Asymmetric Arginine Dimethylation Determines Life Span in C. elegans by Regulating Forkhead Transcription Factor DAF-16
Arginine methylation is a widespread posttranslational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). It is well established that PRMTs are implicated in various cellular processes, but their physiological roles remain unclear. Using nematodes with a l...
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| Veröffentlicht in: | Cell metabolism 2011-05, Vol.13 (5), p.505-516 |
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| creator | Takahashi, Yuta Daitoku, Hiroaki Hirota, Keiko Tamiya, Hiroko Yokoyama, Atsuko Kako, Koichiro Nagashima, Yusuke Nakamura, Ayumi Shimada, Takashi Watanabe, Satoshi Yamagata, Kazuyuki Yasuda, Kayo Ishii, Naoaki Fukamizu, Akiyoshi |
| description | Arginine methylation is a widespread posttranslational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). It is well established that PRMTs are implicated in various cellular processes, but their physiological roles remain unclear. Using nematodes with a loss-of-function mutation, we show that
prmt-1, the major asymmetric arginine methyltransferase, is a positive regulator of longevity in
C. elegans. This regulation is dependent on both its enzymatic activity and DAF-16/FoxO transcription factor, which is negatively regulated by AKT-mediated phosphorylation downstream of the DAF-2/insulin signaling.
prmt-1 is also required for stress tolerance and fat storage but not dauer formation in
daf-2 mutants. Biochemical analyses indicate that PRMT-1 methylates DAF-16, thereby blocking its phosphorylation by AKT. Disruption of PRMT-1 induces phosphorylation of DAF-16 with a concomitant reduction in the expression of longevity-related genes. Thus, we provide a mechanism by which asymmetric arginine dimethylation acts as an antiaging modification in
C. elegans.
► PRMT-1 is the predominant type I protein arginine methyltransferase in
C. elegans ► PRMT-1 controls life span depending on both DAF-16 and its enzymatic activity ► PRMT-1 is also involved in stress tolerance and fat storage, but not dauer arrest ► PRMT-1-induced methylation of DAF-16 blocks its phosphorylation by AKT |
| doi_str_mv | 10.1016/j.cmet.2011.03.017 |
| format | Article |
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prmt-1, the major asymmetric arginine methyltransferase, is a positive regulator of longevity in
C. elegans. This regulation is dependent on both its enzymatic activity and DAF-16/FoxO transcription factor, which is negatively regulated by AKT-mediated phosphorylation downstream of the DAF-2/insulin signaling.
prmt-1 is also required for stress tolerance and fat storage but not dauer formation in
daf-2 mutants. Biochemical analyses indicate that PRMT-1 methylates DAF-16, thereby blocking its phosphorylation by AKT. Disruption of PRMT-1 induces phosphorylation of DAF-16 with a concomitant reduction in the expression of longevity-related genes. Thus, we provide a mechanism by which asymmetric arginine dimethylation acts as an antiaging modification in
C. elegans.
► PRMT-1 is the predominant type I protein arginine methyltransferase in
C. elegans ► PRMT-1 controls life span depending on both DAF-16 and its enzymatic activity ► PRMT-1 is also involved in stress tolerance and fat storage, but not dauer arrest ► PRMT-1-induced methylation of DAF-16 blocks its phosphorylation by AKT</description><identifier>ISSN: 1550-4131</identifier><identifier>EISSN: 1932-7420</identifier><identifier>DOI: 10.1016/j.cmet.2011.03.017</identifier><identifier>PMID: 21531333</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>AKT protein ; Amino Acid Sequence ; Animals ; Arginine - genetics ; Arginine - metabolism ; Blotting, Western ; Caenorhabditis elegans ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - growth & development ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Forkhead Transcription Factors - genetics ; Forkhead Transcription Factors - metabolism ; Gene Expression Regulation ; Immunoprecipitation ; Insulin - genetics ; Insulin - metabolism ; Longevity - genetics ; Methylation ; Molecular Sequence Data ; Mutation - genetics ; Phosphorylation ; Polymerase Chain Reaction ; Protein-Arginine N-Methyltransferases - genetics ; Protein-Arginine N-Methyltransferases - metabolism ; Proto-Oncogene Proteins c-akt - genetics ; Proto-Oncogene Proteins c-akt - metabolism ; Receptor, Insulin - genetics ; Receptor, Insulin - metabolism ; Sequence Homology, Amino Acid ; Signal Transduction ; Transcription Factors - genetics ; Transcription Factors - metabolism</subject><ispartof>Cell metabolism, 2011-05, Vol.13 (5), p.505-516</ispartof><rights>2011 Elsevier Inc.</rights><rights>Copyright © 2011 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c498t-fa3af96222670c2f690a2f27f4172a68456258e56434dc6830b235326679369d3</citedby><cites>FETCH-LOGICAL-c498t-fa3af96222670c2f690a2f27f4172a68456258e56434dc6830b235326679369d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.cmet.2011.03.017$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21531333$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takahashi, Yuta</creatorcontrib><creatorcontrib>Daitoku, Hiroaki</creatorcontrib><creatorcontrib>Hirota, Keiko</creatorcontrib><creatorcontrib>Tamiya, Hiroko</creatorcontrib><creatorcontrib>Yokoyama, Atsuko</creatorcontrib><creatorcontrib>Kako, Koichiro</creatorcontrib><creatorcontrib>Nagashima, Yusuke</creatorcontrib><creatorcontrib>Nakamura, Ayumi</creatorcontrib><creatorcontrib>Shimada, Takashi</creatorcontrib><creatorcontrib>Watanabe, Satoshi</creatorcontrib><creatorcontrib>Yamagata, Kazuyuki</creatorcontrib><creatorcontrib>Yasuda, Kayo</creatorcontrib><creatorcontrib>Ishii, Naoaki</creatorcontrib><creatorcontrib>Fukamizu, Akiyoshi</creatorcontrib><title>Asymmetric Arginine Dimethylation Determines Life Span in C. elegans by Regulating Forkhead Transcription Factor DAF-16</title><title>Cell metabolism</title><addtitle>Cell Metab</addtitle><description>Arginine methylation is a widespread posttranslational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). It is well established that PRMTs are implicated in various cellular processes, but their physiological roles remain unclear. Using nematodes with a loss-of-function mutation, we show that
prmt-1, the major asymmetric arginine methyltransferase, is a positive regulator of longevity in
C. elegans. This regulation is dependent on both its enzymatic activity and DAF-16/FoxO transcription factor, which is negatively regulated by AKT-mediated phosphorylation downstream of the DAF-2/insulin signaling.
prmt-1 is also required for stress tolerance and fat storage but not dauer formation in
daf-2 mutants. Biochemical analyses indicate that PRMT-1 methylates DAF-16, thereby blocking its phosphorylation by AKT. Disruption of PRMT-1 induces phosphorylation of DAF-16 with a concomitant reduction in the expression of longevity-related genes. Thus, we provide a mechanism by which asymmetric arginine dimethylation acts as an antiaging modification in
C. elegans.
► PRMT-1 is the predominant type I protein arginine methyltransferase in
C. elegans ► PRMT-1 controls life span depending on both DAF-16 and its enzymatic activity ► PRMT-1 is also involved in stress tolerance and fat storage, but not dauer arrest ► PRMT-1-induced methylation of DAF-16 blocks its phosphorylation by AKT</description><subject>AKT protein</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Arginine - genetics</subject><subject>Arginine - metabolism</subject><subject>Blotting, Western</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - growth & development</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Forkhead Transcription Factors - genetics</subject><subject>Forkhead Transcription Factors - metabolism</subject><subject>Gene Expression Regulation</subject><subject>Immunoprecipitation</subject><subject>Insulin - genetics</subject><subject>Insulin - metabolism</subject><subject>Longevity - genetics</subject><subject>Methylation</subject><subject>Molecular Sequence Data</subject><subject>Mutation - genetics</subject><subject>Phosphorylation</subject><subject>Polymerase Chain Reaction</subject><subject>Protein-Arginine N-Methyltransferases - genetics</subject><subject>Protein-Arginine N-Methyltransferases - metabolism</subject><subject>Proto-Oncogene Proteins c-akt - genetics</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>Receptor, Insulin - genetics</subject><subject>Receptor, Insulin - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><issn>1550-4131</issn><issn>1932-7420</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1u2zAQRomgQf6aC2RRcNdupJAcipKAbAw7bgsYCNCma4KmRg5diXJIOahvk7PkZKHrtMusZjB831vwI-SKs5wzrq7Xue1xzAXjPGeQM14ekTNeg8hKKdiHtBcFyyQHfkrOY1wzBgpqOCGnghfAAeCM_JnEXZ8swVk6CSvnnUc6c-nysOvM6AZPZzhi6NM90oVrkf7cGE-dp9P85Rk7XBkf6XJHf-Bqu0_4FZ0P4fcDmobeh_Rog9v8Fc2NHYdAZ5N5xtVHctyaLuLl27wgv-a399Nv2eLu6_fpZJFZWVdj1howba2EEKpkVrSqZka0omwlL4VRlSyUKCoslATZWFUBWwooQChV1qDqBi7I54N3E4bHLcZR9y5a7DrjcdhGXSlZJrTiifzyLsll0ie6goSKA2rDEGPAVm-C603Yac70vhu91vtu9L4bzUCnblLo05t_u-yx-R_5V0YCbg4Apv94chh0tA69xcYFtKNuBvee_xU6jJ7f</recordid><startdate>20110504</startdate><enddate>20110504</enddate><creator>Takahashi, Yuta</creator><creator>Daitoku, Hiroaki</creator><creator>Hirota, Keiko</creator><creator>Tamiya, Hiroko</creator><creator>Yokoyama, Atsuko</creator><creator>Kako, Koichiro</creator><creator>Nagashima, Yusuke</creator><creator>Nakamura, Ayumi</creator><creator>Shimada, Takashi</creator><creator>Watanabe, Satoshi</creator><creator>Yamagata, Kazuyuki</creator><creator>Yasuda, Kayo</creator><creator>Ishii, Naoaki</creator><creator>Fukamizu, Akiyoshi</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20110504</creationdate><title>Asymmetric Arginine Dimethylation Determines Life Span in C. elegans by Regulating Forkhead Transcription Factor DAF-16</title><author>Takahashi, Yuta ; Daitoku, Hiroaki ; Hirota, Keiko ; Tamiya, Hiroko ; Yokoyama, Atsuko ; Kako, Koichiro ; Nagashima, Yusuke ; Nakamura, Ayumi ; Shimada, Takashi ; Watanabe, Satoshi ; Yamagata, Kazuyuki ; Yasuda, Kayo ; Ishii, Naoaki ; Fukamizu, Akiyoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c498t-fa3af96222670c2f690a2f27f4172a68456258e56434dc6830b235326679369d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>AKT protein</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Arginine - genetics</topic><topic>Arginine - metabolism</topic><topic>Blotting, Western</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans - growth & development</topic><topic>Caenorhabditis elegans - metabolism</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Forkhead Transcription Factors - genetics</topic><topic>Forkhead Transcription Factors - metabolism</topic><topic>Gene Expression Regulation</topic><topic>Immunoprecipitation</topic><topic>Insulin - genetics</topic><topic>Insulin - metabolism</topic><topic>Longevity - genetics</topic><topic>Methylation</topic><topic>Molecular Sequence Data</topic><topic>Mutation - genetics</topic><topic>Phosphorylation</topic><topic>Polymerase Chain Reaction</topic><topic>Protein-Arginine N-Methyltransferases - genetics</topic><topic>Protein-Arginine N-Methyltransferases - metabolism</topic><topic>Proto-Oncogene Proteins c-akt - genetics</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>Receptor, Insulin - genetics</topic><topic>Receptor, Insulin - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takahashi, Yuta</creatorcontrib><creatorcontrib>Daitoku, Hiroaki</creatorcontrib><creatorcontrib>Hirota, Keiko</creatorcontrib><creatorcontrib>Tamiya, Hiroko</creatorcontrib><creatorcontrib>Yokoyama, Atsuko</creatorcontrib><creatorcontrib>Kako, Koichiro</creatorcontrib><creatorcontrib>Nagashima, Yusuke</creatorcontrib><creatorcontrib>Nakamura, Ayumi</creatorcontrib><creatorcontrib>Shimada, Takashi</creatorcontrib><creatorcontrib>Watanabe, Satoshi</creatorcontrib><creatorcontrib>Yamagata, Kazuyuki</creatorcontrib><creatorcontrib>Yasuda, Kayo</creatorcontrib><creatorcontrib>Ishii, Naoaki</creatorcontrib><creatorcontrib>Fukamizu, Akiyoshi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell metabolism</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takahashi, Yuta</au><au>Daitoku, Hiroaki</au><au>Hirota, Keiko</au><au>Tamiya, Hiroko</au><au>Yokoyama, Atsuko</au><au>Kako, Koichiro</au><au>Nagashima, Yusuke</au><au>Nakamura, Ayumi</au><au>Shimada, Takashi</au><au>Watanabe, Satoshi</au><au>Yamagata, Kazuyuki</au><au>Yasuda, Kayo</au><au>Ishii, Naoaki</au><au>Fukamizu, Akiyoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Asymmetric Arginine Dimethylation Determines Life Span in C. elegans by Regulating Forkhead Transcription Factor DAF-16</atitle><jtitle>Cell metabolism</jtitle><addtitle>Cell Metab</addtitle><date>2011-05-04</date><risdate>2011</risdate><volume>13</volume><issue>5</issue><spage>505</spage><epage>516</epage><pages>505-516</pages><issn>1550-4131</issn><eissn>1932-7420</eissn><abstract>Arginine methylation is a widespread posttranslational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). It is well established that PRMTs are implicated in various cellular processes, but their physiological roles remain unclear. Using nematodes with a loss-of-function mutation, we show that
prmt-1, the major asymmetric arginine methyltransferase, is a positive regulator of longevity in
C. elegans. This regulation is dependent on both its enzymatic activity and DAF-16/FoxO transcription factor, which is negatively regulated by AKT-mediated phosphorylation downstream of the DAF-2/insulin signaling.
prmt-1 is also required for stress tolerance and fat storage but not dauer formation in
daf-2 mutants. Biochemical analyses indicate that PRMT-1 methylates DAF-16, thereby blocking its phosphorylation by AKT. Disruption of PRMT-1 induces phosphorylation of DAF-16 with a concomitant reduction in the expression of longevity-related genes. Thus, we provide a mechanism by which asymmetric arginine dimethylation acts as an antiaging modification in
C. elegans.
► PRMT-1 is the predominant type I protein arginine methyltransferase in
C. elegans ► PRMT-1 controls life span depending on both DAF-16 and its enzymatic activity ► PRMT-1 is also involved in stress tolerance and fat storage, but not dauer arrest ► PRMT-1-induced methylation of DAF-16 blocks its phosphorylation by AKT</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21531333</pmid><doi>10.1016/j.cmet.2011.03.017</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell metabolism, 2011-05, Vol.13 (5), p.505-516 |
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| source | MEDLINE; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present) |
| subjects | AKT protein Amino Acid Sequence Animals Arginine - genetics Arginine - metabolism Blotting, Western Caenorhabditis elegans Caenorhabditis elegans - genetics Caenorhabditis elegans - growth & development Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Forkhead Transcription Factors - genetics Forkhead Transcription Factors - metabolism Gene Expression Regulation Immunoprecipitation Insulin - genetics Insulin - metabolism Longevity - genetics Methylation Molecular Sequence Data Mutation - genetics Phosphorylation Polymerase Chain Reaction Protein-Arginine N-Methyltransferases - genetics Protein-Arginine N-Methyltransferases - metabolism Proto-Oncogene Proteins c-akt - genetics Proto-Oncogene Proteins c-akt - metabolism Receptor, Insulin - genetics Receptor, Insulin - metabolism Sequence Homology, Amino Acid Signal Transduction Transcription Factors - genetics Transcription Factors - metabolism |
| title | Asymmetric Arginine Dimethylation Determines Life Span in C. elegans by Regulating Forkhead Transcription Factor DAF-16 |
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