P. D. Adams, P. V. Afonine, G. Bunkó-czi, V. B. Chen, I. W. Davis et al., PHENIX: a comprehensive Python-based system for macromolecular structure solution, Acta Crystallographica Section D Biological Crystallography, vol.66, pp.213-221, 2010.

W. W. Ahmed, E. Fodor, M. Almonacid, M. Bussonier, M. H. Verlhac et al., Active mechanics reveal molecular-scale force kinetics in living oocytes, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02379042

M. Almonacid, W. W. Ahmed, M. Bussonnier, P. Mailly, T. Betz et al., Active diffusion positions the nucleus in mouse oocytes, Nature Cell Biology, vol.17, pp.470-479, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02107077

K. Austen, P. Ringer, A. Mehlich, A. Chrostek-grashoff, C. Kluger et al., Extracellular rigidity sensing by talin isoform-specific mechanical linkages, Nature Cell Biology, vol.17, pp.1597-1606, 2015.

G. Bricogne, E. Blanc, M. Brandl, C. Flensburg, P. Keller et al.,

J. J. Bultema, J. A. Boyle, P. B. Malenke, F. E. Martin, E. C. Dell'angelica et al., Myosin vc interacts with Rab32 and Rab38 proteins and works in the biogenesis and secretion of melanosomes, Journal of Biological Chemistry, vol.289, pp.33513-33528, 2014.

J. Cheng, A. Grassart, and D. G. Drubin, Myosin 1E coordinates actin assembly and cargo trafficking during clathrin-mediated endocytosis, Molecular Biology of the Cell, vol.23, pp.2891-2904, 2012.

S. S. Correia, S. Bassani, T. C. Brown, M. F. Lisé, D. S. Backos et al., Motor protein-dependent transport of AMPA receptors into spines during long-term potentiation, Nature Neuroscience, vol.11, pp.457-466, 2008.

S. V. Costes, D. Daelemans, E. H. Cho, Z. Dobbin, G. Pavlakis et al., Automatic and quantitative measurement of protein-protein colocalization in live cells, Biophysical Journal, vol.86, pp.3993-4003, 2004.

G. E. Crooks, G. Hon, J. M. Chandonia, and S. E. Brenner, WebLogo: a sequence logo generator, Genome Research, vol.14, pp.1188-1190, 2004.

S. Dietrich, S. Weiß, S. Pleiser, and E. Kerkhoff, Structural and functional insights into the Spir/formin actin nucleator complex, Biological Chemistry, vol.394, pp.1649-1660, 2013.

P. Emsley and K. Cowtan, Coot: model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, pp.2126-2132, 2004.

J. A. Hammer and W. Wagner, Functions of class V myosins in neurons, Journal of Biological Chemistry, vol.288, pp.28428-28434, 2013.

W. Kabsch, Xds. Acta Crystallographica Section D Biological Crystallography, vol.66, pp.125-132, 2010.

E. Kerkhoff, J. C. Simpson, C. B. Leberfinger, I. M. Otto, T. Doerks et al., The Spir actin organizers are involved in vesicle transport processes, Current Biology, vol.11, pp.602-611, 2001.

M. Kukimoto-niino, A. Sakamoto, E. Kanno, K. Hanawa-suetsugu, T. Terada et al., Structural basis for the exclusive specificity of Slac2-a/melanophilin for the Rab27 GTPases, Structure, vol.16, pp.1478-1490, 2008.

L. A. Lapierre, R. Kumar, C. M. Hales, J. Navarre, S. G. Bhartur et al., Myosin Vb is associated with plasma membrane recycling systems, Molecular Biology of the Cell, vol.12, pp.1843-1857, 2001.

W. Li and A. Godzik, Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences, Bioinformatics, vol.22, pp.1658-1659, 2006.

X. D. Li, H. S. Jung, Q. Wang, R. Ikebe, R. Craig et al., The globular tail domain puts on the brake to stop the ATPase cycle of myosin Va, PNAS, vol.105, pp.1140-1145, 2008.

A. J. Lindsay, F. Jollivet, C. P. Horgan, A. R. Khan, G. Raposo et al., Identification and characterization of multiple novel Rab-myosin Va interactions, Molecular Biology of the Cell, vol.24, pp.3420-3434, 2013.

J. Liu, D. W. Taylor, E. B. Krementsova, K. M. Trybus, and K. A. Taylor, Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography, Nature, vol.442, pp.208-211, 2006.

U. Manor, S. Bartholomew, G. Golani, E. Christenson, M. Kozlov et al., A mitochondria-anchored isoform of the actin-nucleating spire protein regulates mitochondrial division, vol.4, p.8828, 2015.

S. Namgoong, M. Boczkowska, M. J. Glista, J. D. Winkelman, G. Rebowski et al., Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation, Nature Structural & Molecular Biology, vol.18, pp.1060-1067, 2011.

A. F. Nascimento, D. M. Trindade, C. C. Tonoli, P. O. De-giuseppe, L. H. Assis et al., Structural insights into functional overlapping and differentiation among myosin V motors, Journal of Biological Chemistry, vol.288, pp.34131-34145, 2013.

I. M. Otto, T. Raabe, U. E. Rennefahrt, P. Bork, U. R. Rapp et al., The p150-Spir protein provides a link between c-Jun N-terminal kinase function and actin reorganization, Current Biology, vol.10, pp.388-390, 2000.

D. Pathak, K. J. Sepp, and P. J. Hollenbeck, Evidence that myosin activity opposes microtubule-based axonal transport of mitochondria, Journal of Neuroscience, vol.30, pp.8984-8992, 2010.

M. Pechlivanis, A. Samol, and E. Kerkhoff, Identification of a short Spir interaction sequence at the C-terminal end of formin subgroup proteins, Journal of Biological Chemistry, vol.284, pp.25324-25333, 2009.

S. Pfender, V. Kuznetsov, S. Pleiser, E. Kerkhoff, and M. Schuh, Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division, Current Biology, vol.21, pp.955-960, 2011.

S. N. Pompey, P. Michaely, and K. Luby-phelps, Quantitative fluorescence co-localization to study proteinreceptor complexes, Methods in Molecular Biology, vol.1008, pp.439-453, 2013.

O. Pylypenko, W. Attanda, C. Gauquelin, M. Lahmani, D. Coulibaly et al., Structural basis of myosin V Rab GTPase-dependent cargo recognition, PNAS, vol.110, pp.20443-20448, 2013.
URL : https://hal.archives-ouvertes.fr/hal-02349624

M. E. Quinlan, S. Hilgert, A. Bedrossian, R. D. Mullins, and E. Kerkhoff, Regulatory interactions between two actin nucleators, Spire and Cappuccino, Journal of Cell Biology, vol.179, pp.117-128, 2007.

J. T. Roland, L. A. Lapierre, and J. R. Goldenring, Alternative splicing in class V myosins determines association with Rab10, Journal of Biological Chemistry, vol.284, pp.1213-1223, 2009.

J. T. Roland, D. M. Bryant, A. Datta, A. Itzen, K. E. Mostov et al., Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization, PNAS, vol.108, pp.2789-2794, 2011.

M. Schuh, An actin-dependent mechanism for long-range vesicle transport, Nature Cell Biology, vol.13, pp.1431-1436, 2011.

N. Schumacher, J. M. Borawski, C. B. Leberfinger, M. Gessler, and E. Kerkhoff, Overlapping expression pattern of the actin organizers Spir-1 and formin-2 in the developing mouse nervous system and the adult brain, Gene Expression Patterns, vol.4, pp.249-255, 2004.

T. L. Schwarz, Mitochondrial trafficking in neurons, Cold Spring Harbor Perspectives in Biology, vol.5, p.11304, 2013.

N. C. Shaner, G. G. Lambert, A. Chammas, Y. Ni, P. J. Cranfill et al., A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum, Nature Methods, vol.10, pp.407-409, 2013.

Z. H. Sheng, Mitochondrial trafficking and anchoring in neurons: New insight and implications, Journal of Cell Biology, vol.204, pp.1087-1098, 2014.

V. Sirotkin, C. C. Beltzner, J. B. Marchand, and T. D. Pollard, Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast, Journal of Cell Biology, vol.170, pp.637-648, 2005.

Y. Sun, A. C. Martin, and D. G. Drubin, Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity, Developmental Cell, vol.11, pp.33-46, 2006.

Y. Sun, C. Rombola, V. Jyothikumar, and A. Periasamy, Fö rster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells, Cytometry Part A, vol.83, pp.780-793, 2013.

K. Thirumurugan, T. Sakamoto, J. A. Hammer, J. R. Sellers, and P. J. Knight, The cargo-binding domain regulates structure and activity of myosin 5, Nature, vol.442, pp.212-215, 2006.

J. Tittel, T. Welz, A. Czogalla, S. Dietrich, A. Samol-wolf et al., Membrane targeting of the SpirÁformin actin nucleator complex requires a sequential handshake of polar interactions, Journal of Biological Chemistry, vol.290, pp.6428-6444, 2015.

A. Vagin and A. Teplyakov, Molecular replacement with MOLREP, Acta Crystallographica Section D Biological Crystallography, vol.66, pp.22-25, 2010.

Z. Wang, J. G. Edwards, N. Riley, D. W. Provance, R. Karcher et al., Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity, Cell, vol.135, pp.535-548, 2008.

Z. Wei, X. Liu, C. Yu, and M. Zhang, Structural basis of cargo recognitions for class V myosins, PNAS, vol.110, pp.11314-11319, 2013.

T. Welz, J. Wellbourne-wood, and E. Kerkhoff, Orchestration of cell surface proteins by Rab11, Trends in Cell Biology, vol.24, pp.407-415, 2014.

L. Yao, Q. Cao, H. Zhang, J. Zhang, Y. Cao et al., Melanophilin stimulates myosin-5a motor function by allosterically inhibiting the interaction between the head and tail of myosin-5a, Scientific Reports, vol.5, p.10874, 2015.

W. B. Zhang, L. L. Yao, and X. D. Li, The globular tail domain of myosin-5a functions as a dimer in regulating the motor activity, Journal of Biological Chemistry, vol.291, pp.13571-13579, 2016.

D. Zimmermann, A. Santos, D. R. Kovar, and R. S. Rock, Actin age orchestrates myosin-5 and myosin-6 run lengths, Current Biology, vol.25, pp.2057-2062, 2015.