanced its transcriptional activity. Our work suggests that the prefoldin-like chaperone complex mediates longevity response from HSF-1 to FOXO to increase the life span in animals with reduced IIS.
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- 2018
4. eIF2A, an initiator tRNA carrier refractory to eIF2α kinases, functions synergistically with eIF5B
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Eunah Kim, Joon Kim, Keunhee Seo, Sung Key Jang, Seung-Jae Lee, Junyoung Kwon, Seon Woo A. An, and Ka Young Hong
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0301 basic medicine ,RNA, Transfer, Met ,Blotting, Western ,Eukaryotic Initiation Factor-2 ,Ribosome ,03 medical and health sciences ,Cellular and Molecular Neuroscience ,eIF-2 Kinase ,Eukaryotic translation ,Eukaryotic initiation factor ,Evolution of initiator tRNA carriers ,Translation initiation ,P-site ,Animals ,Humans ,Eukaryotic Small Ribosomal Subunit ,eIF5B ,Amino Acid Sequence ,Eukaryotic Initiation Factors ,Caenorhabditis elegans ,Caenorhabditis elegans Proteins ,Molecular Biology ,Pharmacology ,eIF2 ,Sequence Homology, Amino Acid ,Chemistry ,Cell Biology ,Ribosomal RNA ,Cell biology ,030104 developmental biology ,HEK293 Cells ,Transfer RNA ,Mutation ,eIF2A ,Molecular Medicine ,Original Article ,RNA Interference ,Protein Binding - Abstract
The initiator tRNA (Met-tRNAiMet) at the P site of the small ribosomal subunit plays an important role in the recognition of an mRNA start codon. In bacteria, the initiator tRNA carrier, IF2, facilitates the positioning of Met-tRNAiMet on the small ribosomal subunit. Eukarya contain the Met-tRNAiMet carrier, eIF2 (unrelated to IF2), whose carrier activity is inhibited under stress conditions by the phosphorylation of its α-subunit by stress-activated eIF2α kinases. The stress-resistant initiator tRNA carrier, eIF2A, was recently uncovered and shown to load Met-tRNAiMet on the 40S ribosomal subunit associated with a stress-resistant mRNA under stress conditions. Here, we report that eIF2A interacts and functionally cooperates with eIF5B (a homolog of IF2), and we describe the functional domains of eIF2A that are required for its binding of Met-tRNAiMet, eIF5B, and a stress-resistant mRNA. The results indicate that the eukaryotic eIF5B–eIF2A complex functionally mimics the bacterial IF2 containing ribosome-, GTP-, and initiator tRNA-binding domains in a single polypeptide. Electronic supplementary material The online version of this article (10.1007/s00018-018-2870-4) contains supplementary material, which is available to authorized users.
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- 2018
5. SREBP and MDT-15 protect C. elegans from glucose-induced accelerated aging by preventing accumulation of saturated fat
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Hyunmin Kim, Youngsook Lee, Tae-Young Roh, Dongyeop Lee, Dae-Eun Jeong, Dae Won Moon, Yasuyo Yamaoka, Keunhee Seo, Heehwa G. Son, Abdul Aziz Khan, and Seung-Jae Lee
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Fatty Acid Desaturases ,endocrine system ,Aging ,Saturated fat ,Transcription factor complex ,digestive system ,Dietary Sucrose ,Genetics ,Animals ,Enzyme inducer ,Caenorhabditis elegans ,Caenorhabditis elegans Proteins ,Transcription factor ,Sterol Regulatory Element Binding Proteins ,chemistry.chemical_classification ,biology ,Fatty Acids ,food and beverages ,Gene Expression Regulation, Developmental ,biology.organism_classification ,Sterol ,Diet ,Sterol regulatory element-binding protein ,Glucose ,Enzyme ,chemistry ,Biochemistry ,Enzyme Induction ,biology.protein ,lipids (amino acids, peptides, and proteins) ,RNA Interference ,Genome-Wide Association Study ,Transcription Factors ,Research Paper ,Developmental Biology - Abstract
Glucose-rich diets shorten the life spans of various organisms. However, the metabolic processes involved in this phenomenon remain unknown. Here, we show that sterol regulatory element-binding protein (SREBP) and mediator-15 (MDT-15) prevent the life-shortening effects of a glucose-rich diet by regulating fat-converting processes in Caenorhabditis elegans. Up-regulation of the SREBP/MDT-15 transcription factor complex was necessary and sufficient for alleviating the life-shortening effect of a glucose-rich diet. Glucose feeding induced key enzymes that convert saturated fatty acids (SFAs) to unsaturated fatty acids (UFAs), which are regulated by SREBP and MDT-15. Furthermore, SREBP/MDT-15 reduced the levels of SFAs and moderated glucose toxicity on life span. Our study may help to develop strategies against elevated blood glucose and free fatty acids, which cause glucolipotoxicity in diabetic patients.
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- 2015
6. KIN-4/MAST kinase promotes PTEN-mediated longevity of Caenorhabditis elegans via binding through a PDZ domain
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Sanguk Kim, Eunji Kim, Wooseon Hwang, Joo-Yeon Yoo, Jae-Seong Yang, Seung-Jae Lee, Bo Kyoung Suh, Hyun-Jun Nam, Heehwa G. Son, Seon Woo A. An, Eunseok Choi, Sang Ki Park, Ikue Mori, Youngjae Ryu, Keunhee Seo, Youngran Kim, Shunji Nakano, Nhung Thi-Cam Nguyen, and Chang Man Ha
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0301 basic medicine ,Mutant ,PDZ domain ,Longevity ,KIN‐4/MAST kinase ,PDZ Domains ,03 medical and health sciences ,0302 clinical medicine ,PTEN ,Animals ,DAF‐18/PTEN ,PDZ ,Protein kinase A ,Caenorhabditis elegans ,Caenorhabditis elegans Proteins ,Original Paper ,biology ,Kinase ,aging ,PTEN Phosphohydrolase ,Cell Biology ,biology.organism_classification ,insulin/IGF‐1 signaling ,Original Papers ,Cell biology ,030104 developmental biology ,biology.protein ,Signal transduction ,030217 neurology & neurosurgery ,lifespan ,Genetic screen - Abstract
PDZ domain‐containing proteins (PDZ proteins) act as scaffolds for protein–protein interactions and are crucial for a variety of signal transduction processes. However, the role of PDZ proteins in organismal lifespan and aging remains poorly understood. Here, we demonstrate that KIN‐4, a PDZ domain‐containing microtubule‐associated serine‐threonine (MAST) protein kinase, is a key longevity factor acting through binding PTEN phosphatase in Caenorhabditis elegans. Through a targeted genetic screen for PDZ proteins, we find that kin‐4 is required for the long lifespan of daf‐2/insulin/IGF‐1 receptor mutants. We then show that neurons are crucial tissues for the longevity‐promoting role of kin‐4. We find that the PDZ domain of KIN‐4 binds PTEN, a key factor for the longevity of daf‐2 mutants. Moreover, the interaction between KIN‐4 and PTEN is essential for the extended lifespan of daf‐2 mutants. As many aspects of lifespan regulation in C. elegans are evolutionarily conserved, MAST family kinases may regulate aging and/or age‐related diseases in mammals through their interaction with PTEN.
- Published
- 2018
7. Mitochondrial chaperone HSP‐60 regulates anti‐bacterial immunity via p38 MAP kinase signaling
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Yujin Lee, Hyung-Jun Kim, Joo-Yeon Yoo, Heehwa G. Son, Mihwa Seo, Dongyeop Lee, Wooseon Hwang, Young Min Oh, Jay-Hyun Jo, Jee-Eun Lee, Sunyoung Hwang, Keunhee Seo, Ara B. Hwang, Seung-Jae Lee, Youngjae Ryu, Dae-Eun Jeong, Chang Man Ha, Murat Artan, and Haeshim Baek
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0301 basic medicine ,Cellular immunity ,MAP Kinase Kinase 4 ,MAP Kinase Signaling System ,MAPK7 ,MAP Kinase Kinase 3 ,Biology ,p38 Mitogen-Activated Protein Kinases ,General Biochemistry, Genetics and Molecular Biology ,MAP2K7 ,Animals, Genetically Modified ,Mitochondrial Proteins ,03 medical and health sciences ,0302 clinical medicine ,Animals ,Humans ,ASK1 ,Caenorhabditis elegans ,Caenorhabditis elegans Proteins ,Molecular Biology ,General Immunology and Microbiology ,MAP kinase kinase kinase ,General Neuroscience ,MAPKAPK2 ,Cyclin-dependent kinase 2 ,Articles ,Chaperonin 60 ,biochemical phenomena, metabolism, and nutrition ,Cell biology ,030104 developmental biology ,Pseudomonas aeruginosa ,biology.protein ,030217 neurology & neurosurgery - Abstract
Mitochondria play key roles in cellular immunity. How mitochondria contribute to organismal immunity remains poorly understood. Here, we show that HSP‐60/HSPD1, a major mitochondrial chaperone, boosts anti‐bacterial immunity through the up‐regulation of p38 MAP kinase signaling. We first identify 16 evolutionarily conserved mitochondrial components that affect the immunity of Caenorhabditis elegans against pathogenic Pseudomonas aeruginosa (PA14). Among them, the mitochondrial chaperone HSP‐60 is necessary and sufficient to increase resistance to PA14. We show that HSP‐60 in the intestine and neurons is crucial for the resistance to PA14. We then find that p38 MAP kinase signaling, an evolutionarily conserved anti‐bacterial immune pathway, is down‐regulated by genetic inhibition of hsp‐60 , and up‐regulated by increased expression of hsp‐60 . Overexpression of HSPD1 , the mammalian ortholog of hsp‐60 , increases p38 MAP kinase activity in human cells, suggesting an evolutionarily conserved mechanism. Further, cytosol‐localized HSP‐60 physically binds and stabilizes SEK‐1/MAP kinase kinase 3, which in turn up‐regulates p38 MAP kinase and increases immunity. Our study suggests that mitochondrial chaperones protect host eukaryotes from pathogenic bacteria by up‐regulating cytosolic p38 MAPK signaling. ![][1] The chaperone HSP‐60 binds and stabilizes SEK‐1/MAP kinase kinase to regulate p38 MAP kinase activity and anti‐bacterial immunity. The EMBO Journal (2017) 36: 1046–1065 [1]: /embed/graphic-1.gif
- Published
- 2017
8. RNA surveillance via nonsense-mediated mRNA decay is crucial forlongevity in daf-2/insulin/IGF-1 mutant C. elegans
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Tae-Young Roh, Seokjin Ham, Murat Artan, Wooseon Hwang, Chang Man Ha, Yoon Ki Kim, Mihwa Seo, Rachel N. Arey, Seon Woo A. An, Rachel Kaletsky, Heehwa G. Son, Coleen T. Murphy, Seung-Jae Lee, Hong Gil Nam, Youngjae Ryu, Keunhee Seo, and Dongyeop Lee
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0301 basic medicine ,media_common.quotation_subject ,Science ,Longevity ,Nonsense-mediated decay ,Mutant ,General Physics and Astronomy ,medicine.disease_cause ,Article ,General Biochemistry, Genetics and Molecular Biology ,Animals, Genetically Modified ,03 medical and health sciences ,Downregulation and upregulation ,medicine ,Animals ,Insulin ,RNA, Messenger ,Insulin-Like Growth Factor I ,Caenorhabditis elegans ,Caenorhabditis elegans Proteins ,media_common ,Genetics ,Mutation ,Multidisciplinary ,biology ,Gene Expression Profiling ,RNA ,General Chemistry ,biology.organism_classification ,Receptor, Insulin ,Nonsense Mediated mRNA Decay ,3. Good health ,Luminescent Proteins ,030104 developmental biology ,Daf-2 - Abstract
Long-lived organisms often feature more stringent protein and DNA quality control. However, whether RNA quality control mechanisms, such as nonsense-mediated mRNA decay (NMD), which degrades both abnormal as well as some normal transcripts, have a role in organismal aging remains unexplored. Here we show that NMD mediates longevity in C. elegans strains with mutations in daf-2/insulin/insulin-like growth factor 1 receptor. We find that daf-2 mutants display enhanced NMD activity and reduced levels of potentially aberrant transcripts. NMD components, including smg-2/UPF1, are required to achieve the longevity of several long-lived mutants, including daf-2 mutant worms. NMD in the nervous system of the animals is particularly important for RNA quality control to promote longevity. Furthermore, we find that downregulation of yars-2/tyrosyl-tRNA synthetase, an NMD target transcript, by daf-2 mutations contributes to longevity. We propose that NMD-mediated RNA surveillance is a crucial quality control process that contributes to longevity conferred by daf-2 mutations., The decline of DNA and protein quality control contributes to organismal ageing. Here, Son et al. report that nonsense-mediated mRNA decay, a RNA quality control mechanism, is enhanced in long-lived daf-2 mutant worms and contributes to their longevity by regulating expression of the yars-2/tyrosyl tRNA synthetase.
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- 2017
9. Heat shock factor 1 mediates the longevity conferred by inhibition of TOR and insulin/IGF-1 signaling pathways inC. elegans
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Dae-Eun Jeong, Keunhee Seo, Sung Key Jang, Seung-Jae Lee, Eunseok Choi, and Dongyeop Lee
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Aging ,media_common.quotation_subject ,Longevity ,Down-Regulation ,P70-S6 Kinase 1 ,Biology ,Mice ,Animals ,Insulin ,Insulin-Like Growth Factor I ,Caenorhabditis elegans ,Caenorhabditis elegans Proteins ,Protein Structure, Quaternary ,HSF1 ,Transcription factor ,media_common ,Genetics ,Ribosomal Protein S6 Kinases, 70-kDa ,Cell Biology ,biology.organism_classification ,Cell biology ,TOR signaling ,Oxidative Stress ,Phosphotransferases (Alcohol Group Acceptor) ,Ribosomal protein s6 ,Mutation ,Signal transduction ,Peptides ,Signal Transduction ,Transcription Factors - Abstract
Summary Target of rapamycin (TOR) signaling is an evolutionarily well-conserved pathway that regulates various physiologic processes, including aging and metabolism. One of the key downstream components of TOR signaling is ribosomal protein S6 kinase (S6K) whose inhibition extends the lifespan of yeast, Caenorhabditis elegans, Drosophila, and mice. Here, we demonstrate that the activation of heat shock factor 1 (HSF-1), a crucial longevity transcription factor known to act downstream of the insulin/IGF-1 signaling (IIS) pathway, mediates the prolonged lifespan conferred by mutations in C. elegans S6K (rsks-1). We found that hsf-1 is required for the longevity caused by down-regulation of components in TOR signaling pathways, including TOR and S6K. The induction of a small heat-shock protein hsp-16, a transcriptional target of HSF-1, mediates the long lifespan of rsks-1 mutants. Moreover, we show that synergistic activation of HSF-1 is required for the further enhanced longevity caused by simultaneous down-regulation of TOR and IIS pathways. Our findings suggest that HSF-1 acts as an essential longevity factor that intersects both IIS and TOR signaling pathways.
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- 2013
10. RNA helicase HEL-1 promotes longevity by specifically activating DAF-16/FOXO transcription factor signaling in Caenorhabditis elegans
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Seong Kyu Han, Hee Jung Koo, Daehee Hwang, Keunhee Seo, Jae-Seong Yang, Hong Gil Nam, Wooseon Hwang, Sanguk Kim, Sung Key Jang, Seung-Jae Lee, Yoontae Lee, Mihwa Seo, and Jeong-Hoon Hahm
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Longevity ,Molecular Sequence Data ,chemical and pharmacologic phenomena ,RNA interference ,Gene expression ,Animals ,Insulin ,RNA, Messenger ,Insulin-Like Growth Factor I ,Intestinal Mucosa ,Caenorhabditis elegans ,Caenorhabditis elegans Proteins ,Transcription factor ,Genes, Helminth ,Neurons ,Genetics ,Messenger RNA ,Multidisciplinary ,Base Sequence ,biology ,Sequence Analysis, RNA ,Gene Expression Profiling ,Reproduction ,Gene Expression Regulation, Developmental ,RNA ,Helicase ,Forkhead Transcription Factors ,biology.organism_classification ,RNA Helicase A ,Receptor, Insulin ,Up-Regulation ,PNAS Plus ,Gene Knockdown Techniques ,Mutation ,biology.protein ,RNA Interference ,RNA Helicases ,Protein Binding ,Signal Transduction - Abstract
The homeostatic maintenance of the genomic DNA is crucial for regulating aging processes. However, the role of RNA homeostasis in aging processes remains unknown. RNA helicases are a large family of enzymes that regulate the biogenesis and homeostasis of RNA. However, the functional significance of RNA helicases in aging has not been explored. Here, we report that a large fraction of RNA helicases regulate the lifespan of Caenorhabditis elegans. In particular, we show that a DEAD-box RNA helicase, helicase 1 (HEL-1), promotes longevity by specifically activating the DAF-16/forkhead box O (FOXO) transcription factor signaling pathway. We find that HEL-1 is required for the longevity conferred by reduced insulin/insulin-like growth factor 1 (IGF-1) signaling (IIS) and is sufficient for extending lifespan. We further show that the expression of HEL-1 in the intestine and neurons contributes to longevity. HEL-1 enhances the induction of a large fraction of DAF-16 target genes. Thus, the RNA helicase HEL-1 appears to promote longevity in response to decreased IIS as a transcription coregulator of DAF-16. Because HEL-1 and IIS are evolutionarily well conserved, a similar mechanism for longevity regulation via an RNA helicase-dependent regulation of FOXO signaling may operate in mammals, including humans.
- Published
- 2015
11. Genes and Pathways That Influence Longevity in Caenorhabditis elegans
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Ara B. Hwang, Murat Artan, Seon Woo A. An, Ozlem Altintas, Wooseon Hwang, Yujin Lee, Seung-Jae Lee, Dae-Eun Jeong, Keunhee Seo, Mihwa Seo, Heehwa G. Son, Dongyeop Lee, and Sangsoon Park
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Genetics ,biology ,ved/biology ,media_common.quotation_subject ,ved/biology.organism_classification_rank.species ,Autophagy ,Longevity ,Mitochondrion ,biology.organism_classification ,Hypoxia-inducible factors ,Reproductive system ,Model organism ,Gene ,Caenorhabditis elegans ,media_common - Abstract
The roundworm Caenorhabditis elegans is one of the most popular model organisms for research on aging because of its short lifespan and genetic tractability. Studies using C. elegans have identified many genes and pathways that regulate aging, several of which are conserved in other species, including mammals. In this chapter, we describe longevity-regulatory pathways including insulin/IGF-1 (insulin-like growth factor 1) signaling, TOR (target of rapamycin) signaling, autophagy, mitochondrial respiration, and HIF-1 (hypoxia-inducible factor 1) pathways. We also review the effects of dietary restriction, a key environmental factor that influences aging, on longevity-regulatory genetic factors. In addition, we illustrate the roles of two important C. elegans tissues, those of the sensory neural and reproductive systems, in regulating longevity at the molecular level. For each of the subtopics, we explain how changes in the expression of genes involved in each pathway and system alter longevity. We also speculate on the evolutionary significance of the genes and pathways that affect longevity. Given the conserved nature of longevity regulation, the dissection of the roles of these genetic factors in determining the C. elegans lifespan will provide important clues for understanding the secrets of human aging.
- Published
- 2015
12. RNA helicase HEL-1 promotes longevity by specifically activating DAF-16/FOXO transcription factor signaling in Caenorhabditis elegans.
- Author
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Mihwa Seo, Keunhee Seo, Wooseon Hwang, Hee Jung Koo, Jeong-Hoon Hahm, Jae-Seong Yang, Seong Kyu Han, Daehee Hwang, Sanguk Kim, Sung Key Jang, Yoontae Lee, Hong Gil Nam, and Lee, Seung-Jae V.
- Subjects
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CAENORHABDITIS elegans genetics , *GENETICS of aging , *RNA helicase , *LONGEVITY , *ORIGIN of life - Abstract
The homeostatic maintenance of the genomic DNA is crucial for regulating aging processes. However, the role of RNA homeostasis in aging processes remains unknown. RNA helicases are a large family of enzymes that regulate the biogenesis and homeostasis of RNA. However, the functional significance of RNA helicases in aging has not been explored. Here, we report that a large fraction of RNA helicases regulate the lifespan of Caenorhabditis elegans. In particular, we show that a DEAD-box RNA helicase, helicase 1 (HEL-1), promotes longevity by specifically activating the DAF-16/forkhead box O (FOXO) transcription factor signaling pathway. We find that HEL-1 is required for the longevity conferred by reduced insulin/insulin-like growth factor 1 (IGF-1) signaling (IIS) and is sufficient for extending lifespan. We further showthat the expression of HEL-1 in the intestine and neurons contributes to longevity. HEL-1 enhances the induction of a large fraction of DAF-16 target genes. Thus, the RNA helicase HEL-1 appears to promote longevity in response to decreased IIS as a transcription coregulator of DAF-16. Because HEL-1 and IIS are evolutionarily well conserved, a similar mechanism for longevity regulation via an RNA helicase-dependent regulation of FOXO signaling may operate in mammals, including humans. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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