CNBP regulates wing development in Drosophila melanogaster by promoting IRES-dependent translation of dMyc

Cell Cycle

Volumn 13, Issue 3, 2014, Pages 434-439

  Antonucci, Laura ^a,b   D'Amico, Davide ^a   Di Magno, Laura ^a,b   Coni, Sonia ^b,c   Di Marcotullio, Lucia ^a   Cardinali, Beatrice ^d   Gulino, Alberto ^a,b,e,f   Ciapponi, Laura ^g   Canettieri, Gianluca ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b Pasteur Institute   (Italy)

^c INSERM   (France)

^d CNR   (Italy)

^e IRCCS NEUROMED   (Italy)

^f ISTITUTO ITALIANO DI TECNOLOGIA   (Italy)

^g SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

CNBP; Development; dMyc; Drosophila; Oncogene

Indexed keywords

CCHC TYPE ZINC FINGER NUCLEIC ACID BINDING PROTEIN; DROSOPHILA PROTEIN; MESSENGER RNA; MYC PROTEIN; NUCLEIC ACID BINDING PROTEIN; UNCLASSIFIED DRUG; CNBP PROTEIN, DROSOPHILA; DIMINUTIVE PROTEIN, DROSOPHILA; DNA BINDING PROTEIN; RNA BINDING PROTEIN; TRANSCRIPTION FACTOR;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; EMBRYO DEVELOPMENT; ESSENTIAL GENE; FORELIMB; GENE EXPRESSION; GENE SILENCING; IMAGINAL DISC; INTERNAL RIBOSOME ENTRY SITE; LETHALITY; LIMB DEVELOPMENT; NONHUMAN; ORGAN SIZE; PROTEIN FUNCTION; PROTEIN STRUCTURE; RNA TRANSLATION; SIGNAL TRANSDUCTION; TRANSLATION REGULATION; AMINO ACID SEQUENCE; ANIMAL; GENETICS; GROWTH, DEVELOPMENT AND AGING; HEK293 CELL LINE; HUMAN; LARVA; METABOLISM; MOLECULAR GENETICS; POLYSOME;

AMINO ACID SEQUENCE; ANIMALS; DNA-BINDING PROTEINS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; HEK293 CELLS; HUMANS; LARVA; MOLECULAR SEQUENCE DATA; POLYRIBOSOMES; RNA-BINDING PROTEINS; TRANSCRIPTION FACTORS; WING;

EID: 84896873986     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.27268     Document Type: Article

References (23)

1. Calcaterra NB, Armas P, Weiner AM, Borgognone M. CNBP: a multifunctional nucleic acid chaperone involved in cell death and proliferation control. IUBMB Life 2010; 62:707-14; PMID:20960530; http://dx.doi.org/10.1002/iub.379
2. Armas P, Agüero TH, Borgognone M, Aybar MJ, Calcaterra NB. Dissecting CNBP, a zinc-finger protein required for neural crest development, in its structural and functional domains. J Mol Biol 2008; 382:1043-56; PMID:18703071; http://dx.doi.org/10.1016/j.jmb.2008.07.079
3. Armas P, Nasif S, Calcaterra NB. Cellular nucleic acid binding protein binds G-rich single-stranded nucleic acids and may function as a nucleic acid chaperone. J Cell Biochem 2008; 103:1013-36; PMID:17661353; http://dx.doi.org/ 10.1002/jcb.21474
4. Rajavashisth TB, Taylor AK, Andalibi A, Svenson KL, Lusis AJ. Identification of a zinc finger protein that binds to the sterol regulatory element. Science 1989; 245:640-3; PMID:2562787; http://dx.doi.org/10.1126/ science.2562787
5. Flink IL, Morkin E. Alternatively processed isoforms of cellular nucleic acid-binding protein interact with a suppressor region of the human beta-myosin heavy chain gene. J Biol Chem 1995; 270:6959-65; PMID:7896846; http://dx.doi.org/10.1074/jbc.270.12.6959
6. Konicek BW, Xia X, Rajavashisth T, Harrington MA. Regulation of mouse colony-stimulating factor-1 gene promoter activity by AP1 and cellular nucleic acid-binding protein. DNA Cell Biol 1998; 17:799-809; PMID:9778039; http://dx.doi.org/10.1089/dna.1998.17.799
7. Michelotti EF, Tomonaga T, Krutzsch H, Levens D. Cellular nucleic acid binding protein regulates the CT element of the human c-myc protooncogene. J Biol Chem 1995; 270:9494-9; PMID:7721877; http://dx.doi.org/10.1074/jbc.270.16. 9494
8. Schlatter S, Fussenegger M. Novel CNBP- and La-based translation control systems for mammalian cells. Biotechnol Bioeng 2003; 81:1-12; PMID:12432575; http://dx.doi.org/10.1002/bit.10549
9. Huichalaf C, Schoser B, Schneider-Gold C, Jin B, Sarkar P, Timchenko L. Reduction of the rate of protein translation in patients with myotonic dystrophy 2. J Neurosci 2009; 29:9042-9; PMID:19605641; http://dx.doi.org/10.1523/ JNEUROSCI.1983-09.2009
10. Gerbasi VR, Link AJ. The myotonic dystrophy type 2 protein ZNF9 is part of an ITAF complex that promotes cap-independent translation. Mol Cell Proteomics 2007; 6:1049-58; PMID:17327219; http://dx.doi.org/10.1074/mcp. M600384-MCP200
11. Sammons MA, Antons AK, Bendjennat M, Udd B, Krahe R, Link AJ. ZNF9 activation of IRES-mediated translation of the human ODC mRNA is decreased in myotonic dystrophy type 2. PLoS One 2010; 5:e9301; PMID:20174632; http://dx.doi.org/10.1371/journal.pone.0009301
12. Sammons MA, Samir P, Link AJ. Saccharomyces cerevisiae Gis2 interacts with the translation machinery and is orthogonal to myotonic dystrophy type 2 protein ZNF9. Biochem Biophys Res Commun 2011; 406:13-9; PMID:21277287; http://dx.doi.org/10.1016/j.bbrc.2011.01.086
13. Liquori CL, Ricker K, Moseley ML, Jacobsen JF, Kress W, Naylor SL, Day JW, Ranum LP. Myotonic dystrophy type 2 caused by a CCTG expansion in intron 1 of ZNF9. Science 2001; 293:864-7; PMID:11486088; http://dx.doi.org/10.1126/ science.1062125
14. Chen W, Liang Y, Deng W, Shimizu K, Ashique AM, Li E, Li YP. The zinc-finger protein CNBP is required for forebrain formation in the mouse. Development 2003; 130:1367-79; PMID:12588852; http://dx.doi.org/10.1242/dev. 00349
15. Abe Y, Chen W, Huang W, Nishino M, Li YP. CNBP regulates forebrain formation at organogenesis stage in chick embryos. Dev Biol 2006; 295:116-27; PMID:16626683; http://dx.doi.org/10.1016/j.ydbio.2006.03.012
16. Weiner AM, Allende ML, Becker TS, Calcaterra NB. CNBP mediates neural crest cell expansion by controlling cell proliferation and cell survival during rostral head development. J Cell Biochem 2007; 102:1553-70; PMID:17471504; http://dx.doi.org/10.1002/jcb.21380
17. Stoneley M, Paulin FE, Le Quesne JP, Chappell SA, Willis AE. C-Myc 5′ untranslated region contains an internal ribosome entry segment. Oncogene 1998; 16:423-8; PMID:9467968; http://dx.doi.org/10.1038/sj.onc.1201763
18. Baird SD, Turcotte M, Korneluk RG, Holcik M. Searching for IRES. RNA 2006; 12:1755-85; PMID:16957278; http://dx.doi.org/10.1261/rna.157806
19. Wu DC, Johnston LA. Control of wing size and proportions by Drosophila myc. Genetics 2010; 184:199-211; PMID:19897747; http://dx.doi.org/10.1534/ genetics.109.110379
20. Créancier L, Mercier P, Prats AC, Morello D. c-myc Internal ribosome entry site activity is developmentally controlled and subjected to a strong translational repression in adult transgenic mice. Mol Cell Biol 2001; 21:1833-40; PMID:11238920; http://dx.doi.org/10.1128/MCB.21.5.1833-1840.2001
21. Canettieri G, Di Marcotullio L, Greco A, Coni S, Antonucci L, Infante P, Pietrosanti L, De Smaele E, Ferretti E, Miele E, et al. Histone deacetylase and Cullin3-REN(KCTD11) ubiquitin ligase interplay regulates Hedgehog signalling through Gli acetylation. Nat Cell Biol 2010; 12:132-42; PMID:20081843; http://dx.doi.org/10.1038/ncb2013
22. Canettieri G, Coni S, Della Guardia M, Nocerino V, Antonucci L, Di Magno L, Screaton R, Screpanti I, Giannini G, Gulino A. The coactivator CRTC1 promotes cell proliferation and transformation via AP-1. Proc Natl Acad Sci USA 2009; 106:1445-50; PMID:19164581; http://dx.doi.org/10.1073/pnas.0808749106
23. Cardinali B, Carissimi C, Gravina P, Pierandrei-Amaldi P. La protein is associated with terminal oligopyrimidine mRNAs in actively translating polysomes. J Biol Chem 2003; 278:35145-51; PMID:12840030; http://dx.doi.org/10. 1074/jbc.M300722200