, Le projet de l'équipe Infection et devenir de l'ARN porte sur l'étude des régulations posttranscriptionnelles affectant l'expression génique des cellules épithéliales humaines, lors de l'infection par Listeria monocytogenes

, L'infection s'accompagne-t-elle de dégradations globales ou spécifiques des ARNm cellulaires ? 2. La traduction des ARNm est-elle affectée par l'infection ?

, Quels mécanismes moléculaires de la bactérie ou de l'hôte sont impliqués dans ces processus ? 4. Quelles en sont les conséquences sur la viabilité cellulaire ou la prolifération bactérienne ?

F. Allerberger and M. Wagner, Listeriosis: a resurgent foodborne infection, Clin Microbiol Infect, vol.16, pp.16-23, 2010.

C. Allmang, J. Kufel, G. Chanfreau, P. Mitchell, E. Petfalski et al., Functions of the exosome in rRNA, snoRNA and snRNA synthesis, EMBO J, vol.18, pp.5399-5410, 1999.

J. S. Anderson and R. Parker, The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3" to 5" exonucleases of the exosome complex, EMBO J, vol.17, pp.1497-1506, 1998.

C. Archambaud, M. Nahori, G. Soubigou, C. Bécavin, L. Laval et al., Impact of lactobacilli on orally acquired listeriosis, Proc Natl Acad Sci, vol.109, pp.16684-16689, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01003361

C. Archambaud, O. Sismeiro, J. Toedling, G. Soubigou, C. Bécavin et al., The intestinal microbiota interferes with the microRNA response upon oral Listeria infection, MBio, vol.4, pp.707-720, 2013.
URL : https://hal.archives-ouvertes.fr/hal-01350904

K. Armache, J. D. Garlick, D. Canzio, G. J. Narlikar, and R. E. Kingston, Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution, Science, vol.334, pp.977-982, 2011.

A. Ben-shem, L. Jenner, G. Yusupova, and M. Yusupov, Crystal structure of the eukaryotic ribosome, Science, vol.330, pp.1203-1209, 2010.

H. Bierne, M. A. Hamon, and P. Cossart, Epigenetics and bacterial infections, Cold Spring Harb Perspect Med, vol.2, pp.10272-010272, 2012.

H. Bierne, T. N. Tham, E. Batsche, A. Dumay, M. Leguillou et al., Human BAHD1 promotes heterochromatic gene silencing, Proc Natl Acad Sci, vol.106, pp.13826-13831, 2009.
URL : https://hal.archives-ouvertes.fr/pasteur-00411478

H. Bierne, L. Travier, T. Mahlakõiv, L. Tailleux, A. Subtil et al., Activation of type III interferon genes by pathogenic bacteria in infected epithelial cells and mouse placenta, PLoS ONE, vol.7, p.39080, 2012.
URL : https://hal.archives-ouvertes.fr/pasteur-00750162

B. Bradatsch, C. Leidig, S. Granneman, M. Gnädig, D. Tollervey et al., Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel, Nat Struct Mol Biol, vol.19, pp.1234-1241, 2012.

I. Callebaut, J. C. Courvalin, and J. P. Mornon, The BAH (bromo-adjacent homology) domain: a link between DNA methylation, replication and transcriptional regulation, FEBS Lett, vol.446, pp.189-193, 1999.

J. Colin, D. Libri, and O. Porrua, Cryptic transcription and early termination in the control of gene expression, Genet Res Int, pp.653494-653504, 2011.

J. Copp, M. Marino, M. Banerjee, P. Ghosh, and P. Van-der-geer, Multiple regions of internalin B contribute to its ability to turn on the Ras-mitogenactivated protein kinase pathway, J Biol Chem, vol.278, pp.7783-7789, 2003.

P. Cossart, Illuminating the landscape of hostpathogen interactions with the bacterium Listeria monocytogenes, Proc Natl Acad Sci, vol.108, pp.19484-19491, 2011.

P. Cossart and A. Lebreton, A trip in the "New Microbiology" with the bacterial pathogen Listeria monocytogenes, FEBS Lett, vol.588, pp.2437-2445, 2014.
URL : https://hal.archives-ouvertes.fr/pasteur-01161887

S. I. De-azevedo-wäsch, J. R. Van-der-ploeg, M. T. Lebreton, A. Kiener, A. Leisinger et al., Transformation of isopropylamine to L-alaninol by Pseudomonas sp. strain KIE171 involves Nglutamylated intermediates, Appl Environ Microbiol, vol.68, pp.2368-2375, 2002.

T. Decker, M. Muller, and S. Stockinger, The yin and yang of type I interferon activity in bacterial infection, Nat Rev Immunol, vol.5, pp.675-687, 2005.

E. Demoinet, A. Jacquier, G. Lutfalla, and M. Fromont-racine, The Hsp40 chaperone Jjj1 is required for the nucleo-cytoplasmic recycling of preribosomal factors in Saccharomyces cerevisiae, RNA, vol.13, pp.1570-1581, 2007.
URL : https://hal.archives-ouvertes.fr/hal-00167448

Z. Ding, L. L. Gillespie, F. C. Mercer, and G. D. Paterno, The SANT domain of human MI-ER1 interacts with Sp1 to interfere with GC box recognition and repress transcription from its own promoter, J Biol Chem, vol.279, pp.28009-28016, 2004.

A. Dziembowski, E. Lorentzen, E. Conti, and B. Séraphin, A single subunit, Dis3, is essentially responsible for yeast exosome core activity, Nat Struct Mol Biol, vol.14, pp.15-22, 2007.
URL : https://hal.archives-ouvertes.fr/hal-00167461

J. Eitel, N. Suttorp, and B. Opitz, Innate immune recognition and inflammasome activation in Listeria monocytogenes infection, Frontiers in Microbiology, vol.1, p.149, 2010.

A. Eulalio, K. S. Fröhlich, M. Mano, M. Giacca, and J. Vogel, A candidate approach implicates the secreted Salmonella effector protein SpvB in P-body disassembly, PLoS ONE, vol.6, p.17296, 2011.

A. Eulalio, L. N. Schulte, and J. Vogel, The mammalian microRNA response to bacterial infections, RNA biology, vol.9, pp.742-750, 2012.

M. B. Fasken, S. W. Leung, A. Banerjee, M. O. Kodani, R. Chavez et al., Air1 zinc knuckles, 2011.

, J Biol Chem, vol.286, pp.37429-37445

A. Ferreira, D. Sue, C. P. O'byrne, and K. J. Boor, Role of Listeria monocytogenes sigma(B) in survival of lethal acidic conditions and in the acquired acid tolerance response, Appl Environ Microbiol, vol.69, pp.2692-2698, 2003.

M. F. Fontana, S. Banga, K. C. Barry, X. Shen, Y. Tan et al., Secreted bacterial effectors that inhibit host protein synthesis are critical for induction of the innate immune response to virulent Legionella pneumophila, PLoS Pathog, vol.7, p.1001289, 2011.

M. Fromont-racine, B. Senger, C. Saveanu, and F. Fasiolo, Ribosome assembly in eukaryotes, Gene, vol.313, pp.17-42, 2003.
URL : https://hal.archives-ouvertes.fr/pasteur-01404699

M. Gartmann, M. Blau, J. Armache, T. Mielke, M. Topf et al., Mechanism of eIF6-mediated inhibition of ribosomal subunit joining, J Biol Chem, vol.285, pp.14848-14851, 2010.

A. Gavin, P. Aloy, P. Grandi, R. Krause, M. Boesche et al., Proteome survey reveals modularity of the yeast cell machinery, Nature, vol.440, pp.631-636, 2006.

M. R. Gonzalez, M. Bischofberger, B. Frêche, S. Ho, R. G. Parton et al., Pore-forming toxins induce multiple cellular responses promoting survival, Cell Microbiol, vol.13, pp.1026-1043, 2011.

E. Gouin, M. Adib-conquy, D. Balestrino, M. Nahori, V. Villiers et al., The Listeria monocytogenes InlC protein interferes with innate immune responses by targeting the I?B kinase subunit IKK?, Proc Natl Acad Sci, vol.107, pp.17333-17338, 2010.
URL : https://hal.archives-ouvertes.fr/hal-01901815

B. J. Greber, D. Boehringer, C. Montellese, and N. Ban, Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunit, Nat Struct Mol Biol, vol.19, pp.1228-1233, 2012.

R. K. Gudipati, Z. Xu, A. Lebreton, B. Séraphin, L. M. Steinmetz et al., Extensive degradation of RNA precursors by the exosome in wild-type cells, Mol Cell, vol.48, pp.409-421, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01350901

J. Houseley, J. Lacava, and D. Tollervey, RNAquality control by the exosome, Nat Rev Mol Cell Biol, vol.7, pp.529-539, 2006.

N. Hung and A. W. Johnson, Nuclear recycling of the pre-60S ribosomal subunit-associated factor Arx1 depends on Rei1 in Saccharomyces cerevisiae, Mol Cell Biol, vol.26, pp.3718-3727, 2006.

O. Isken and L. E. Maquat, Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function, Genes Dev, vol.21, pp.1833-1856, 2007.

B. Izar, G. K. Mannala, M. A. Mraheil, T. Chakraborty, and T. Hain, 2012. microRNA response to Listeria monocytogenes infection in epithelial cells, Int J Mol Sci, vol.13, pp.1173-1185

H. Jia, X. Wang, J. T. Anderson, and E. Jankowsky, RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex, Proc Natl Acad Sci, vol.109, pp.7292-7297, 2012.

H. Jia, X. Wang, F. Liu, U. Guenther, S. Srinivasan et al., The RNA helicase Mtr4p modulates polyadenylation in the TRAMP complex, Cell, vol.145, pp.890-901, 2011.

S. Jiwani, Y. Wang, G. C. Dowd, A. Gianfelice, P. Pichestapong et al., Identification of components of the host type IA phosphoinositide 3-kinase pathway that promote internalization of Listeria monocytogenes, Infect Immun, vol.80, pp.1252-1266, 2012.

S. Klinge, F. Voigts-hoffmann, M. Leibundgut, S. Arpagaus, and N. Ban, Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6, Science, vol.334, pp.941-948, 2011.

N. J. Krogan, M. Lam, J. Fillingham, M. Keogh, M. Gebbia et al., Proteasome involvement in the repair of DNA double-strand breaks, Mol Cell, vol.16, pp.1027-1034, 2004.

J. La-cruz-de, D. Kressler, D. Tollervey, and P. Linder, Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3' end formation of 5.8S rRNA in Saccharomyces cerevisiae, EMBO J, vol.17, pp.1128-1140, 1998.

G. Lakisic, A. Lebreton, R. Pourpre, O. Wendling, E. Libertini et al., Role of the BAHD1 Chromatin-Repressive Complex in Placental Development and Regulation of Steroid Metabolism, PLoS Genet, vol.12, p.1005898, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01350966

A. Lebreton, Dynamique des facteurs préribosomiques au cours de la biogenèse de la grande sous-unité ribosomique chez S. cerevisiae. Mémoire de thèse, 2006.

A. Lebreton, H. Bierne, and P. Cossart, Les multiples stratégies de Listeria. Pour la science, pp.42-49, 2012.

A. Lebreton, P. Cossart, and H. Bierne, Bacteria tune interferon responses by playing with chromatin, Virulence, vol.3, pp.87-91, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01350803

A. Lebreton, V. Job, M. Ragon, L. Monnier, A. Dessen et al., Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA, MBio, vol.5, pp.775-788, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01109386

A. Lebreton, G. Lakisic, V. Job, L. Fritsch, T. N. Tham et al., A bacterial protein targets the BAHD1 chromatin complex to stimulate type III interferon response, Science, vol.331, pp.1319-1321, 2011.
URL : https://hal.archives-ouvertes.fr/cea-00819299

A. Lebreton, J. Rousselle, P. Lenormand, A. Namane, A. Jacquier et al., 60S ribosomal subunit assembly dynamics defined by semi-quantitative mass spectrometry of purified complexes, Nucleic Acids Res, vol.36, pp.4988-4999, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01350774

A. Lebreton, C. Saveanu, L. Decourty, A. Jacquier, and M. Fromont-racine, Nsa2 is an unstable, conserved factor required for the maturation of 27 SB pre-rRNAs, J Biol Chem, vol.281, pp.27099-27108, 2006.
URL : https://hal.archives-ouvertes.fr/hal-01350676

A. Lebreton, C. Saveanu, L. Decourty, J. Rain, A. Jacquier et al., A functional network involved in the recycling of nucleocytoplasmic pre-60S factors, J Cell Biol, vol.173, pp.349-360, 2006.
URL : https://hal.archives-ouvertes.fr/hal-01350674

A. Lebreton and B. Séraphin, Exosome-mediated quality control: substrate recruitment and molecular activity, Biochim Biophys Acta, vol.1779, pp.558-565, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01350691

A. Lebreton, F. Stavru, and P. Cossart, Organelle targeting during bacterial infection: insights from Listeria, Trends Cell Biol, vol.25, pp.330-338, 2015.
URL : https://hal.archives-ouvertes.fr/pasteur-01162370

A. Lebreton, R. Tomecki, A. Dziembowski, and B. Séraphin, Endonucleolytic RNA cleavage by a eukaryotic exosome, Nature, vol.456, pp.993-996, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01350769

W. Li, A. Song, F. Zhao, Y. Hu, and M. Hua, A novel human TINP1 gene promotes cell proliferation through inhibition of p53 and p21 expression, Oncol Rep, vol.30, pp.1848-1852, 2013.

E. Libertini, A. Lebreton, G. Lakisic, M. Dilliès, S. Beck et al., Overexpression of the Heterochromatinization Factor BAHD1 in HEK293 Cells Differentially Reshapes the DNA Methylome on Autosomes and X Chromosome, vol.6, p.339, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01350961

Q. Liu, J. C. Greimann, and C. D. Lima, Reconstitution, activities, and structure of the eukaryotic RNA exosome, Cell, vol.127, pp.1223-1237, 2006.

M. Lubas, M. S. Christensen, M. S. Kristiansen, M. Domanski, L. G. Falkenby et al., Interaction profiling identifies the human nuclear exosome targeting complex, Mol Cell, vol.43, pp.624-637, 2011.

D. L. Makino, M. Baumgärtner, and E. Conti, Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex, Nature, vol.495, pp.70-75, 2013.

A. R. Malik, M. Urbanska, M. Macias, A. Skalecka, and J. Jaworski, Beyond control of protein translation: What we have learned about the noncanonical regulation and function of mammalian target of rapamycin (mTOR), Biochim Biophys Acta, 2012.

T. Mateus, J. Silva, R. L. Maia, and P. Teixeira, Listeriosis during Pregnancy: A Public Health Concern, Obstet Gynecol, vol.2013, pp.851712-851718, 2013.

A. E. Meyer, L. A. Hoover, and E. A. Craig, The cytosolic J-protein, Jjj1, and Rei1 function in the removal of the pre-60 S subunit factor Arx1, J Biol Chem, vol.285, pp.961-968, 2010.

C. J. Millard, P. J. Watson, I. Celardo, Y. Gordiyenko, S. M. Cowley et al., Class I HDACs share a common mechanism of regulation by inositol phosphates, Mol Cell, vol.51, pp.57-67, 2013.

J. Minàrovits, Microbe-induced epigenetic alterations in host cells: the coming era of pathoepigenetics of microbial infections. A review, Acta Microbiol Immunol Hung, vol.56, pp.1-19, 2009.

P. Mitchell and D. Tollervey, An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3"-->5" degradation, Mol Cell, vol.11, pp.1405-1413, 2003.

I. Mohr and N. Sonenberg, Host translation at the nexus of infection and immunity, Cell Host Microbe, vol.12, pp.470-483, 2012.

N. Nagaraj, J. R. Wisniewski, T. Geiger, J. Cox, M. Kircher et al., Deep proteome and transcriptome mapping of a human cancer cell line, Mol Syst Biol, vol.7, p.548, 2011.

U. Nakari, L. Rantala, A. Pihlajasaari, S. Toikkanen, T. Johansson et al., Investigation of increased listeriosis revealed two fishery production plants with persistent Listeria contamination in Finland in 2010, Epidemiol Infect, vol.142, pp.2261-2269, 2014.

T. A. Nissan, J. Bassler, E. Petfalski, D. Tollervey, and E. Hurt, 60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm, EMBO J, vol.21, pp.5539-5547, 2002.

B. Pertschy, C. Saveanu, G. Zisser, A. Lebreton, M. Tengg et al., Cytoplasmic recycling of 60S preribosomal factors depends on the AAA protein Drg1, Mol Cell Biol, vol.27, pp.6581-6592, 2007.
URL : https://hal.archives-ouvertes.fr/hal-01350677

M. Plamont, E. Billon-denis, S. Maurin, C. Gauron, F. M. Pimenta et al., Small fluorescenceactivating and absorption-shifting tag for tunable protein imaging in vivo, Proc Natl Acad Sci, vol.113, pp.497-502, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01259909

F. Pontiroli, O. Dussurget, I. Zanoni, M. Urbano, O. Beretta et al., The Timing of IFN? Production Affects Early Innate Responses to Listeria monocytogenes and Determines the Overall Outcome of Lethal Infection, PLoS ONE, vol.7, p.43455, 2012.

I. Popovic, B. Heron, and C. Covacin, Listeria: an Australian perspective, vol.11, pp.425-432, 2001.

C. Saveanu, A. Namane, P. Gleizes, A. Lebreton, J. Rousselle et al., Sequential protein association with nascent 60S ribosomal particles, Mol Cell Biol, vol.23, pp.4449-4460, 2003.
URL : https://hal.archives-ouvertes.fr/hal-01350680

D. Schaeffer, B. Tsanova, A. Barbas, F. P. Reis, E. G. Dastidar et al., The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities, Nat Struct Mol Biol, vol.16, pp.56-62, 2009.

K. Schmidt and J. S. Butler, Nuclear RNA surveillance: role of TRAMP in controlling exosome specificity, Wiley Interdiscip Rev RNA, vol.4, pp.217-231, 2013.

C. Schneider, E. Leung, J. Brown, and D. Tollervey, The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome, Nucleic Acids Res, vol.37, pp.1127-1140, 2009.

B. Senger, D. Lafontaine, J. S. Graindorge, O. Gadal, A. Camasses et al., The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis, Mol Cell, vol.8, pp.1363-1373, 2001.
URL : https://hal.archives-ouvertes.fr/hal-02370147

R. Shahni, A. Czajka, B. S. Mankoo, A. K. Guvenel, A. J. King et al., Nop-7-associated 2 (NSA2), a candidate gene for diabetic nephropathy, is involved in the TGF?1 pathway, Int J Biochem Cell Biol, vol.45, pp.626-635, 2013.

R. Shahni, L. Gnudi, A. King, P. Jones, and A. N. Malik, Elevated levels of renal and circulating Nop-7-associated 2 (NSA2) in rat and mouse models of diabetes, in mesangial cells in vitro and in patients with diabetic nephropathy, Diabetologia, vol.55, pp.825-834, 2012.

N. Shrestha, W. Bahnan, D. J. Wiley, G. Barber, K. A. Fields et al., Eukaryotic initiation factor 2 (eIF2) signaling regulates proinflammatory cytokine expression and bacterial invasion, J Biol Chem, vol.287, pp.28738-28744, 2012.

I. H. Siddique, B. E. Mckenzie, W. J. Sapp, and P. Rich, Light and electron microscopic study of the livers of pregnant mice infected with Listeria monocytogenes, Am J Vet Res, vol.39, pp.887-892, 1978.

K. E. Sloan, C. Schneider, and N. J. Watkins, Comparison of the yeast and human nuclear exosome complexes, Biochem Soc Trans, vol.40, pp.850-855, 2012.

S. Slomovic, D. Laufer, D. Geiger, and G. Schuster, Polyadenylation of ribosomal RNA in human cells, Nucleic Acids Res, vol.34, pp.2966-2975, 2006.

C. Staedel and F. Darfeuille, MicroRNAs and bacterial infection, Cell Microbiol, vol.15, pp.1496-1507, 2013.

D. Staiger, C. Korneli, M. Lummer, and L. Navarro, Emerging role for RNA-based regulation in plant immunity, New Phytol, vol.197, pp.394-404, 2013.

L. Tafforeau, C. Zorbas, J. Langhendries, S. Mullineux, V. Stamatopoulou et al., The complexity of human ribosome biogenesis revealed by systematic nucleolar screening of pre-rRNA processing factors, Mol Cell, vol.51, pp.539-551, 2013.

I. Tattoli, M. T. Sorbara, D. Vuckovic, A. Ling, F. Soares et al., Amino acid starvation induced by invasive bacterial pathogens triggers an innate host defense program, Cell Host Microbe, vol.11, pp.563-575, 2012.

I. Tattoli, M. T. Sorbara, C. Yang, S. A. Tooze, D. J. Philpott et al., Listeria phospholipases subvert host autophagic defenses by stalling preautophagosomal structures, EMBO J, vol.32, pp.3066-3078, 2013.

P. Traub and M. Nomura, Structure and function of Escherichia coli ribosomes. VI. Mechanism of assembly of 30 s ribosomes studied in vitro, J Mol Biol, vol.40, pp.391-413, 1969.

R. J. Turner, Y. Lu, and R. L. Switzer, Regulation of the Bacillus subtilis pyrimidine biosynthetic (pyr) gene cluster by an autogenous transcriptional attenuation mechanism, J Bacteriol, vol.176, pp.3708-3722, 1994.

A. Van-hoof, P. A. Frischmeyer, H. C. Dietz, and R. Parker, Exosome-mediated recognition and degradation of mRNAs lacking a termination codon, Science, vol.295, pp.2262-2264, 2002.

L. Wang, B. Charroux, S. Kerridge, and C. Tsai, Atrophin recruits HDAC1/2 and G9a to modify histone H3K9 and to determine cell fates, EMBO Rep, vol.9, pp.555-562, 2008.

X. Wang, H. Jia, E. Jankowsky, and J. T. Anderson, Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p, RNA, vol.14, pp.107-116, 2008.

T. Weichhart, G. Costantino, M. Poglitsch, M. Rosner, M. Zeyda et al., The TSC-mTOR signaling pathway regulates the innate inflammatory response, Immunity, vol.29, pp.565-577, 2008.

S. West, N. Gromak, C. J. Norbury, and N. J. Proudfoot, Adenylation and exosome-mediated degradation of cotranscriptionally cleaved premessenger RNA in human cells, Mol Cell, vol.21, pp.437-443, 2006.

M. M. Yusupov, G. Z. Yusupova, A. Baucom, K. Lieberman, T. N. Earnest et al., Crystal structure of the ribosome at 5.5 A resolution, Science, vol.292, pp.883-896, 2001.

H. Zhang, X. Ma, T. Shi, Q. Song, H. Zhao et al., NSA2, a novel nucleolus protein regulates cell proliferation and cell cycle, Biochem Biophys Res Commun, vol.391, pp.651-658, 2010.