G. Screaton, M. Bell, D. Jackson, F. Cornelis, U. Gerth et al., Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons., Proceedings of the National Academy of Sciences, vol.89, issue.24, pp.12160-12164, 1992.
DOI : 10.1073/pnas.89.24.12160

S. Ghaffari, F. Smadja-joffe, R. Oostendorp, J. Levesque, G. Dougherty et al., CD44 isoforms in normal and leukemic hematopoiesis, Experimental Hematology, vol.27, issue.6, pp.978-993, 1999.
DOI : 10.1016/S0301-472X(99)00023-5

J. Lesley, R. Hyman, and P. Kincade, CD44 and Its Interaction with Extracellular Matrix, Adv Immunol, vol.54, pp.271-335, 1993.
DOI : 10.1016/S0065-2776(08)60537-4

P. Herrlich, H. Morrison, J. Sleeman, V. Orian-rousseau, H. Konig et al., CD44 Acts Both as a Growth- and Invasiveness-Promoting Molecule and as a Tumor-Suppressing Cofactor, Annals of the New York Academy of Sciences, vol.71, issue.1, pp.106-118, 2000.
DOI : 10.1111/j.1749-6632.2000.tb06704.x

D. Naor, S. Nedvetzki, I. Golan, L. Melnik, and Y. Faitelson, CD44 in Cancer, Critical Reviews in Clinical Laboratory Sciences, vol.3, issue.6, pp.527-579, 2002.
DOI : 10.1016/S0140-6736(95)90521-9

H. Ponta, L. Sherman, and P. Herrlich, CD44: From adhesion molecules to signalling regulators, Nature Reviews Molecular Cell Biology, vol.4, issue.1, pp.33-45, 2003.
DOI : 10.1038/nrm1004

R. Charrad, Y. Li, B. Delpech, N. Balitrand, D. Clay et al., Ligation of the CD44 adhesion molecule reverses blockage of differentiation in human acute myeloid leukemia, Nature Medicine, vol.5, issue.6, pp.669-676, 1999.
DOI : 10.1038/9518

R. Charrad, Z. Gadhoum, J. Qi, A. Glachant, M. Allouche et al., Effects of anti-CD44 monoclonal antibodies on differentiation and apoptosis of human myeloid leukemia cell lines, Blood, vol.99, issue.1, pp.290-299, 2002.
DOI : 10.1182/blood.V99.1.290

M. Lanotte, V. Martin-thouvenin, S. Najman, P. Balerini, F. Valensi et al., NB4, a maturation inducible cell line with t(15;17) marker isolated from a human acute promyelocytic leukemia (M3), Blood, vol.77, pp.1080-1086, 1991.

M. Allouche, R. Charrad, A. Bettaieb, C. Greenland, C. Grignon et al., Ligation of the CD44 adhesion molecule inhibits drug-induced apoptosis in human myeloid leukemia cells, Blood, vol.96, pp.1187-1190, 2000.

Z. Gadhoum, M. Leibovitch, J. Qi, D. Dumenil, L. Durand et al., CD44: a new means to inhibit acute myeloid leukemia cell proliferation via p27Kip1, Blood, vol.103, issue.3, pp.1059-1068, 2004.
DOI : 10.1182/blood-2003-04-1218

R. Gallagher, Retinoic acid resistance in acute promyelocytic leukemia, Leukemia, vol.16, issue.10, pp.1940-1958, 2002.
DOI : 10.1038/sj.leu.2402719

A. Melnick and J. Licht, Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia, Blood, vol.93, pp.3167-3215, 1999.

G. Benoit, M. Roussel, F. Pendino, E. Segal-bendirdjian, and M. Lanotte, Orchestration of multiple arrays of signal cross-talk and combinatorial interactions for maturation and cell death: another vision of t(15;17) preleukemic blast and APL-cell maturation, Oncogene, vol.20, issue.49, pp.7161-7177, 2001.
DOI : 10.1038/sj.onc.1204760

S. Ruchaud, E. Duprez, M. Gendron, G. Houge, H. Genieser et al., Two distinctly regulated events, priming and triggering, during retinoid-induced maturation and resistance of NB4 promyelocytic leukemia cell line., Proceedings of the National Academy of Sciences, vol.91, issue.18, pp.8428-8432, 1994.
DOI : 10.1073/pnas.91.18.8428

M. Roussel and M. Lanotte, Maturation sensitive and resistant t(15;17) NB4 cell lines as tools for APL physiopathology: nomenclature of cells and repertory of their known genetic alterations and phenotypes, Oncogene, vol.20, issue.49, pp.7287-7291, 2001.
DOI : 10.1038/sj.onc.1204863

E. Duprez, J. Lillehaug, T. Naoe, and M. Lanotte, cAMP signalling is decisive for recovery of nuclear bodies (PODs) during maturation of RA-resistant t(15;17) promyelocytic leukemia NB4 cells expressing PML-RAR alpha, Oncogene, vol.12, pp.2451-2459, 1996.

Q. Zhu, J. Zhang, H. Zhu, Y. Shen, M. Flexor et al., Synergic effects of arsenic trioxide and cAMP during acute promyelocytic leukemia cell maturation subtends a novel signaling cross-talk, Blood, vol.99, pp.1014-1022, 2002.

F. Boisvert, M. Kruhlak, A. Box, M. Hendzel, and D. Bazett-jones, The Transcription Coactivator Cbp Is a Dynamic Component of the Promyelocytic Leukemia Nuclear Body, The Journal of Cell Biology, vol.13, issue.5, pp.1099-1106, 2001.
DOI : 10.1038/35010583

E. Parrella, M. Gianni, V. Cecconi, E. Nigro, M. Barzago et al., Phosphodiesterase IV Inhibition by Piclamilast Potentiates the Cytodifferentiating Action of Retinoids in Myeloid Leukemia Cells: CROSS-TALK BETWEEN THE cAMP AND THE RETINOIC ACID SIGNALING PATHWAYS, Journal of Biological Chemistry, vol.279, issue.40, pp.42026-42040, 2004.
DOI : 10.1074/jbc.M406530200

D. Kamashev, D. Vitoux, D. The, and H. , PML???RARA-RXR Oligomers Mediate Retinoid and Rexinoid/cAMP Cross-Talk in Acute Promyelocytic Leukemia Cell Differentiation, The Journal of Experimental Medicine, vol.6, issue.8, pp.1163-1174, 2004.
DOI : 10.1073/pnas.180290497

A. 22-razin, CpG methylation, chromatin structure and gene silencing---a three-way connection, The EMBO Journal, vol.17, issue.17, pp.4905-4908, 1998.
DOI : 10.1093/emboj/17.17.4905

E. Baker and A. El-osta, The rise of DNA methylation and the importance of chromatin on multidrug resistance in cancer, Experimental Cell Research, vol.290, issue.2, pp.177-194, 2003.
DOI : 10.1016/S0014-4827(03)00342-2

Y. Yamada, H. Watanabe, F. Miura, H. Soejima, M. Uchiyama et al., A Comprehensive Analysis of Allelic Methylation Status of CpG Islands on Human Chromosome 21q, Genome Research, vol.14, issue.2, pp.247-266, 2004.
DOI : 10.1101/gr.1351604

E. Maquarre, C. Artus, Z. Gadhoum, C. Jasmin, F. Smadja-joffe et al., CD44 ligation induces apoptosis via caspase- and serine protease-dependent pathways in acute promyelocytic leukemia cells, Leukemia, vol.93, issue.12, pp.2296-2303, 2005.
DOI : 10.1016/S1097-2765(01)00341-0

E. Shtivelman and J. Bishop, Expression of CD44 is repressed in neuroblastoma cells., Molecular and Cellular Biology, vol.11, issue.11, pp.5446-5453, 1991.
DOI : 10.1128/MCB.11.11.5446

M. Gardiner-garden and M. Frommer, CpG Islands in vertebrate genomes, Journal of Molecular Biology, vol.196, issue.2, pp.261-282, 1987.
DOI : 10.1016/0022-2836(87)90689-9

S. Berger, Histone modifications in transcriptional regulation, Current Opinion in Genetics & Development, vol.12, issue.2, pp.142-148, 2002.
DOI : 10.1016/S0959-437X(02)00279-4

A. Eberharter and P. Becker, Histone acetylation: a switch between repressive and permissive chromatin: Second in review series on chromatin dynamics, EMBO Reports, vol.3, issue.3, pp.224-229, 2002.
DOI : 10.1093/embo-reports/kvf053

M. 30-grunstein, Histone acetylation in chromatin structure and transcription, Nature, vol.389, issue.6649, pp.349-352, 1997.
DOI : 10.1038/38664

G. Benoit, L. Altucci, M. Flexor, S. Ruchaud, J. Lillehaug et al., RAR-independent RXR signaling induces t(15;17) leukemia cell maturation, The EMBO Journal, vol.18, issue.24, pp.7011-7018, 1999.
DOI : 10.1093/emboj/18.24.7011

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171764

W. Fischle, Y. Wang, and C. Allis, Histone and chromatin cross-talk, Current Opinion in Cell Biology, vol.15, issue.2, pp.172-183, 2003.
DOI : 10.1016/S0955-0674(03)00013-9

URL : http://hdl.handle.net/11858/00-001M-0000-0012-F138-4

C. Peterson and M. Laniel, Histones and histone modifications, Current Biology, vol.14, issue.14, pp.546-551, 2004.
DOI : 10.1016/j.cub.2004.07.007

URL : http://doi.org/10.1016/j.cub.2004.07.007

B. Strahl and C. Allis, The language of covalent histone modifications, Nature, vol.96, issue.6765, pp.41-45, 2000.
DOI : 10.1038/47412

P. Cheung, K. Tanner, W. Cheung, P. Sassone-corsi, J. Denu et al., Synergistic Coupling of Histone H3 Phosphorylation and Acetylation in Response to Epidermal Growth Factor Stimulation, Molecular Cell, vol.5, issue.6, pp.905-915, 2000.
DOI : 10.1016/S1097-2765(00)80256-7

W. Lo, R. Trievel, J. Rojas, L. Duggan, J. Hsu et al., Phosphorylation of Serine 10 in Histone H3 Is Functionally Linked In Vitro and In Vivo to Gcn5-Mediated Acetylation at Lysine 14, Molecular Cell, vol.5, issue.6, pp.917-926, 2000.
DOI : 10.1016/S1097-2765(00)80257-9

S. Nowak and V. Corces, Phosphorylation of histone H3 correlates with transcriptionally active loci, Genes & Development, vol.14, issue.23, pp.3003-3013, 2000.
DOI : 10.1101/gad.848800

M. Lachner, O. Carroll, D. Rea, S. Mechtler, K. Jenuwein et al., Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins, Nature, vol.410, issue.6824, pp.116-120, 2001.
DOI : 10.1038/35065132

J. Nakayama, J. Rice, B. Strahl, C. Allis, and S. Grewal, Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly, Science, vol.292, issue.5514, pp.110-113, 2001.
DOI : 10.1126/science.1060118

Y. Zhang and D. Reinberg, Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails, Genes & Development, vol.15, issue.18, pp.2343-2360, 2001.
DOI : 10.1101/gad.927301

T. Kouzarides, Histone methylation in transcriptional control, Current Opinion in Genetics & Development, vol.12, issue.2, pp.198-209, 2002.
DOI : 10.1016/S0959-437X(02)00287-3

A. Zambon, L. Zhang, S. Minovitsky, J. Kanter, S. Prabhakar et al., Gene expression patterns define key transcriptional events in cell-cycle regulation by cAMP and protein kinase A, Proceedings of the National Academy of Sciences, vol.102, issue.24, pp.8561-8566, 2005.
DOI : 10.1073/pnas.0503363102

J. Li, Y. Guo, F. Schroeder, R. Youngs, T. Schmidt et al., Dopamine D2-like antagonists induce chromatin remodeling in striatal neurons through cyclic AMP-protein kinase A and NMDA receptor signaling, Journal of Neurochemistry, vol.90, issue.5, pp.1117-1131, 2004.
DOI : 10.1111/j.1471-4159.2004.02569.x

L. Salvador, Y. Park, J. Cottom, E. Maizels, J. Jones et al., Follicle-stimulating Hormone Stimulates Protein Kinase A-mediated Histone H3 Phosphorylation and Acetylation Leading to Select Gene Activation in Ovarian Granulosa Cells, Journal of Biological Chemistry, vol.276, issue.43, pp.40146-40155, 2001.
DOI : 10.1074/jbc.M106710200

R. Hyman, Lack of a consistent relationship between demethylation of the CD44 promoter and CD44 expression, Immunogenetics, vol.53, issue.10-11, pp.914-924, 2002.
DOI : 10.1007/s00251-001-0417-5

F. Banine, C. Bartlett, R. Gunawardena, C. Muchardt, M. Yaniv et al., SWI/SNF Chromatin-Remodeling Factors Induce Changes in DNA Methylation to Promote Transcriptional Activation, Cancer Research, vol.65, issue.9, pp.3542-3547, 2005.
DOI : 10.1158/0008-5472.CAN-04-3554

URL : https://hal.archives-ouvertes.fr/hal-00016351

E. Batsché, M. Yaniv, and C. Muchardt, The human SWI/SNF subunit Brm is a regulator of alternative splicing, Nature Structural & Molecular Biology, vol.29, issue.1, pp.22-29, 2006.
DOI : 10.1038/nsmb1030

R. Schmits, J. Filmus, N. Gerwin, G. Senaldi, F. Kiefer et al., CD44 regulates hematopoietic progenitor distribution, granuloma formation, and tumorigenicity, Blood, vol.90, pp.2217-2233, 1997.

C. Rochette-egly, Dynamic Combinatorial Networks in Nuclear Receptor-mediated Transcription, Journal of Biological Chemistry, vol.280, issue.38, pp.32565-32568, 2005.
DOI : 10.1074/jbc.R500008200

URL : https://hal.archives-ouvertes.fr/hal-00187731

M. Gianni, M. Terao, P. Norio, T. Barbui, A. Rambaldi et al., All-trans retinoic acid and cyclic adenosine monophosphate cooperate in the expression of leukocyte alkaline phosphatase in acute promyelocytic leukemia cells, Blood, vol.85, pp.3619-3635, 1995.

J. Kim, L. Jia, M. Stallcup, and G. Coetzee, The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus, Journal of Molecular Endocrinology, vol.34, issue.1, pp.107-118, 2005.
DOI : 10.1677/jme.1.01701

V. Doucas, M. Tini, D. Egan, and R. Evans, Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling, Proceedings of the National Academy of Sciences, vol.96, issue.6, pp.2627-2632, 1999.
DOI : 10.1073/pnas.96.6.2627