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, pp.7189-7200, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02173623

A. Aguzzi and M. Altmeyer, Phase separation: linking cellular compartmentalization to disease, Trends Cell Biol, vol.26, pp.547-558, 2016.

M. Altmeyer, K. J. Neelsen, F. Teloni, I. Pozdnyakova, S. Pellegrino et al., , 2015.

, Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose), Nat. Commun, vol.6, p.8088

S. Ambadipudi, J. Biernat, D. Riedel, E. Mandelkow, and M. Zweckstetter, Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau, Nat. Commun, vol.8, p.275, 2017.

A. Aulas and C. Vande-velde, Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS? Front, Cell Neurosci, vol.9, p.423, 2015.

A. Aulas, G. Caron, C. G. Gkogkas, N. Mohamed, L. Destroismaisons et al., G3BP1 promotes stress-induced RNA granule interactions to preserve polyadenylated mRNA, J. Cell Biol, vol.209, pp.73-84, 2015.

W. M. Aumiller, J. Keating, and C. D. , Phosphorylation-mediated RNA/ peptide complex coacervation as a model for intracellular liquid organelles, Nat. Chem, vol.8, pp.129-137, 2016.

S. F. Banani, A. M. Rice, W. B. Peeples, Y. Lin, S. Jain et al., Compositional control of phase-separated cellular bodies, Cell, vol.166, pp.651-663, 2016.

L. Bergeron-sandoval, N. Safaee, and S. W. Michnick, Mechanisms and consequences of macromolecular phase separation, Cell, vol.165, pp.1067-1079, 2016.

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, Sci. Rep, vol.5, p.17304, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02272729

O. Bounedjah, L. Hamon, P. Savarin, B. Desforges, P. A. Curmi et al., Macromolecular crowding regulates assembly of mRNA stress granules after osmotic stress: new role for compatible osmolytes, J. Biol. Chem, vol.287, pp.2446-2458, 2012.
URL : https://hal.archives-ouvertes.fr/hal-02292253

O. Bounedjah, B. Desforges, T. Wu, C. Pioche-durieu, S. Marco et al., , 2014.

, Free mRNA in excess upon polysome dissociation is a scaffold for protein multimerization to form stress granules, Nucleic Acids Res, vol.42, pp.8678-8691

K. A. Butner and M. W. Kirschner, Tau protein binds to microtubules through a flexible array of distributed weak sites, J. Cell Biol, vol.115, pp.717-730, 1991.

A. Castello, B. Fischer, C. K. Frese, R. Horos, A. Alleaume et al., Comprehensive identification of RNA-binding domains in human cells, Mol. Cell, vol.63, pp.696-710, 2016.

A. E. Conicella, G. H. Zerze, J. Mittal, and N. L. Fawzi, ALS mutations disrupt phase separation mediated by alpha-helical structure in the TDP-43 lowcomplexity C-terminal domain, Structure, vol.24, pp.1537-1549, 2016.

M. Feric, N. Vaidya, T. S. Harmon, D. M. Mitrea, L. Zhu et al., Coexisting liquid phases underlie nucleolar subcompartments, Cell, vol.165, pp.1686-1697, 2016.

E. J. Fialcowitz-white, B. Y. Brewer, J. D. Ballin, C. D. Willis, E. A. Toth et al., Specific protein domains mediate cooperative assembly of HuR oligomers on AU-rich mRNA-destabilizing sequences, J. Biol. Chem, vol.282, pp.20948-20959, 2007.

A. H. Fox, S. Nakagawa, T. Hirose, and C. S. Bond, Paraspeckles: where long noncoding RNA meets phase separation, Trends Biochem. Sci, vol.43, pp.124-135, 2018.

A. P. French, S. Mills, R. Swarup, M. J. Bennett, and T. P. Pridmore, Colocalization of fluorescent markers in confocal microscope images of plant cells, Nat. Protoc, vol.3, pp.619-628, 2008.

P. P. Gopal, J. J. Nirschl, E. Klinman, and E. L. Holzbaur, Amyotrophic lateral sclerosis-linked mutations increase the viscosity of liquid-like TDP-43 RNP granules in neurons, Proc. Natl. Acad. Sci. USA, vol.114, pp.2466-2475, 2017.

S. Gueroussov, R. J. Weatheritt, D. O'hanlon, Z. Y. Lin, A. Narula et al., Regulatory expansion in mammals of multivalent hnRNP assemblies that globally control alternative splicing, Cell, vol.170, pp.324-339, 2017.

S. Hennig, G. Kong, T. Mannen, A. Sadowska, S. Kobelke et al., Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles, J. Cell Biol, vol.210, pp.529-539, 2015.

D. Hnisz, K. Shrinivas, R. A. Young, A. K. Chakraborty, and P. A. Sharp, A phase separation model for transcriptional control, Cell, vol.169, pp.13-23, 2017.

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

S. Jain, J. R. Wheeler, R. W. Walters, A. Agrawal, A. Barsic et al., ATPase-modulated stress granules contain a diverse proteome and substructure, Cell, vol.164, pp.487-498, 2016.

D. Janning, M. Igaev, F. Sundermann, J. Bruhmann, O. Beutel et al., Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons, Mol. Biol. Cell, vol.25, pp.3541-3551, 2014.

T. Kampers, P. Friedhoff, J. Biernat, E. Mandelkow, and E. Mandelkow, RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments, FEBS Lett, vol.399, pp.344-349, 1996.

N. Kedersha, S. Chen, N. Gilks, W. Li, I. J. Miller et al., Evidence that ternary complex (eIF2-GTP-tRNA(i)(Met))-deficient preinitiation complexes are core constituents of mammalian stress granules, Mol. Biol. Cell, vol.13, pp.195-210, 2002.

N. Kedersha, M. D. Panas, C. A. Achorn, S. Lyons, S. Tisdale et al., G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits, J. Cell Biol, vol.212, pp.845-860, 2016.

S. H. Kim, N. P. Shanware, M. J. Bowler, and R. S. Tibbetts, Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA, J. Biol. Chem, vol.285, pp.34097-34105, 2010.

G. Lee, R. L. Neve, and K. S. Kosik, The microtubule binding domain of tau protein, Neuron, vol.2, pp.1615-1624, 1989.

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

Y. R. Li, O. D. King, J. Shorter, and A. D. Gitler, Stress granules as crucibles of ALS pathogenesis, J. Cell Biol, vol.201, pp.361-372, 2013.

Y. Lin, D. S. Protter, M. K. Rosen, and R. Parker, Formation and maturation of phase-separated liquid droplets by RNA-binding proteins, Mol. Cell, vol.60, pp.208-219, 2015.

S. Markmiller, S. Soltanieh, K. L. Server, R. Mak, W. Jin et al., Context-dependent and diseasespecific diversity in protein interactions within stress granules, Cell, vol.172, pp.590-604, 2018.

D. Mateju, T. M. Franzmann, A. Patel, A. Kopach, E. E. Boczek et al., An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function, EMBO J, vol.36, pp.1669-1687, 2017.

A. Me?hon-gaspard, M. Boca, C. Pioche-durieu, B. Desforges, A. Burgo et al., Role of tau in the spatial organization of axonal microtubules: keeping parallel microtubules evenly distributed despite macromolecular crowding, Cell. Mol. Life Sci, vol.73, pp.3745-3760, 2016.

D. M. Mitrea and R. W. Kriwacki, Phase separation in biology; functional organization of a higher order, Cell Commun. Signal, vol.14, p.1, 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, pp.123-133, 2015.

T. Murakami, S. Qamar, J. Q. Lin, G. S. Schierle, E. Rees et al., ALS/FTD mutation-induced phase transition of fus liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function, Neuron, vol.88, pp.678-690, 2015.

D. T. Murray, M. Kato, Y. Lin, K. R. Thurber, I. Hung et al., Structure of FUS protein fibrils and its relevance to selfassembly and phase separation of low-complexity domains, Cell, vol.171, pp.615-627, 2017.

B. Niewidok, M. Igaev, A. Pereira-da-graca, A. Strassner, C. Lenzen et al., Single-molecule imaging reveals dynamic biphasic partition of RNA-binding proteins in stress granules, J. Cell Biol, vol.217, p.1303, 2018.

T. J. Nott, T. D. Craggs, and A. J. Baldwin, Membraneless organelles can melt nucleic acid duplexes and act as biomolecular filters, Nat. Chem, vol.8, pp.569-575, 2016.

C. W. Pak, M. Kosno, A. S. Holehouse, S. B. Padrick, A. Mittal et al., Sequence determinants of intracellular phase separation by complex coacervation of a disordered protein, Mol. Cell, vol.63, pp.72-85, 2016.

A. Patel, H. O. Lee, L. Jawerth, S. Maharana, M. Jahnel et al., A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation, Cell, vol.162, pp.1066-1077, 2015.

L. C. Reineke, N. Kedersha, M. A. Langereis, F. J. Van-kuppeveld, and R. E. Lloyd, Stress granules regulate double-stranded RNA-dependent protein kinase activation through a complex containing G3BP1 and Caprin1, MBio, vol.6, pp.2486-2500, 2015.

R. M. Scheiba, A. I. De-opakua, A. D?áz-quintana, I. Cruz-gallardo, L. A. Mart??ez-cruz et al., , 2014.

, The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets, RNA Biol, vol.11, pp.1250-1261

Y. Shin, J. Berry, N. Pannucci, M. P. Haataja, J. E. Toettcher et al., Spatiotemporal control of intracellular phase transitions using light-activated optoDroplets, Cell, vol.168, pp.159-171, 2017.

P. Strzyz, Organelle dynamics: controlling phase separation of P granules, Nat. Rev. Mol. Cell Biol, vol.18, p.4, 2016.

V. N. Uversky, Protein intrinsic disorder-based liquid-liquid phase transitions in biological systems: Complex coacervates and membrane-less organelles, Adv. Colloid Interface Sci, vol.239, pp.97-114, 2017.

B. Van-treeck, D. S. Protter, T. Matheny, A. Khong, C. D. Link et al., RNA self-assembly contributes to stress granule formation and defining the stress granule transcriptome, Proc. Natl. Acad. Sci. USA, vol.115, pp.2734-2739, 2018.

T. Vanderweyde, D. J. Apicco, K. Youmans-kidder, P. E. Ash, C. Cook et al., Interaction of tau with the RNA-binding protein TIA1 regulates tau pathophysiology and toxicity, Cell Rep, vol.15, pp.1455-1466, 2016.

J. A. West, M. Mito, S. Kurosaka, T. Takumi, C. Tanegashima et al., Structural, superresolution microscopy analysis of paraspeckle nuclear body organization, J. Cell Biol, vol.214, pp.817-830, 2016.

S. Xing, N. Wallmeroth, K. W. Berendzen, and C. Grefen, Techniques for the Analysis of Protein-Protein Interactions in Vivo, Plant Physiol, vol.171, pp.727-758, 2016.

Y. Ying, X. J. Wang, C. K. Vuong, C. H. Lin, A. Damianov et al., Splicing activation by Rbfox requires self-aggregation through its tyrosinerich domain, Cell, vol.170, pp.312-323, 2017.

J. Y. Youn, W. H. Dunham, S. J. Hong, J. D. Knight, M. Bashkurov et al., Highdensity proximity mapping reveals the subcellular organization of mRNAassociated granules and bodies, Mol. Cell, vol.69, pp.517-532, 2018.

H. Zhang, S. Elbaum-garfinkle, E. M. Langdon, N. Taylor, P. Occhipinti et al., RNA controls polyQ protein phase transitions, Mol. Cell, vol.60, pp.220-230, 2015.

L. Zhu and C. P. Brangwynne, Nuclear bodies: the emerging biophysics of nucleoplasmic phases, Curr. Opin. Cell Biol, vol.34, pp.23-30, 2015.