H. Barth, K. Aktories, M. Popoff, and B. Stiles, Binary Bacterial Toxins: Biochemistry, Biology, and Applications of Common Clostridium and Bacillus Proteins, Microbiology and Molecular Biology Reviews, vol.68, issue.3, pp.373-402, 2004.
DOI : 10.1128/MMBR.68.3.373-402.2004
URL : http://mmbr.asm.org/content/68/3/373.full.pdf

K. Aktories, C. Schwan, P. Papatheodorou, and A. Lang, Bidirectional attack on the actin cytoskeleton. Bacterial protein toxins causing polymerization or depolymerization of actin, Toxicon, vol.60, issue.4, pp.572-581, 2012.
DOI : 10.1016/j.toxicon.2012.04.338

S. Perelle, S. Scalzo, S. Kochi, M. Mock, and M. Popoff, Immunological and functional comparison between Clostridium perfringens iota toxin, C. spiroforme toxin, and anthrax toxins, FEMS Microbiology Letters, vol.269, issue.1, pp.117-121, 1997.
DOI : 10.1099/00221287-139-10-2459
URL : https://academic.oup.com/femsle/article-pdf/146/1/117/19101495/146-1-117.pdf

K. Aktories, M. Barmann, I. Ohishi, S. Tsuyama, and K. Jakobs, Botulinum C2 toxin ADP-ribosylates actin, Nature, vol.85, issue.6077, pp.390-392, 1986.
DOI : 10.1038/322390a0

J. Vandekerckhove, B. Schering, M. Barmann, and K. Aktories, iota toxin ADP-ribosylates skeletal muscle actin in Arg-177, FEBS Letters, vol.75, issue.1-2, pp.48-52, 1987.
DOI : 10.1073/pnas.75.3.1106
URL : http://onlinelibrary.wiley.com/doi/10.1016/0014-5793(87)81129-8/pdf

K. Aktories and A. Wegner, Mechanisms of the cytopathic action of actin-ADP-ribosylating toxins, Molecular Microbiology, vol.267, issue.20, pp.2905-2908, 1992.
DOI : 10.1083/jcb.109.2.593

H. Hilger, S. Pust, V. Figura, G. Kaiser, E. Stiles et al., The Long-Lived Nature of Clostridium perfringens Iota Toxin in Mammalian Cells Induces Delayed Apoptosis, Infection and Immunity, vol.77, issue.12, pp.5593-5601, 2009.
DOI : 10.1128/IAI.00710-09
URL : http://iai.asm.org/content/77/12/5593.full.pdf

M. Eckhardt, H. Barth, D. Blocker, and K. Aktories, C2 Toxin to Asparagine-linked Complex and Hybrid Carbohydrates, Journal of Biological Chemistry, vol.266, issue.4, pp.2328-2334, 2000.
DOI : 10.1146/annurev.ge.18.120184.002521
URL : http://www.jbc.org/content/275/4/2328.full.pdf

G. Fritz, P. Schroeder, and K. Aktories, Isolation and characterization of Clostridium botulinum C2 toxin-resistant cell line: evidence for possible involvement of the cellular C2II receptor in growth regulation, Infect Immun, vol.63, pp.2334-2340, 1995.

P. Papatheodorou, J. Carette, G. Bell, C. Schwan, and G. Guttenberg, Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT), Proceedings of the National Academy of Sciences, vol.69, issue.5, pp.16422-16427, 2011.
DOI : 10.1128/IAI.69.5.2980-2987.2001
URL : http://www.pnas.org/content/108/39/16422.full.pdf

P. Papatheodorou, C. Wilczek, T. Nolke, G. Guttenberg, and D. Hornuss, ABSTRACT, Infection and Immunity, vol.80, issue.4, pp.1418-1423, 2012.
DOI : 10.1128/IAI.06378-11

F. Van-der-goot and J. Young, Receptors of anthrax toxin and cell entry, Molecular Aspects of Medicine, vol.30, issue.6, pp.406-412, 2009.
DOI : 10.1016/j.mam.2009.08.007

B. Stiles, M. Hale, J. Marvaud, and M. Popoff, Clostridium perfringens Iota Toxin: Binding Studies and Characterization of Cell Surface Receptor by Fluorescence-Activated Cytometry, Infection and Immunity, vol.68, issue.6, pp.3475-3484, 2000.
DOI : 10.1128/IAI.68.6.3475-3484.2000
URL : http://iai.asm.org/content/68/6/3475.full.pdf

M. Nagahama, A. Yamaguchi, T. Hagiyama, N. Ohkubo, and K. Kobayashi, Binding and Internalization of Clostridium perfringens Iota-Toxin in Lipid Rafts, Infection and Immunity, vol.72, issue.6, pp.3267-3275, 2004.
DOI : 10.1128/IAI.72.6.3267-3275.2004
URL : http://iai.asm.org/content/72/6/3267.full.pdf

M. Nagahama, T. Hagiyama, T. Kojima, K. Aoyanagi, and C. Takahashi, Binding and Internalization of Clostridium botulinum C2 Toxin, Infection and Immunity, vol.77, issue.11, pp.5139-5148, 2009.
DOI : 10.1128/IAI.00638-09
URL : http://iai.asm.org/content/77/11/5139.full.pdf

B. Stiles, M. Hale, J. Marvaud, and M. Popoff, Clostridium perfringens iota toxin: characterization of the cell-associated iota b complex, Biochemical Journal, vol.367, issue.3, pp.801-808, 2002.
DOI : 10.1042/bj20020566

M. Hale, J. Marvaud, M. Popoff, and B. Stiles, Detergent-Resistant Membrane Microdomains Facilitate Ib Oligomer Formation and Biological Activity of Clostridium perfringens Iota-Toxin, Infection and Immunity, vol.72, issue.4, pp.2186-2193, 2004.
DOI : 10.1128/IAI.72.4.2186-2193.2004
URL : http://iai.asm.org/content/72/4/2186.full.pdf

D. Blocker, J. Behlke, K. Aktories, and H. Barth, Cellular Uptake of the Clostridium perfringens Binary Iota-Toxin, Infection and Immunity, vol.69, issue.5, pp.2980-2987, 2001.
DOI : 10.1128/IAI.69.5.2980-2987.2001
URL : http://iai.asm.org/content/69/5/2980.full.pdf

J. Blonder, M. Hale, K. Chan, L. Yu, and D. Lucas, Quantitative Profiling of the Detergent-Resistant Membrane Proteome of Iota-b Toxin Induced Vero Cells, Journal of Proteome Research, vol.4, issue.2, pp.523-531, 2005.
DOI : 10.1021/pr049790s

H. Ponta, L. Sherman, and P. Herrlich, CD44: From adhesion molecules to signalling regulators, Nature Reviews Molecular Cell Biology, vol.121, issue.1, pp.33-45, 2003.
DOI : 10.1083/jcb.121.6.1299

S. Oliferenko, K. Paiha, T. Harder, V. Gerke, and C. Schwarzler, Analysis of Cd44-Containing Lipid Rafts, The Journal of Cell Biology, vol.78, issue.4, pp.843-854, 1999.
DOI : 10.1016/0003-2697(84)90782-6
URL : http://jcb.rupress.org/content/jcb/146/4/843.full.pdf

J. Sleeman, R. W. Hofmann, M. Moll, J. Herrlich, and P. , Regulated clustering of variant CD44 proteins increases their hyaluronate binding capacity, The Journal of Cell Biology, vol.135, issue.4, pp.1139-1150, 1996.
DOI : 10.1083/jcb.135.4.1139
URL : http://jcb.rupress.org/content/jcb/135/4/1139.full.pdf

M. Nagahama, K. Nagayasu, K. Kobayashi, and J. Sakurai, Binding Component of Clostridium perfringens Iota-Toxin Induces Endocytosis in Vero Cells, Infection and Immunity, vol.70, issue.4, pp.1909-1914, 2002.
DOI : 10.1128/IAI.70.4.1909-1914.2002
URL : http://iai.asm.org/content/70/4/1909.full.pdf

A. Skoudy, J. Mounier, A. Aruffo, H. Ohayan, and P. Gounon, CD44 binds to the Shigella IpaB protein and participates in bacterial invasion of epithelial cells, Cellular Microbiology, vol.154, issue.1, pp.19-33, 2000.
DOI : 10.1126/science.283.5410.2092

B. Stiles and T. Wilkins, Purification and characterization of Clostridium perfringens iota toxin: dependence on two nonlinked proteins for biological activity, Infect Immun, vol.54, pp.683-688, 1986.

J. Richard, G. Mainguy, M. Gibert, J. Marvaud, and B. Stiles, Transcytosis of iota-toxin across polarized CaCo-2 cells, Molecular Microbiology, vol.57, issue.4, pp.907-917, 2002.
DOI : 10.1128/IAI.68.6.3475-3484.2000
URL : http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2958.2002.02806.x/pdf

L. Bourguignon, P. Singleton, F. Diedrich, R. Stern, and E. Gilad, Exchanger (NHE1) Creates Acidic Microenvironments Leading to Hyaluronidase-2 and Cathepsin B Activation and Breast Tumor Cell Invasion, Journal of Biological Chemistry, vol.264, issue.26, pp.26991-27007, 2004.
DOI : 10.1007/BF01052628
URL : http://www.jbc.org/content/279/26/26991.full.pdf

M. Howes, M. Kirkham, J. Riches, C. K. Walser, and P. , Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells, The Journal of Cell Biology, vol.114, issue.4, pp.675-691, 2010.
DOI : 10.1083/jcb.201002119.dv

C. Eyster, J. Higginson, R. Huebner, N. Porat-shilom, and R. Weigert, Discovery of New Cargo Proteins that Enter Cells through Clathrin-Independent Endocytosis, Traffic, vol.5, issue.5, pp.590-599, 2009.
DOI : 10.1111/j.1600-0854.2009.00894.x
URL : http://onlinelibrary.wiley.com/doi/10.1111/j.1600-0854.2009.00894.x/pdf

M. Gibert, M. Monier, R. Ruez, M. Hale, and B. Stiles, Endocytosis and toxicity of clostridial binary toxins depend on a clathrin-independent pathway regulated by Rho-GDI, Cellular Microbiology, vol.109, issue.1, pp.154-170, 2011.
DOI : 10.1093/jb/mvi052
URL : https://hal.archives-ouvertes.fr/pasteur-01762176

D. Blocker, K. Pohlmann, G. Haug, C. Bachmeyer, and R. Benz, C2 Toxin, Journal of Biological Chemistry, vol.10, issue.39, pp.37360-37367, 2003.
DOI : 10.1074/jbc.M303980200

I. Okamoto, Y. Kawano, H. Tsuiki, J. Sasaki, and M. Nakao, CD44 cleavage induced by a membrane-associated metalloprotease plays a critical role in tumor cell migration, Oncogene, vol.18, issue.7, pp.1435-1446, 1999.
DOI : 10.1111/j.1432-1033.1995.tb20738.x
URL : http://www.nature.com/onc/journal/v18/n7/pdf/1202447a.pdf

D. Liu and M. Sy, A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid, Journal of Experimental Medicine, vol.183, issue.5, pp.1987-1994, 1996.
DOI : 10.1084/jem.183.5.1987

S. Thankamony and W. Knudson, Acylation of CD44 and Its Association with Lipid Rafts Are Required for Receptor and Hyaluronan Endocytosis, Journal of Biological Chemistry, vol.1451, issue.45, pp.34601-34609, 2006.
DOI : 10.1074/jbc.273.25.15830
URL : http://www.jbc.org/content/281/45/34601.full.pdf

S. Jalkanen and M. Jalkanen, Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin, The Journal of Cell Biology, vol.116, issue.3, pp.817-825, 1992.
DOI : 10.1083/jcb.116.3.817
URL : http://jcb.rupress.org/content/jcb/116/3/817.full.pdf

M. Naujokas, M. Morin, M. Anderson, M. Peterson, and J. Miller, The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44, Cell, vol.74, issue.2, pp.257-268, 1993.
DOI : 10.1016/0092-8674(93)90417-O

G. Weber, S. Ashkar, M. Glimcher, and H. Cantor, Receptor-Ligand Interaction Between CD44 and Osteopontin (Eta-1), Science, vol.271, issue.5248, pp.509-512, 1996.
DOI : 10.1126/science.271.5248.509

K. Bennett, B. Modrell, G. Greenfield, A. Bartolazzi, and I. Stamenkovic, Regulation of CD44 binding to hyaluronan by glycosylation of variably spliced exons, The Journal of Cell Biology, vol.131, issue.6, pp.1623-1633, 1995.
DOI : 10.1083/jcb.131.6.1623
URL : http://jcb.rupress.org/content/jcb/131/6/1623.full.pdf

K. Bennett, D. Jackson, J. Simon, E. Tanczos, and R. Peach, CD44 isoforms containing exon V3 are responsible for the presentation of heparin-binding growth factor, The Journal of Cell Biology, vol.128, issue.4, pp.687-698, 1995.
DOI : 10.1083/jcb.128.4.687
URL : http://jcb.rupress.org/content/jcb/128/4/687.full.pdf

J. Lee, M. Wang, P. Sudhir, and J. Chen, CD44 Engagement Promotes Matrix-Derived Survival through the CD44-SRC-Integrin Axis in Lipid Rafts, Molecular and Cellular Biology, vol.28, issue.18, pp.5710-5723, 2008.
DOI : 10.1128/MCB.00186-08
URL : http://mcb.asm.org/content/28/18/5710.full.pdf

D. Lefebvre, J. Lai, N. Maeshima, J. Ford, and A. Wong, CD44 interacts directly with Lck in a zinc-dependent manner, Molecular Immunology, vol.47, issue.10, pp.1882-1889, 2010.
DOI : 10.1016/j.molimm.2010.03.018

A. Bretscher, K. Edwards, and R. Fehon, ERM proteins and merlin: integrators at the cell cortex, Nature Reviews Molecular Cell Biology, vol.12, issue.8, pp.586-599, 2002.
DOI : 10.1091/mbc.12.10.3060

J. Legg, C. Lewis, M. Parsons, T. Ng, and C. Isacke, A novel PKC-regulated mechanism controls CD44???ezrin association and directional cell motility, Nature Cell Biology, vol.75, issue.6, pp.399-407, 2002.
DOI : 10.1038/sj.onc.1200824

V. Lokeshwar, N. Fregien, and L. Bourguignon, Ankyrin-binding domain of CD44(GP85) is required for the expression of hyaluronic acid-mediated adhesion function, The Journal of Cell Biology, vol.126, issue.4, pp.1099-1109, 1994.
DOI : 10.1083/jcb.126.4.1099

V. Samanna, T. Ma, T. Mak, M. Rogers, and M. Chellaiah, Actin polymerization modulates CD44 surface expression, MMP-9 activation, and osteoclast function, Journal of Cellular Physiology, vol.39, issue.3, pp.710-720, 2007.
DOI : 10.1016/S0005-2728(01)00198-0
URL : http://onlinelibrary.wiley.com/doi/10.1002/jcp.21137/pdf

M. Martchenko, S. Jeong, and S. Cohen, Heterodimeric integrin complexes containing ??1-integrin promote internalization and lethality of anthrax toxin, Proceedings of the National Academy of Sciences, vol.79, issue.22, pp.15583-15588, 2010.
DOI : 10.1021/ac701741s
URL : http://www.pnas.org/content/107/35/15583.full.pdf

C. Montecucco, O. Rossetto, and G. Schiavo, Presynaptic receptor arrays for clostridial neurotoxins, Trends in Microbiology, vol.12, issue.10, pp.442-446, 2004.
DOI : 10.1016/j.tim.2004.08.002

C. Cywes and M. Wessels, Group A Streptococcus tissue invasion by CD44-mediated cell signalling, Nature, vol.107, issue.6864, pp.648-652, 2001.
DOI : 10.1172/JCI11138

C. Jung, A. Matzke, H. Niemann, C. Schwerk, and . Tenenbaum, invasion, Molecular Microbiology, vol.16, issue.Pt 13, pp.1196-1207, 2009.
DOI : 10.1111/j.1365-2958.2009.06716.x
URL : https://hal.archives-ouvertes.fr/hal-00921880

F. Lafont, T. Van-nhieu, G. Hanada, K. Sansonetti, P. Van-der-goot et al., Initial steps of Shigella infection depend on the cholesterol/sphingolipid raft-mediated CD44-IpaB interaction, The EMBO Journal, vol.21, issue.17, pp.4449-4457, 2002.
DOI : 10.1093/emboj/cdf457
URL : http://emboj.embopress.org/content/embojnl/21/17/4449.full.pdf

M. Shepley and V. Racaniello, A monoclonal antibody that blocks poliovirus attachment recognized the lymphocyte homing receptor CD44, 1994.

M. Freistadt and K. Eberle, Physical association between CD155 and CD44 in human monocytes, Molecular Immunology, vol.34, issue.18, pp.1247-1257, 1997.
DOI : 10.1016/S0161-5890(98)00003-0

R. Pilpa, M. Bayrhuber, J. Marlett, R. Riek, and J. Young, A Receptor-based Switch that Regulates Anthrax Toxin Pore Formation, PLoS Pathogens, vol.110, issue.12, p.1002354, 2011.
DOI : 10.1371/journal.ppat.1002354.s006
URL : https://doi.org/10.1371/journal.ppat.1002354

H. Scobie and J. Young, Interactions between anthrax toxin receptors and protective antigen, Current Opinion in Microbiology, vol.8, issue.1, pp.106-112, 2005.
DOI : 10.1016/j.mib.2004.12.005

E. Pure and C. Cuff, A crucial role for CD44 in inflammation, Trends in Molecular Medicine, vol.7, issue.5, pp.213-221, 2001.
DOI : 10.1016/S1471-4914(01)01963-3

D. Blocker, H. Barth, E. Maier, R. Benz, and J. Barbieri, The C Terminus of Component C2II of Clostridium botulinum C2 Toxin Is Essential for Receptor Binding, Infection and Immunity, vol.68, issue.8, pp.4566-4573, 2000.
DOI : 10.1128/IAI.68.8.4566-4573.2000

K. Heine, S. Pust, S. Enzenmuller, and H. Barth, ADP-Ribosylation of Actin by the Clostridium botulinum C2 Toxin in Mammalian Cells Results in Delayed Caspase-Dependent Apoptotic Cell Death, Infection and Immunity, vol.76, issue.10, pp.4600-4608, 2008.
DOI : 10.1128/IAI.00651-08

U. Protin, T. Schweighoffer, W. Jochum, and F. Hilberg, CD44-deficient mice develop normally with changes in subpopulations and recirculation of lymphocyte subsets, J Immunol, vol.163, pp.4917-4923, 1999.