DAF-16/FOXO requires Protein Phosphatase 4 to initiate transcription of stress resistance and longevity promoting genes.

Aging / genetics Animals Caenorhabditis elegans / genetics Caenorhabditis elegans Proteins / genetics Chromosomal Proteins, Non-Histone / genetics Forkhead Transcription Factors / genetics Gene Expression Regulation / genetics Longevity / genetics Multiprotein Complexes / metabolism Phosphoprotein Phosphatases / genetics RNA Interference RNA Polymerase II / metabolism Stress, Physiological / genetics Transcription, Genetic / genetics Transcriptional Elongation Factors / genetics

Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
09 01 2020
Historique:
received: 09 12 2018
accepted: 09 12 2019
entrez: 11 1 2020
pubmed: 11 1 2020
medline: 25 3 2020
Statut: epublish

Résumé

In C. elegans, the conserved transcription factor DAF-16/FOXO is a powerful aging regulator, relaying dire conditions into expression of stress resistance and longevity promoting genes. For some of these functions, including low insulin/IGF signaling (IIS), DAF-16 depends on the protein SMK-1/SMEK, but how SMK-1 exerts this role has remained unknown. We show that SMK-1 functions as part of a specific Protein Phosphatase 4 complex (PP4

Identifiants

DOI: 10.1038/s41467-019-13931-7 PMID: 31919361 PMC: PMC6952425
pubmed: 31919361
doi: 10.1038/s41467-019-13931-7
pii: 10.1038/s41467-019-13931-7
pmc: PMC6952425
doi:

Substances chimiques

Caenorhabditis elegans Proteins 0
Chromosomal Proteins, Non-Histone 0
Forkhead Transcription Factors 0
Multiprotein Complexes 0
Transcriptional Elongation Factors 0
daf-16 protein, C elegans 0
SPT5 transcriptional elongation factor 138673-72-0
RNA Polymerase II EC 2.7.7.-
Phosphoprotein Phosphatases EC 3.1.3.16
SMK-1 protein, C elegans EC 3.1.3.16
protein phosphatase 4 EC 3.1.3.16

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

138

Références

Kimura, K. D., Tissenbaum, H. A., Liu, Y. & Ruvkun, G. daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans. Science 277, 942–946 (1997).
pubmed: 9252323 doi: 10.1126/science.277.5328.942
Tatar, M. et al. A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function. Science 292, 107–110 (2001).
pubmed: 11292875 doi: 10.1126/science.1057987
Kenyon, C., Chang, J., Gensch, E., Rudner, A. & Tabtiang, R. A. C. elegans mutant that lives twice as long as wild type. Nature 366, 461–464 (1993).
pubmed: 8247153 doi: 10.1038/366461a0
Lee, S. S., Kennedy, S., Tolonen, A. C. & Ruvkun, G. DAF-16 target genes that control C. elegans life-span and metabolism. Science 300, 644–647 (2003).
pubmed: 12690206 doi: 10.1126/science.1083614
Calnan, D. R. & Brunet, A. The FoxO code. Oncogene 27, 2276–2288 (2008).
pubmed: 18391970 doi: 10.1038/onc.2008.21
Murphy, C. T. et al. Genes that act downstream of DAF-16 to influence the lifespan of Caenorhabditis elegans. Nature 424, 277–283 (2003).
pubmed: 12845331 doi: 10.1038/nature01789
Lin, K., Hsin, H., Libina, N. & Kenyon, C. Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling. Nat. Genet. 28, 139–145 (2001).
pubmed: 11381260 doi: 10.1038/88850
Wolff, S. et al. SMK-1, an essential regulator of DAF-16-mediated longevity. Cell 124, 1039–1053 (2006).
pubmed: 16530049 doi: 10.1016/j.cell.2005.12.042
Gingras, A.-C. et al. A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity. Mol. Cell. Proteom. 4, 1725–1740 (2005).
doi: 10.1074/mcp.M500231-MCP200
Chowdhury, D. et al. A PP4-phosphatase complex dephosphorylates γ-H2AX generated during DNA replication. Mol. Cell 31, 33–46 (2008).
pubmed: 18614045 pmcid: 3242369 doi: 10.1016/j.molcel.2008.05.016
Chen, G. I. et al. PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4. J. Biol. Chem. 283, 29273–29284 (2008).
pubmed: 18715871 pmcid: 2662017 doi: 10.1074/jbc.M803443200
Janssens, V. & Goris, J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353, 417–439 (2001).
pubmed: 11171037 pmcid: 1221586 doi: 10.1042/bj3530417
Henderson, S. T. & Johnson, T. E. daf-16 integrates developmental and environmental inputs to mediate aging in the nematode Caenorhabditis elegans. Curr. Biol. 11, 1975–1980 (2001).
pubmed: 11747825 doi: 10.1016/S0960-9822(01)00594-2
Zhou, G. et al. Protein phosphatase 4 is involved in tumor necrosis factor-alpha-induced activation of c-Jun N-terminal kinase. J. Biol. Chem. 277, 6391–6398 (2002).
pubmed: 11698396 doi: 10.1074/jbc.M107014200
Sato-Carlton, A. et al. Protein phosphatase 4 promotes chromosome pairing and synapsis, and contributes to maintaining crossover competence with increasing age. PLoS Genet. 10, e1004638 (2014).
pubmed: 25340746 pmcid: 4207613 doi: 10.1371/journal.pgen.1004638
Stroustrup, N. et al. The Caenorhabditis elegans Lifespan Machine. Nat. Methods 10, 665–670 (2013).
pubmed: 23666410 pmcid: 3865717 doi: 10.1038/nmeth.2475
Riedel, C. G. et al. DAF-16 employs the chromatin remodeller SWI/SNF to promote stress resistance and longevity. Nat. Cell Biol. 15, 491–501 (2013).
pubmed: 23604319 pmcid: 3748955 doi: 10.1038/ncb2720
Lin, X.-X. et al. DAF-16/FOXO and HLH-30/TFEB function as combinatorial transcription factors to promote stress resistance and longevity. Nat. Commun. 9, 4400 (2018).
pubmed: 30353013 pmcid: 6199276 doi: 10.1038/s41467-018-06624-0
Maxwell, C. S. et al. Pol II docking and pausing at growth and stress genes in C. elegans. Cell Rep. 6, 455–466 (2014).
pubmed: 24485661 pmcid: 4026043 doi: 10.1016/j.celrep.2014.01.008
Baugh, L. R., Demodena, J. & Sternberg, P. W. RNA Pol II accumulates at promoters of growth genes during developmental arrest. Science 324, 92–94 (2009).
pubmed: 19251593 doi: 10.1126/science.1169628
Wade, J. T. & Struhl, K. The transition from transcriptional initiation to elongation. Curr. Opin. Genet. Dev. 18, 130–136 (2008).
pubmed: 18282700 pmcid: 2563432 doi: 10.1016/j.gde.2007.12.008
Garrido-Lecca, A. & Blumenthal, T. RNA polymerase II C-terminal domain phosphorylation patterns in caenorhabditis elegans operons, polycistronic gene clusters with only one promoter. Mol. Cell. Biol. 30, 3887–3893 (2010).
pubmed: 20498277 pmcid: 2916409 doi: 10.1128/MCB.00325-10
Chen, R. A. J. et al. The landscape of RNA polymerase II transcription initiation in C. elegans reveals promoter and enhancer architectures. Genome Res. 23, 1339–1347 (2013).
pubmed: 23550086 pmcid: 3730107 doi: 10.1101/gr.153668.112
Adelman, K. & Lis, J. T. Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans. Nat. Rev. Genet. 13, 720–731 (2012).
pubmed: 22986266 pmcid: 3552498 doi: 10.1038/nrg3293
Sacco, F. et al. Combining affinity proteomics and network context to identify new phosphatase substrates and adapters in growth pathways. Front. Genet. 5, 115 (2014).
pubmed: 24847354 pmcid: 4019850 doi: 10.3389/fgene.2014.00115
Kaplan, C. D., Morris, J. R., Wu, C. T. & Winston, F. Spt5 and Spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster. Genes Dev. 14, 2623–2634 (2000).
pubmed: 11040216 pmcid: 316994 doi: 10.1101/gad.831900
Kato, H. et al. Spt6 prevents transcription-coupled loss of posttranslationally modified histone H3. Sci. Rep. 3, 2186 (2013).
pubmed: 23851719 pmcid: 3711048 doi: 10.1038/srep02186
Ding, B., LeJeune, D. & Li, S. The C-terminal repeat domain of Spt5 plays an important role in suppression of Rad26-independent transcription coupled repair. J. Biol. Chem. 285, 5317–5326 (2010).
pubmed: 20042611 doi: 10.1074/jbc.M109.082818
Agostinis, P., Derua, R., Sarno, S., Goris, J. & Merlevede, W. Specificity of the polycation-stimulated (type-2A) and ATP,Mg-dependent (type-1) protein phosphatases toward substrates phosphorylated by P34cdc2 kinase. Eur. J. Biochem. 205, 241–248 (1992).
pubmed: 1313364 doi: 10.1111/j.1432-1033.1992.tb16774.x
Zhang, X. et al. Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4. Genes Dev. 19, 827–839 (2005).
pubmed: 15805470 pmcid: 1074320 doi: 10.1101/gad.1286005
Lee, D.-H. et al. A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. Nat. Struct. Mol. Biol. 17, 365–372 (2010).
pubmed: 20154705 pmcid: 3057140 doi: 10.1038/nsmb.1769
Hartzog, G. A. & Fu, J. The Spt4-Spt5 complex: A multi-faceted regulator of transcription elongation. Biochim. Biophys. Acta 1829, 105–115 (2013).
pubmed: 22982195 doi: 10.1016/j.bbagrm.2012.08.007
Pavri, R. et al. Activation-induced cytidine deaminase targets DNA at sites of RNA polymerase II stalling by interaction with Spt5. Cell 143, 122–133 (2010).
pubmed: 20887897 pmcid: 2993080 doi: 10.1016/j.cell.2010.09.017
Parua, P. K. et al. A Cdk9-PP1 switch regulates the elongation-termination transition of RNA polymerase II. Nature 558, 460–464 (2018).
pubmed: 29899453 pmcid: 6021199 doi: 10.1038/s41586-018-0214-z
Fitz, J., Neumann, T. & Pavri, R. Regulation of RNA polymerase II processivity by Spt5 is restricted to a narrow window during elongation. EMBO J. 37, e97965 (2018).
pubmed: 29514850 pmcid: 5897773 doi: 10.15252/embj.201797965
Diamant, G. et al. The elongation factor Spt5 facilitates transcription initiation for rapid induction of inflammatory-response genes. Nat. Commun. 7, 11547 (2016).
pubmed: 27180651 pmcid: 4873663 doi: 10.1038/ncomms11547
Grohmann, D. et al. The initiation factor TFE and the elongation factor Spt4/5 compete for the RNAP clamp during transcription initiation and elongation. Mol. Cell 43, 263–274 (2011).
pubmed: 21777815 pmcid: 3223566 doi: 10.1016/j.molcel.2011.05.030
Yamada, T. et al. P-TEFb-mediated phosphorylation of hSpt5 C-terminal repeats is critical for processive transcription elongation. Mol. Cell 21, 227–237 (2006).
pubmed: 16427012 doi: 10.1016/j.molcel.2005.11.024
Lu, X. et al. Multiple P-TEFbs cooperatively regulate the release of promoter-proximally paused RNA polymerase II. Nucleic Acids Res. 44, 6853–6867 (2016).
pubmed: 27353326 pmcid: 5001612 doi: 10.1093/nar/gkw571
Liu, Y. et al. Phosphorylation of the transcription elongation factor Spt5 by yeast Bur1 kinase stimulates recruitment of the PAF complex. Mol. Cell. Biol. 29, 4852–4863 (2009).
pubmed: 19581288 pmcid: 2725703 doi: 10.1128/MCB.00609-09
Guo, S. et al. A regulator of transcriptional elongation controls vertebrate neuronal development. Nature 408, 366–369 (2000).
pubmed: 11099044 doi: 10.1038/35042590
Jennings, B. H. et al. Locus-specific requirements for Spt5 in transcriptional activation and repression in Drosophila. Curr. Biol. 14, 1680–1684 (2004).
pubmed: 15380072 doi: 10.1016/j.cub.2004.08.066
Gaertner, B. & Zeitlinger, J. RNA polymerase II pausing during development. Development 141, 1179–1183 (2014).
pubmed: 24595285 pmcid: 3943177 doi: 10.1242/dev.088492
Hsu, A.-L., Murphy, C. T. & Kenyon, C. Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science 300, 1142–1145 (2003).
pubmed: 12750521 doi: 10.1126/science.1083701
Mahat, D. B., Salamanca, H. H., Duarte, F. M., Danko, C. G. & Lis, J. T. Mammalian heat shock response and mechanisms underlying its genome-wide transcriptional regulation. Mol. Cell 62, 63–78 (2016).
pubmed: 27052732 pmcid: 4826300 doi: 10.1016/j.molcel.2016.02.025
Ewald, C. Y., Landis, J. N., Porter Abate, J., Murphy, C. T. & Blackwell, T. K. Dauer-independent insulin/IGF-1-signalling implicates collagen remodelling in longevity. Nature 519, 97–101 (2015).
pubmed: 25517099 doi: 10.1038/nature14021
Panowski, S. H., Wolff, S., Aguilaniu, H., Durieux, J. & Dillin, A. PHA-4/Foxa mediates diet-restriction-induced longevity of C. elegans. Nature 447, 550–555 (2007).
pubmed: 17476212 doi: 10.1038/nature05837
Stiernagle, T. Maintenance of C. elegans. WormBook 1, 1–11 (2006).
Reboul, J. et al. C. elegans ORFeome version 1.1: experimental verification of the genome annotation and resource for proteomescale protein expression. Nat. Genet. 34, 35–41 (2003).
pubmed: 12679813 doi: 10.1038/ng1140
Kamath, R. S. et al. Systematic functional analysis of the Caenorhabditis elegans genome using RNAi. Nature 421, 231–237 (2003).
pubmed: 12529635 doi: 10.1038/nature01278
Kennedy, S., Wang, D. & Ruvkun, G. A conserved siRNA-degrading RNase negatively regulates RNA interference in C. elegans. Nature 427, 645–649 (2004).
pubmed: 14961122 doi: 10.1038/nature02302
Hamilton, B. et al. A systematic RNAi screen for longevity genes in C. elegans. Genes Dev. 19, 1544–1555 (2005).
pubmed: 15998808 pmcid: 1172061 doi: 10.1101/gad.1308205
Xu, T. et al. ProLuCID, a Fast and Sensitive Tandem Mass Spectra-based Protein Identification Program. Mol. Cell. Proteom. 5, S174 (2006).
Tabb, D. L., McDonald, W. H. & Yates, J. R. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1, 21–26 (2002).
pubmed: 12643522 pmcid: 2811961 doi: 10.1021/pr015504q
Frigola, J., Remus, D., Mehanna, A. & Diffley, J. F. X. ATPase-dependent quality control of DNA replication origin licensing. Nature 495, 339–343 (2013).
pubmed: 23474987 pmcid: 4825857 doi: 10.1038/nature11920
Kanno, T., Berta, D. G. & Sjögren, C. The Smc5/6 complex is an ATP-dependent intermolecular DNA Linker. Cell Rep. 12, 1471–1482 (2015).
pubmed: 26299966 doi: 10.1016/j.celrep.2015.07.048
Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367–1372 (2008).
pubmed: 19029910 doi: 10.1038/nbt.1511
Cox, J. et al. Andromeda: a peptide search engine integrated into the MaxQuant environment. J. Proteome Res. 10, 1794–1805 (2011).
pubmed: 21254760 doi: 10.1021/pr101065j
R Core Team. R: a language and environment for statistical computing. http://www.r-project.org/ (2013).
Ritchie, M. E. et al. limma powers differential expression analyses for RNA-sequencing and microarray studies. Nucleic Acids Res. 43, e47 (2015).
pubmed: 25605792 pmcid: 4402510 doi: 10.1093/nar/gkv007
Bowman, S. K. et al. Multiplexed Illumina sequencing libraries from picogram quantities of DNA. BMC Genom. 14, 466 (2013).
doi: 10.1186/1471-2164-14-466
Trapnell, C., Pachter, L. & Salzberg, S. L. TopHat: discovering splice junctions with RNA-Seq. Bioinformatics 25, 1105–1111 (2009).
pubmed: 19289445 pmcid: 2672628
Trapnell, C. et al. Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation. Nat. Biotechnol. 28, 511–515 (2010).
pubmed: 20436464 pmcid: 3146043 doi: 10.1038/nbt.1621
Langmead, B., Trapnell, C., Pop, M. & Salzberg, S. L. Ultrafast and memory-efficient alignment of short DNA sequences to the human genome. Genome Biol. 10, R25 (2009).
pubmed: 19261174 pmcid: 2690996 doi: 10.1186/gb-2009-10-3-r25
Shen, L., Shao, N., Liu, X. & Nestler, E. ngs.plot: Quick mining and visualization of next-generation sequencing data by integrating genomic databases. BMC Genom. 15, 284 (2014).
doi: 10.1186/1471-2164-15-284
Whyte, Wa et al. Enhancer decommissioning by LSD1 during embryonic stem cell differentiation. Nature 482, 221–225 (2012).
pubmed: 22297846 pmcid: 4144424 doi: 10.1038/nature10805
Ramírez, F. et al. deepTools2: a next generation web server for deep-sequencing data analysis. Nucleic Acids Res. 44, W160–W165 (2016).
pubmed: 27079975 pmcid: 4987876 doi: 10.1093/nar/gkw257
Huang, D. W., Sherman, B. T. & Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44–57 (2009).
doi: 10.1038/nprot.2008.211
Yang, J.-S. et al. OASIS: online application for the survival analysis of lifespan assays performed in aging research. PLoS ONE 6, e23525 (2011).
pubmed: 21858155 pmcid: 3156233 doi: 10.1371/journal.pone.0023525

Auteurs

Ilke Sen (I)

Integrated Cardio Metabolic Centre (ICMC), Department of Medicine, Karolinska Institute, Blickagången 6, 14157, Huddinge, Sweden.
Department of Biosciences and Nutrition, Karolinska Institute, Blickagången 16, 14157, Huddinge, Sweden.
European Research Institute for the Biology of Ageing (ERIBA), University Medical Center Groningen (UMCG), University of Groningen, Antonius Deusinglaan, 1, 9713AV, Groningen, The Netherlands.

Xin Zhou (X)

Integrated Cardio Metabolic Centre (ICMC), Department of Medicine, Karolinska Institute, Blickagången 6, 14157, Huddinge, Sweden.
Department of Biosciences and Nutrition, Karolinska Institute, Blickagången 16, 14157, Huddinge, Sweden.
ORCID: 0000-0002-3917-5516

Alexey Chernobrovkin (A)

Department of Medical Biochemistry and Biophysics, Karolinska Institute, Solnavägen 9, 17165, Solna, Sweden.

Nataly Puerta-Cavanzo (N)

European Research Institute for the Biology of Ageing (ERIBA), University Medical Center Groningen (UMCG), University of Groningen, Antonius Deusinglaan, 1, 9713AV, Groningen, The Netherlands.
ORCID: 0000-0002-3905-4861

Takaharu Kanno (T)

Department of Biosciences and Nutrition, Karolinska Institute, Blickagången 16, 14157, Huddinge, Sweden.
Department of Cellular and Molecular Biology, Karolinska Institute, Solnavägen 9, 17165, Solna, Sweden.

Jérôme Salignon (J)

Integrated Cardio Metabolic Centre (ICMC), Department of Medicine, Karolinska Institute, Blickagången 6, 14157, Huddinge, Sweden.
Department of Biosciences and Nutrition, Karolinska Institute, Blickagången 16, 14157, Huddinge, Sweden.

Andrea Stoehr (A)

Integrated Cardio Metabolic Centre (ICMC), Department of Medicine, Karolinska Institute, Blickagången 6, 14157, Huddinge, Sweden.
Department of Biosciences and Nutrition, Karolinska Institute, Blickagången 16, 14157, Huddinge, Sweden.
ORCID: 0000-0003-3573-1818

Xin-Xuan Lin (XX)

Integrated Cardio Metabolic Centre (ICMC), Department of Medicine, Karolinska Institute, Blickagången 6, 14157, Huddinge, Sweden.
Department of Biosciences and Nutrition, Karolinska Institute, Blickagången 16, 14157, Huddinge, Sweden.

Bora Baskaner (B)

Integrated Cardio Metabolic Centre (ICMC), Department of Medicine, Karolinska Institute, Blickagången 6, 14157, Huddinge, Sweden.

Simone Brandenburg (S)

European Research Institute for the Biology of Ageing (ERIBA), University Medical Center Groningen (UMCG), University of Groningen, Antonius Deusinglaan, 1, 9713AV, Groningen, The Netherlands.

Camilla Björkegren (C)

Department of Biosciences and Nutrition, Karolinska Institute, Blickagången 16, 14157, Huddinge, Sweden.
Department of Cellular and Molecular Biology, Karolinska Institute, Solnavägen 9, 17165, Solna, Sweden.
ORCID: 0000-0001-7354-9270

Roman A Zubarev (RA)

Department of Medical Biochemistry and Biophysics, Karolinska Institute, Solnavägen 9, 17165, Solna, Sweden.

Christian G Riedel (CG)

Integrated Cardio Metabolic Centre (ICMC), Department of Medicine, Karolinska Institute, Blickagången 6, 14157, Huddinge, Sweden. christian.riedel@ki.se.
Department of Biosciences and Nutrition, Karolinska Institute, Blickagången 16, 14157, Huddinge, Sweden. christian.riedel@ki.se.
European Research Institute for the Biology of Ageing (ERIBA), University Medical Center Groningen (UMCG), University of Groningen, Antonius Deusinglaan, 1, 9713AV, Groningen, The Netherlands. christian.riedel@ki.se.
ORCID: 0000-0002-3689-8022

Articles similaires

Evaluating the efficacy of telesurgery with dual console SSI Mantra Surgical Robotic System: experiment on animal model and clinical trials.

Sudhir Prem Srivastava, Vishwajyoti Pascual Srivastava, Avinesh Singh et al.
1.00
Robotic Surgical Procedures Animals Humans Telemedicine Models, Animal

Odour generalisation and detection dog training.

Lyn Caldicott, Thomas W Pike, Helen E Zulch et al.
1.00
Animals Odorants Dogs Generalization, Psychological Smell

FBXO22 inhibits colitis and colorectal carcinogenesis by regulating the degradation of the S2448-phosphorylated form of mTOR.

Minle Li, Xuan Chen, Pengfei Qu et al.
1.00
Animals TOR Serine-Threonine Kinases Colorectal Neoplasms Colitis Mice

Use of organic material provided by an automatic enrichment device by weaner pigs and its influence on tail lesions.

Philipp Heseker, Jeanette Probst, Stefanie Ammer et al.
1.00
Animals Tail Swine Behavior, Animal Animal Husbandry

Classifications MeSH

questionsmedicales.fr › Phénomènes physiologiques › Croissance et développement › Vieillissement › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Eucaryotes › Animaux › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Eucaryotes › Animaux › Invertébrés › Helminthes › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Caenorhabditis › Caenorhabditis elegans › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines d'helminthes › Protéines de Caenorhabditis elegans › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Nucléoprotéines › Protéines chromosomiques nonhistones › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Facteurs de transcription à motif hélice ailée › Facteurs de transcription Forkhead › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Phénomènes physiologiques › Longévité › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Structures macromoléculaires › Complexes multiprotéiques › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Phosphoprotein Phosphatases › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Épigenèse génétique › Extinction de l'expression des gènes › Interférence par ARN › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Phosphotransferases › Nucleotidyltransferases › RNA nucleotidyltransferases › DNA-directed RNA polymerases › RNA polymerase II › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Phénomènes physiologiques › Stress physiologique › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Phénomènes génétiques › Expression des gènes › Transcription génétique › DAF-16/FOXO requires Protein Phosphatase 4 to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Facteurs d'élongation transcriptionnelle › DAF-16/FOXO requires Protein Phosphatase 4 to...