C. P. Brangwynne, C. R. Eckmann, D. S. Courson, A. Rybarska, C. Hoege et al., Germline P Granules Are Liquid Droplets That Localize by Controlled Dissolution/Condensation, Science, vol.324, issue.5935, pp.1729-1732, 2009.

A. A. Hyman and K. Simons, Beyond Oil and Water--Phase Transitions in Cells, Science, vol.337, issue.6098, pp.1047-1049, 2012.

L. P. Bergeron-sandoval, N. Safaee, and S. W. Michnick, Mechanisms and Consequences of Macromolecular Phase Separation, Cell, vol.165, issue.5, pp.1067-1079, 2016.

A. Putnam, M. Cassani, J. Smith, and G. Seydoux, A gel phase promotes condensation of liquid P granules in Caenorhabditis elegans embryos, Nature Structural & Molecular Biology, vol.26, issue.3, pp.220-226, 2019.

D. C. Tatomer, E. Terzo, K. P. Curry, H. Salzler, I. Sabath et al., Concentrating pre-mRNA processing factors in the histone locus body facilitates efficient histone mRNA biogenesis, Journal of Cell Biology, vol.213, issue.5, pp.557-570, 2016.

C. A. Strulson, R. C. Molden, C. D. Keating, and P. C. Bevilacqua, RNA catalysis through compartmentalization, Nature Chemistry, vol.4, issue.11, pp.941-946, 2012.

I. Novotný, M. Bla?íková, D. Stane?k, P. Herman, and J. Malinsky, In vivo kinetics of U4/U6·U5 tri-snRNP formation in Cajal bodies, Molecular Biology of the Cell, vol.22, issue.4, pp.513-523, 2011.

X. Su, J. A. Ditlev, E. Hui, W. Xing, S. Banjade et al., Phase separation of signaling molecules promotes T cell receptor signal transduction, Science, vol.352, issue.6285, pp.595-599, 2016.

A. Molliex, J. Temirov, J. Lee, M. Coughlin, A. P. Kanagaraj et al., Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization, Cell, vol.163, issue.1, pp.123-133, 2015.

S. Wegmann, B. Eftekharzadeh, K. Tepper, K. M. Zoltowska, R. E. Bennett et al., Tau protein liquid?liquid phase separation can initiate tau aggregation, The EMBO Journal, vol.37, issue.7, p.98049, 2018.

J. Wang, J. M. Choi, A. S. Holehouse, H. O. Lee, X. Zhang et al., A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins, Cell, vol.174, issue.3, pp.688-699.e16, 2018.

L. Zhu and C. P. Brangwynne, Nuclear bodies: the emerging biophysics of nucleoplasmic phases, Current Opinion in Cell Biology, vol.34, pp.23-30, 2015.

D. Stan?k and A. H. Fox, Nuclear bodies: news insights into structure and function, Current Opinion in Cell Biology, vol.46, pp.94-101, 2017.

M. Kato, T. W. Han, S. Xie, K. Shi, X. Du et al., Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels, Cell, vol.149, issue.4, pp.753-767, 2012.

A. Aguzzi and M. Altmeyer, Phase Separation: Linking Cellular Compartmentalization to Disease, Trends in Cell Biology, vol.26, issue.7, pp.547-558, 2016.

Y. Lin, D. S. Protter, M. K. Rosen, and R. Parker, Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins, Molecular Cell, vol.60, issue.2, pp.208-219, 2015.

S. Maharana, J. Wang, D. K. Papadopoulos, D. Richter, A. Pozniakovsky et al., RNA buffers the phase separation behavior of prion-like RNA binding proteins, Science, vol.360, issue.6391, pp.918-921, 2018.

J. C. Schwartz, X. Wang, E. R. Podell, and T. R. Cech, RNA Seeds Higher-Order Assembly of FUS Protein, Cell Reports, vol.5, issue.4, pp.918-925, 2013.

P. R. Banerjee, A. N. Milin, M. M. Moosa, P. L. Onuchic, and A. A. Deniz, Frontispiece: Reentrant Phase Transition Drives Dynamic Substructure Formation in Ribonucleoprotein Droplets, Angewandte Chemie International Edition, vol.56, issue.38, pp.11354-11359, 2017.

B. Van-treeck and R. Parker, Emerging Roles for Intermolecular RNA-RNA Interactions in RNP Assemblies, Cell, vol.174, issue.4, pp.791-802, 2018.

A. Patel, L. Malinovska, S. Saha, J. Wang, S. Alberti et al., ATP as a biological hydrotrope, Science, vol.356, issue.6339, pp.753-756, 2017.

J. R. Mann, A. M. Gleixner, J. C. Mauna, E. Gomes, M. R. Dechellis-marks et al., RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43, Neuron, vol.102, issue.2, pp.321-338.e8, 2019.

E. M. Langdon, Y. Qiu, A. Ghanbari-niaki, G. A. Mclaughlin, C. A. Weidmann et al., mRNA structure determines specificity of a polyQ-driven phase separation, Science, vol.360, issue.6391, pp.922-927, 2018.

A. Jain and R. D. Vale, RNA phase transitions in repeat expansion disorders, Nature, vol.546, issue.7657, pp.243-247, 2017.

T. Pawson and P. Nash, Assembly of Cell Regulatory Systems Through Protein Interaction Domains, Science, vol.300, issue.5618, pp.445-452, 2003.

T. S. Harmon, A. S. Holehouse, M. K. Rosen, and R. V. Pappu, Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins, eLife, vol.6, p.30294, 2017.

P. Li, S. Banjade, H. C. Cheng, S. Kim, B. Chen et al., Phase transitions in the assembly of multivalent signalling proteins, Nature, vol.483, issue.7389, pp.336-340, 2012.

M. Yamabhai, N. G. Hoffman, N. L. Hardison, P. S. Mcpherson, L. Castagnoli et al., Intersectin, a Novel Adaptor Protein with Two Eps15 Homology and Five Src Homology 3 Domains, Journal of Biological Chemistry, vol.273, issue.47, pp.31401-31407, 1998.

E. Herrero-garcia and J. P. O'bryan, Intersectin scaffold proteins and their role in cell signaling and endocytosis, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1864, issue.1, pp.23-30, 2017.

O. Gubar, D. Morderer, L. Tsyba, P. Croisé, S. Houy et al., Intersectin: The Crossroad between Vesicle Exocytosis and Endocytosis, Frontiers in Endocrinology, vol.4, p.109, 2013.
URL : https://hal.archives-ouvertes.fr/hal-02323390

B. Jakob, G. Kochlamazashvili, M. Jäpel, A. Gauhar, H. H. Bock et al., Intersectin 1 is a component of the Reelin pathway to regulate neuronal migration and synaptic plasticity in the hippocampus, Proceedings of the National Academy of Sciences, vol.114, issue.21, pp.5533-5538, 2017.

Y. Yu, P. Y. Chu, D. N. Bowser, D. J. Keating, D. Dubach et al., Mice deficient for the chromosome 21 ortholog Itsn1 exhibit vesicle-trafficking abnormalities, Human Molecular Genetics, vol.17, issue.21, pp.3281-3290, 2008.

G. Alvisi, L. Paolini, A. Contarini, C. Zambarda, V. Di-antonio et al., Intersectin goes nuclear: secret life of an endocytic protein, Biochemical Journal, vol.475, issue.8, pp.1455-1472, 2018.

B. Asbach, C. Ludwig, K. Saksela, and R. Wagner, Comprehensive Analysis of Interactions between the Src-Associated Protein in Mitosis of 68 kDa and the Human Src-Homology 3 Proteome, PLoS ONE, vol.7, issue.6, p.e38540, 2012.

K. A. Wong, J. Wilson, A. Russo, L. Wang, M. N. Okur et al., Intersectin (ITSN) Family of Scaffolds Function as Molecular Hubs in Protein Interaction Networks, PLoS ONE, vol.7, issue.4, p.e36023, 2012.

S. Thalappilly, M. Suliman, O. Gayet, P. Soubeyran, A. Hermant et al., Identification of multi-SH3 domain-containing protein interactome in pancreatic cancer: A yeast two-hybrid approach, PROTEOMICS, vol.8, issue.15, pp.3071-3081, 2008.

N. H. Meyer, K. Tripsianes, M. Vincendeau, T. Madl, F. Kateb et al., Structural Basis for Homodimerization of the Src-associated during Mitosis, 68-kDa Protein (Sam68) Qua1 Domain, Journal of Biological Chemistry, vol.285, issue.37, pp.28893-28901, 2010.

M. Feracci, J. N. Foot, S. N. Grellscheid, M. Danilenko, R. Stehle et al., Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68, Nature Communications, vol.7, issue.1, p.10355, 2016.

T. Chen, B. B. Damaj, C. Herrera, P. Lasko, and S. Richard, Self-association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domain., Molecular and Cellular Biology, vol.17, issue.10, pp.5707-5718, 1997.

T. Chen, F. M. Boisvert, D. P. Bazett-jones, and S. Richard, A Role for the GSG Domain in Localizing Sam68 to Novel Nuclear Structures in Cancer Cell Lines, Molecular Biology of the Cell, vol.10, issue.9, pp.3015-3033, 1999.

M. Boca, D. A. Kretov, B. Desforges, A. Mephon-gaspard, P. A. Curmi et al., Probing protein interactions in living mammalian cells on a microtubule bench, Scientific Reports, vol.5, issue.1, p.17304, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02272729

A. Maucuer, B. Desforges, V. Joshi, M. Boca, D. A. Kretov et al., Microtubules as platforms for probing liquid?liquid phase separation in cells ? application to RNA-binding proteins, Journal of Cell Science, vol.131, issue.11, p.jcs214692, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02166855

O. Dergai, O. Novokhatska, M. Dergai, I. Skrypkina, L. Tsyba et al., Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits, Biochemical and Biophysical Research Communications, vol.402, issue.2, pp.408-413, 2010.

M. Dergai, L. Tsyba, O. Dergai, I. Zlatskii, I. Skrypkina et al., Microexon-based regulation of ITSN1 and Src SH3 domains specificity relies on introduction of charged amino acids into the interaction interface, Biochemical and Biophysical Research Communications, vol.399, issue.2, pp.307-312, 2010.

O. Nikolaienko, I. Skrypkina, L. Tsyba, Y. Fedyshyn, D. Morderer et al., Intersectin 1 forms a complex with adaptor protein Ruk/CIN85 in vivo independently of epidermal growth factor stimulation, Cellular Signalling, vol.21, issue.5, pp.753-759, 2009.

J. Moffat, D. A. Grueneberg, X. Yang, S. Y. Kim, A. M. Kloepfer et al., A Lentiviral RNAi Library for Human and Mouse Genes Applied to an Arrayed Viral High-Content Screen, Cell, vol.124, issue.6, pp.1283-1298, 2006.

J. P. Venables, C. Dalgliesh, M. P. Paronetto, L. Skitt, J. K. Thornton et al., SIAH1 targets the alternative splicing factor T-STAR for degradation by the proteasome, Human Molecular Genetics, vol.13, issue.14, pp.1525-1534, 2004.

M. Llorian, M. Beullens, B. Lesage, E. Nicolaescu, L. Beke et al., Nucleocytoplasmic Shuttling of the Splicing Factor SIPP1, Journal of Biological Chemistry, vol.280, issue.46, pp.38862-38869, 2005.

R. Shao, S. J. Scully, W. Yan, B. W. Bentley, J. Mueller et al., The novel lupus antigen related protein acheron enhances the development of human breast cancer, International Journal of Cancer, vol.130, issue.3, pp.544-554, 2011.

S. Abrakhi, D. A. Kretov, B. Desforges, I. Dobra, A. Bouhss et al., Nanoscale Analysis Reveals the Maturation of Neurodegeneration-Associated Protein Aggregates: Grown in mRNA Granules then Released by Stress Granule Proteins, ACS Nano, vol.11, issue.7, pp.7189-7200, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02173623

W. F. Vranken, W. Boucher, T. J. Stevens, R. H. Fogh, A. Pajon et al., The CCPN data model for NMR spectroscopy: Development of a software pipeline, Proteins: Structure, Function, and Bioinformatics, vol.59, issue.4, pp.687-696, 2005.

P. Schanda and B. Brutscher, Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds, Journal of the American Chemical Society, vol.127, issue.22, pp.8014-8015, 2005.

S. J. Taylor and D. Shalloway, An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis, Nature, vol.368, issue.6474, pp.867-871, 1994.

S. Fumagalli, N. F. Totty, J. J. Hsuan, and S. A. Courtneidge, A target for Src in mitosis, Nature, vol.368, issue.6474, pp.871-874, 1994.

L. Hamon, D. Pastre, P. Dupaigne, C. L. Breton, E. L. Cam et al., High-resolution AFM imaging of single-stranded DNA-binding (SSB) protein--DNA complexes, Nucleic Acids Research, vol.35, issue.8, pp.e58-e58, 2007.
URL : https://hal.archives-ouvertes.fr/hal-02295472

A. Lin, C. Li, Z. Xing, Q. Hu, K. Liang et al., The LINK-A lncRNA activates normoxic HIF1? signalling in triple-negative breast cancer, Nature Cell Biology, vol.18, issue.2, pp.213-224, 2016.

L. Tsyba, O. Nikolaienko, O. Dergai, M. Dergai, O. Novokhatska et al., Intersectin multidomain adaptor proteins: Regulation of functional diversity, Gene, vol.473, issue.2, pp.67-75, 2011.

J. O. Narcís, O. Tapia, O. Tarabal, L. Piedrafita, J. Calderó et al., Accumulation of poly(A) RNA in nuclear granules enriched in Sam68 in motor neurons from the SMN?7 mouse model of SMA, Scientific Reports, vol.8, issue.1, p.9646, 2018.

P. Thandapani, T. R. O?connor, T. L. Bailey, and S. Richard, Defining the RGG/RG Motif, Molecular Cell, vol.50, issue.5, pp.613-623, 2013.

P. A. Chong, R. M. Vernon, and J. D. Forman-kay, RGG/RG Motif Regions in RNA Binding and Phase Separation, Journal of Molecular Biology, vol.430, issue.23, pp.4650-4665, 2018.

I. A. Sawyer, D. Sturgill, and M. Dundr, Membraneless nuclear organelles and the search for phases within phases, Wiley Interdisciplinary Reviews: RNA, vol.10, issue.2, p.e1514, 2018.

C. Naro, L. Pellegrini, A. Jolly, D. Farini, E. Cesari et al., Functional Interaction between U1snRNP and Sam68 Insures Proper 3? End Pre-mRNA Processing during Germ Cell Differentiation, Cell Reports, vol.26, issue.11, pp.2929-2941.e5, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02082557

Z. Monahan, V. H. Ryan, A. M. Janke, K. A. Burke, S. N. Rhoads et al., Phosphorylation of the FUS low?complexity domain disrupts phase separation, aggregation, and toxicity, The EMBO Journal, vol.36, issue.20, pp.2951-2967, 2017.

P. Frisone, D. Pradella, A. Di-matteo, E. Belloni, C. Ghigna et al., SAM68: Signal Transduction and RNA Metabolism in Human Cancer, BioMed Research International, vol.2015, pp.1-14, 2015.

N. Nagaraj, J. R. Wisniewski, T. Geiger, J. Cox, M. Kircher et al., Deep proteome and transcriptome mapping of a human cancer cell line, Molecular Systems Biology, vol.7, issue.1, p.548, 2011.

M. Uhlen, P. Oksvold, L. Fagerberg, E. Lundberg, K. Jonasson et al., Towards a knowledge-based Human Protein Atlas, Nature Biotechnology, vol.28, issue.12, pp.1248-1250, 2010.

A. S. Sengar, J. Ellegood, A. P. Yiu, H. Wang, W. Wang et al., Vertebrate Intersectin1 Is Repurposed to Facilitate Cortical Midline Connectivity and Higher Order Cognition, Journal of Neuroscience, vol.33, issue.9, pp.4055-4065, 2013.

F. Sánchez-jiménez and V. Sánchez-margalet, Role of Sam68 in Post-Transcriptional Gene Regulation, International Journal of Molecular Sciences, vol.14, issue.12, pp.23402-23419, 2013.

S. Pedrotti, P. Bielli, M. P. Paronetto, F. Ciccosanti, G. M. Fimia et al., The splicing regulator Sam68 binds to a novel exonic splicing silencer and functions in SMN2 alternative splicing in spinal muscular atrophy, The EMBO Journal, vol.29, issue.7, pp.1235-1247, 2010.

C. Sellier, F. Rau, Y. Liu, F. Tassone, R. K. Hukema et al., Sam68 sequestration and partial loss of function are associated with splicing alterations in FXTAS patients, The EMBO Journal, vol.29, issue.7, pp.1248-1261, 2010.