Axonal transport: Driving synaptic function

Molecular anatomy of a trafficking organelle

Takamori, S., Holt, M., Stenius, K., Lemke, E. A., Grønborg, M., Riedel, D., Urlaub, H., Schenck, S., Brügger, B., Ringler, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.030 · Cited by 2,373

Kinesin Transports RNA

Kanai, Y., Dohmae, N., & Hirokawa, N. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.022 · Cited by 1,109

Differential Regulation of Dynein and Kinesin Motor Proteins by Tau

Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012

Quantitative ultrastructural analysis of hippocampal excitatory synapses

Schikorski, T., & Stevens, C. F. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-15-05858.1997 · Cited by 997

Mutant dynactin in motor neuron disease

Puls, I., Jonnakuty, C., LaMonte, B. H., Holzbaur, E. L. F., Tokito, M. K., MANN, E. A., Floeter, M. K., Bidus, K., Drayna, D. T., Oh, S. J., et al. (2003) · Nature Genetics · doi:10.1038/ng1123 · Cited by 973

The Biology of Huntingtin

Saudou, F., & Humbert, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.02.003 · Cited by 945

Control of microtubule organization and dynamics: Two ends in the limelight

Akhmanova, A., & Steinmetz, M. O. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4084 · Cited by 895

The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility

Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871

Activity-driven local ATP synthesis is required for synaptic function

Rangaraju, V., Calloway, N., & Ryan, T. A. (2014) · Cell · doi:10.1016/j.cell.2013.12.042 · Cited by 836

Neuropeptide Transmission in Brain Circuits

van den Pol, A. N. (2012) · Neuron · doi:10.1016/j.neuron.2012.09.014 · Cited by 810

Polarity orientation of microtubules in hippocampal neurons: uniformity in the axon and nonuniformity in the dendrite

Baas, P. W., Deitch, J. S., Black, M. M., & Banker, G. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.8335 · Cited by 742

Visualization of Microtubule Growth in Cultured Neurons via the Use of EB3-GFP (End-Binding Protein 3-Green Fluorescent Protein)

Stepanova, T., Slemmer, J., Hoogenraad, C. C., Lansbergen, G. W. A., Dortland, B. R., Zeeuw, C. I. D., Grosveld, F. G., van Cappellen, G. W. A., Akhmanova, A. S., & Galjart, N. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02655.2003 · Cited by 702

Miro1 Is a Calcium Sensor for Glutamate Receptor-Dependent Localization of Mitochondria at Synapses

MacAskill, A. F., Rinholm, J. E., Twelvetrees, A. E., Arancibia‐Cárcamo, I. L., Muir, J., Fransson, Å., Aspenström, P., Attwell, D., & Kittler, J. T. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.030 · Cited by 687

Genome-Wide Analyses Identify KIF5A as a Novel ALS Gene

Nicolas, A., Kenna, K. P., Renton, A. E., Ticozzi, N., Faghri, F., Chia, R., Dominov, J. A., Kenna, B., Nalls, M. A., Keagle, P. J., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.02.027 · Cited by 686

Building the Neuronal Microtubule Cytoskeleton

Kapitein, L. C., & Hoogenraad, C. C. (2015) · Neuron · doi:10.1016/j.neuron.2015.05.046 · Cited by 684

Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons

Maday, S., Wallace, K. E., & Holzbaur, E. L. F. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201106120 · Cited by 681 · cited 3×

The cytoplasmic dynein transport machinery and its many cargoes

Reck‐Peterson, S. L., Redwine, W. B., Vale, R. D., & Carter, A. P. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0004-3 · Cited by 680

The neuron-specific kinesin superfamily protein KIF1A is a uniqye monomeric motor for anterograde axonal transport of synaptic vesicle precursors

Okada, Y., Yamazaki, H., Sekine‐Aizawa, Y., & Hirokawa, N. (1995) · Cell · doi:10.1016/0092-8674(95)90538-3 · Cited by 679

Kinetic Analysis of Secretory Protein Traffic and Characterization of Golgi to Plasma Membrane Transport Intermediates in Living Cells

Hirschberg, K., Miller, C. M., Ellenberg, J., Presley, J. F., Siggia, E. D., Phair, R. D., & Lippincott‐Schwartz, J. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.6.1485 · Cited by 610

Microtubule Stabilization Reduces Scarring and Causes Axon Regeneration After Spinal Cord Injury

Hellal, F., Hurtado, A., Ruschel, J., Flynn, K. C., Laskowski, C. J., Umlauf, M., Kapitein, L. C., Strikis, D., Lemmon, V., Bixby, J. L., et al. (2011) · Science · doi:10.1126/science.1201148 · Cited by 600

Microtubule dynamics: an interplay of biochemistry and mechanics

Brouhard, G. J., & Rice, L. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0009-y · Cited by 584

Activation of cytoplasmic dynein motility by dynactin-cargo adapter complexes

McKenney, R. J., Huynh, W., Tanenbaum, M. E., Bhabha, G., & Vale, R. D. (2014) · Science · doi:10.1126/science.1254198 · Cited by 571

Microtubule stabilization specifies initial neuronal polarization

Witte, H., Neukirchen, D., & Bradke, F. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707042 · Cited by 564

Mitostasis in Neurons: Maintaining Mitochondria in an Extended Cellular Architecture

Misgeld, T., & Schwarz, T. L. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.055 · Cited by 562

Activation of endosomal dynein motors by stepwise assembly of Rab7–RILP–p150Glued, ORP1L, and the receptor βlll spectrin

Johansson, M., Rocha, N., Zwart, W., Jordens, I., Janssen, L., Kuijl, C., Olkkonen, V. M., & Neefjes, J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606077 · Cited by 505

Microtubules acquire resistance from mechanical breakage through intralumenal acetylation

Xu, Z., Schaedel, L., Portran, D., Aguilar, A., Gaillard, J., Marinkovich, M. P., Théry, M., & Nachury, M. V. (2017) · Science · doi:10.1126/science.aai8764 · Cited by 505

Axonal mRNA localization and local protein synthesis in nervous system assembly, maintenance and repair

Jung, H., Yoon, B. C., & Holt, C. E. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3210 · Cited by 503

Cytoplasmic dynein functions as a gear in response to load

Mallik, R., Carter, B. C., Lex, S. A., King, S. J., & Gross, S. P. (2004) · Nature · doi:10.1038/nature02293 · Cited by 494

Tubulin acetylation protects long-lived microtubules against mechanical ageing

Portran, D., Schaedel, L., Xu, Z., Théry, M., & Nachury, M. V. (2017) · Nature Cell Biology · doi:10.1038/ncb3481 · Cited by 493

Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of cortical development and microcephaly

Poirier, K., Lebrun, N., Broix, L., Tian, G., Saillour, Y., Boscheron, C., Parrini, E., Valence, S., Saintpierre, B., Oger, M., et al. (2013) · Nature Genetics · doi:10.1038/ng.2613 · Cited by 479

Dynamic Axonal Translation in Developing and Mature Visual Circuits

Shigeoka, T., Jung, H., Jung, J., Turner-Bridger, B., Ohk, J., Lin, J. Q., Amieux, P. S., & Holt, C. E. (2016) · Cell · doi:10.1016/j.cell.2016.05.029 · Cited by 462

TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites

van Spronsen, M., Mikhaylova, M., Lipka, J., Schlager, M. A., van den Heuvel, D. J., Kuijpers, M., Wulf, P. S., Keijzer, N., Demmers, J., Kapitein, L. C., et al. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.027 · Cited by 450

Systemic administration of epothilone B promotes axon regeneration after spinal cord injury

Ruschel, J., Hellal, F., Flynn, K. C., Dupraz, S., Elliott, D. A., Tedeschi, A., Bates, M., Sliwinski, C., Brook, G. A., Dobrindt, K., et al. (2015) · Science · doi:10.1126/science.aaa2958 · Cited by 444

Late Endosomes Act as mRNA Translation Platforms and Sustain Mitochondria in Axons

Cioni, J.-M., Lin, J. Q., Holtermann, A., Koppers, M., Jakobs, M. A., Azizi, A., Turner-Bridger, B., Shigeoka, T., Franze, K., Harris, W. A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.11.030 · Cited by 444

Motor coordination via a tug-of-war mechanism drives bidirectional vesicle transport

Hendricks, A. G., Perlson, E., Ross, J. L., Schroeder, H. W., Tokito, M., & Holzbaur, E. L. F. (2010) · Current Biology · doi:10.1016/j.cub.2010.02.058 · Cited by 423

The structure of the dynactin complex and its interaction with dynein

Urnavicius, L., Zhang, K., Diamant, A. G., Motz, C., Schlager, M. A., Yu, M., Patel, N. A., Robinson, C. V., & Carter, A. P. (2015) · Science · doi:10.1126/science.aaa4080 · Cited by 421

Near-atomic model of microtubule-tau interactions

Kellogg, E. H., Hejab, N. M. A., Poepsel, S., Downing, K. H., DiMaio, F., & Nogales, E. (2018) · Science · doi:10.1126/science.aat1780 · Cited by 416

A Family of Protein-Deglutamylating Enzymes Associated with Neurodegeneration

Rogowski, K., van Dijk, J., Magiera, M. M., Bosc, C., Deloulme, J., Bosson, A., Peris, L., Gold, N. D., Lacroix, B., Bosch, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.10.014 · Cited by 397

Microtubule interaction site of the kinesin motor

Woehlke, G., Ruby, A. K., Hart, C. L., Ly, B., Hom-Booher, N., & Vale, R. D. (1997) · Cell · doi:10.1016/s0092-8674(00)80329-3 · Cited by 386

The Regulation of Autophagosome Dynamics by Huntingtin and HAP1 Is Disrupted by Expression of Mutant Huntingtin, Leading to Defective Cargo Degradation

Wong, Y., & Holzbaur, E. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1870-13.2014 · Cited by 380

Autophagosome Biogenesis in Primary Neurons Follows an Ordered and Spatially Regulated Pathway

Maday, S., & Holzbaur, E. L. F. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.001 · Cited by 372

Fueling thought: Management of glycolysis and oxidative phosphorylation in neuronal metabolism

Yellen, G. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201803152 · Cited by 371

Precisely measured protein lifetimes in the mouse brain reveal differences across tissues and subcellular fractions

Fornasiero, E. F., Mandad, S., Wildhagen, H., Alevra, M., Rammner, B., Keihani, S., Opazo, F., Urban, I., Ischebeck, T., Sakib, M. S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06519-0 · Cited by 356

In vitro reconstitution of a highly processive recombinant human dynein complex

Schlager, M. A., Hoang, H. T., Urnavicius, L., Bullock, S. L., & Carter, A. P. (2014) · The EMBO Journal · doi:10.15252/embj.201488792 · Cited by 351

Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin

Okada, Y., & Hirokawa, N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.640 · Cited by 350

A Targeted Multienzyme Mechanism for Selective Microtubule Polyglutamylation

van Dijk, J., Rogowski, K., Miro, J., Lacroix, B., Eddé, B., & Janke, C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.012 · Cited by 320

DCTN1 mutations in Perry syndrome

Farrer, M. J., Hulihan, M., Kachergus, J. M., Dächsel, J. C., Stoessl, A. J., Grantier, L. L., Calne, S. M., Calne, D. B., Lechevalier, B., Chapon, F., et al. (2009) · Nature Genetics · doi:10.1038/ng.293 · Cited by 320

The Axon Initial Segment: An Updated Viewpoint

Leterrier, C. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1922-17.2018 · Cited by 317

The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1).

Waterman, C. M., Karki, S., & Holzbaur, E. L. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1634 · Cited by 316

Causes and Consequences of Microtubule Acetylation

Janke, C., & Montagnac, G. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.044 · Cited by 316

Detection of GTP-Tubulin Conformation in Vivo Reveals a Role for GTP Remnants in Microtubule Rescues

Dimitrov, A., Quesnoit, M., Moutel, S., Cantaloube, I., Poüs, C., & Perez, F. (2008) · Science · doi:10.1126/science.1165401 · Cited by 313

Differentiation between oppositely oriented microtubules controls polarized neuronal transport

Tas, R. P., Chazeau, A., Cloin, B. M. C., Lambers, M. L. A., Hoogenraad, C. C., & Kapitein, L. C. (2017) · Neuron · doi:10.1016/j.neuron.2017.11.018 · Cited by 306

Super-Resolution Imaging of the Extracellular Space in Living Brain Tissue

Tønnesen, J., Inavalli, V. V. G. K., & Nägerl, U. V. (2018) · Cell · doi:10.1016/j.cell.2018.02.007 · Cited by 303

Axon Extension Occurs Independently of Centrosomal Microtubule Nucleation

Stieß, M., Maghelli, N., Kapitein, L. C., Gomis-Rüth, S., Wilsch‐Bräuninger, M., Hoogenraad, C. C., Tolić, I. M., & Bradke, F. (2010) · Science · doi:10.1126/science.1182179 · Cited by 299

Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated

Zhang, K., Foster, H. E., Rondelet, A., Lacey, S. E., Bahi‐Buisson, N., Bird, A. W., & Carter, A. P. (2017) · Cell · doi:10.1016/j.cell.2017.05.025 · Cited by 297

Changes in microtubule polarity orientation during the development of hippocampal neurons in culture.

Baas, P. W., Black, M. M., & Banker, G. A. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.6.3085 · Cited by 295

A vital role of tubulin-tyrosine-ligase for neuronal organization

Erck, C., Peris, L., Andrieux, A., Meissirel, C., Gruber, A. D., Vernet, M., Schweitzer, A., Saoudi, Y., Pointu, H., Bosc, C., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409626102 · Cited by 295

Microtubules self-repair in response to mechanical stress

Schaedel, L., John, K., Gaillard, J., Nachury, M. V., Blanchoin, L., & Théry, M. (2015) · Nature Materials · doi:10.1038/nmat4396 · Cited by 294

Characterization of LAMP1-labeled nondegradative lysosomal and endocytic compartments in neurons

Cheng, X.-T., Xie, Y.-X., Zhou, B., Huang, N., Farfel-Becker, T., & Sheng, Z.-H. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711083 · Cited by 294

Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation

Aillaud, C., Bosc, C., Peris, L., Bosson, A., Heemeryck, P., Van Dijk, J., Le Friec, J., Boulan, B., Vossier, F., Sanman, L. E., et al. (2017) · Science · doi:10.1126/science.aao4165 · Cited by 293

Microtubule Minus-End Stabilization by Polymerization-Driven CAMSAP Deposition

Jiang, K., Hua, S., Mohan, R., Grigoriev, I., Yau, K. W., Liu, Q., Katrukha, E. A., Altelaar, M. A. F., Heck, A. J. R., Hoogenraad, C. C., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.01.001 · Cited by 290

Dynein is required for polarized dendritic transport and uniform microtubule orientation in axons

Zheng, Y., Wildonger, J., Ye, B., Zhang, Y., Kita, A. M., Younger, S. H., Zimmerman, S., Jan, L. Y., & Jan, Y. N. (2008) · Nature Cell Biology · doi:10.1038/ncb1777 · Cited by 290

Molecular Adaptations Allow Dynein to Generate Large Collective Forces inside Cells

Rai, A. K., Rai, A., Ramaiya, A., Jha, R., & Mallik, R. (2013) · Cell · doi:10.1016/j.cell.2012.11.044 · Cited by 284

JIP1 regulates the directionality of APP axonal transport by coordinating kinesin and dynein motors

Fu, M., & Holzbaur, E. L. F. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302078 · Cited by 277

Cryo-EM shows how dynactin recruits two dyneins for faster movement

Urnavicius, L., Lau, C. K., Elshenawy, M. M., Morales‐Ríos, E., Motz, C., Yıldız, A., & Carter, A. P. (2018) · Nature · doi:10.1038/nature25462 · Cited by 277

Quantitative imaging of energy expenditure in human brain

Zhu, X., Qiao, H., Du, F., Xiong, Q., Liu, X., Zhang, X., Uǧurbil, K., & Chen, W. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.02.013 · Cited by 275

Mutations in the neuronal β-tubulin subunit TUBB3 result in malformation of cortical development and neuronal migration defects

Poirier, K., Saillour, Y., Bahi‐Buisson, N., Jaglin, X. H., Fallet‐Bianco, C., Nabbout, R., Castelnau, L., Roubertie, A., Attié‐Bitach, T., Desguerre, I., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq377 · Cited by 273

Cortical energy demands of signaling and nonsignaling components in brain are conserved across mammalian species and activity levels

Hyder, F., Rothman, D. L., & Bennett, M. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214912110 · Cited by 271

Long-distance retrograde neurotrophic factor signalling in neurons

Harrington, A., & Ginty, D. D. (2013) · Nature reviews. Neuroscience · doi:10.1038/nrn3253 · Cited by 269

Graded Control of Microtubule Severing by Tubulin Glutamylation

Valenstein, M. L., & Roll‐Mecak, A. (2016) · Cell · doi:10.1016/j.cell.2016.01.019 · Cited by 268

Integrated regulation of motor-driven organelle transport by scaffolding proteins

Fu, M., & Holzbaur, E. L. F. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.002 · Cited by 266

Amyotrophic lateral sclerosis-linked mutations increase the viscosity of liquid-like TDP-43 RNP granules in neurons

Gopal, P. P., Nirschl, J., Klinman, E., & Holzbaur, E. L. F. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614462114 · Cited by 266

Vasohibins encode tubulin detyrosinating activity

Nieuwenhuis, J., Adamopoulos, A., Bleijerveld, O. B., Mazouzi, A., Stickel, E., Celie, P., Altelaar, M., Knipscheer, P., Perrakis, A., Blomen, V. A., et al. (2017) · Science · doi:10.1126/science.aao5676 · Cited by 266

MFF-dependent mitochondrial fission regulates presynaptic release and axon branching by limiting axonal mitochondria size

Lewis, T. L., Kwon, S.-K., Lee, A., Shaw, R., & Polleux, F. (2018) · Nature Communications · doi:10.1038/s41467-018-07416-2 · Cited by 260

Drosophila Spastin Regulates Synaptic Microtubule Networks and Is Required for Normal Motor Function

Sherwood, N. T., Sun, Q., Xue, M., Zhang, B., & Zinn, K. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020429 · Cited by 258

The interaction between cytoplasmic dynein and dynactin is required for fast axonal transport

Waterman, C. M., Karki, S., Kuznetsov, S. A., Tabb, J. S., Weiss, D. G., Langford, G. M., & Holzbaur, E. L. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.22.12180 · Cited by 257

Organization of neuronal microtubules in the nematode Caenorhabditis elegans.

Chalfie, M., & Thomson, J. N. (1979) · The Journal of Cell Biology · doi:10.1083/jcb.82.1.278 · Cited by 257

Taxol Facilitates Axon Regeneration in the Mature CNS

Sengottuvel, V., Leibinger, M., Pfreimer, M., Andreadaki, A., & Fischer, D. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4885-10.2011 · Cited by 253

Kinesin-1–syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport

Chen, Y., & Sheng, Z.-H. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201302040 · Cited by 250

KIF1Bβ- and KIF1A-mediated axonal transport of presynaptic regulator Rab3 occurs in a GTP-dependent manner through DENN/MADD

Niwa, S., Tanaka, Y., & Hirokawa, N. (2008) · Nature Cell Biology · doi:10.1038/ncb1785 · Cited by 232

Tyrosination of α‐tubulin controls the initiation of processive dynein–dynactin motility

McKenney, R. J., Huynh, W., Vale, R. D., & Sirajuddin, M. (2016) · The EMBO Journal · doi:10.15252/embj.201593071 · Cited by 232

Microtubule Minus-End Binding Protein CAMSAP2 Controls Axon Specification and Dendrite Development

Yau, K. W., van Beuningen, S. F. B., Cunha‐Ferreira, I., Cloin, B. M. C., van Battum, E. Y., Will, L., Schätzle, P., Tas, R. P., van Krugten, J., Katrukha, E. A., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.019 · Cited by 228

BORC/kinesin-1 ensemble drives polarized transport of lysosomes into the axon

Farías, G. G., Guardia, C. M., De Pace, R., Britt, D. J., & Bonifacino, J. S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616363114 · Cited by 228

TRIM46 Controls Neuronal Polarity and Axon Specification by Driving the Formation of Parallel Microtubule Arrays

van Beuningen, S. F. B., Will, L., Harterink, M., Chazeau, A., van Battum, E. Y., Frias, C. P., Franker, M. A. M., Katrukha, E. A., Stucchi, R., Vocking, K., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.11.012 · Cited by 225

Dynein activators and adaptors at a glance

Olenick, M. A., & Holzbaur, E. L. F. (2019) · Journal of Cell Science · doi:10.1242/jcs.227132 · Cited by 218

Metabolic Turnover of Synaptic Proteins: Kinetics, Interdependencies and Implications for Synaptic Maintenance

Cohen, L. D., Zuchman, R., Sorokina, O., Müller, A., Dieterich, D. C., Armstrong, J. D., Ziv, T., & Ziv, N. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063191 · Cited by 215

Changes in microtubule number and length during axon differentiation

Yu, W., & Baas, P. (1994) · The Journal of Neuroscience · doi:10.1523/jneurosci.14-05-02818.1994 · Cited by 213

Competition between microtubule-associated proteins directs motor transport

Monroy, B. Y., Sawyer, D. L., Ackermann, B. E., Borden, M. M., Tan, T. C., & Ori-McKenney, K. M. (2018) · Nature Communications · doi:10.1038/s41467-018-03909-2 · Cited by 213

Severing enzymes amplify microtubule arrays through lattice GTP-tubulin incorporation

Vemu, A., Szczesna, E., Zehr, E. A., Spector, J. O., Grigorieff, N., Deaconescu, A. M., & Roll-Mecak, A. (2018) · Science · doi:10.1126/science.aau1504 · Cited by 210

Resolving bundled microtubules using anti-tubulin nanobodies

Mikhaylova, M., Cloin, B. M. C., Finan, K., van den Berg, R., Teeuw, J., Kijanka, M. M., Sokołowski, M., Katrukha, E. A., Maidorn, M., Opazo, F., et al. (2015) · Nature Communications · doi:10.1038/ncomms8933 · Cited by 206

Stable kinesin and dynein assemblies drive the axonal transport of mammalian prion protein vesicles

Encalada, S. E., Szpankowski, L., Xia, C.-H., & Goldstein, L. S. B. (2011) · Cell · doi:10.1016/j.cell.2011.01.021 · Cited by 206

Serial analysis of microtubules in cultured rat sensory axons

Bray, D., & Bunge, M. B. (1981) · Journal of Neurocytology · doi:10.1007/bf01262592 · Cited by 203

LC3 Binding to the Scaffolding Protein JIP1 Regulates Processive Dynein-Driven Transport of Autophagosomes

Fu, M.-M., Nirschl, J. J., & Holzbaur, E. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.04.015 · Cited by 202

Dynactin Is Required for Transport Initiation from the Distal Axon

Moughamian, A. J., & Holzbaur, E. L. F. (2012) · Neuron · doi:10.1016/j.neuron.2012.02.025 · Cited by 201

Non-centrosomal nucleation mediated by augmin organizes microtubules in post-mitotic neurons and controls axonal microtubule polarity

Sánchez-Huertas, C., Freixo, F., Viais, R., Lacasa, C., Soriano, E., & Lüders, J. (2016) · Nature Communications · doi:10.1038/ncomms12187 · Cited by 195

Cytoskeleton dynamics in axon regeneration

Blanquie, O., & Bradke, F. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.02.024 · Cited by 189

Evidence That Myosin Activity Opposes Microtubule-Based Axonal Transport of Mitochondria

Pathak, D., Sepp, K. J., & Hollenbeck, P. J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1621-10.2010 · Cited by 188

α-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate the Initiation of Dynein-Driven Transport in Neurons

Nirschl, J., Magiera, M. M., Lazarus, J. E., Janke, C., & Holzbaur, E. L. F. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.046 · Cited by 187

Mutations in BICD2 Cause Dominant Congenital Spinal Muscular Atrophy and Hereditary Spastic Paraplegia

Oates, E. C., Rossor, A. M., Hafezparast, M., Gonzalez, M., Speziani, F., MacArthur, D. G., Lek, M., Cottenie, E., Scoto, M., Foley, A. R., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.04.018 · Cited by 186

Self-repair promotes microtubule rescue

Aumeier, C., Schaedel, L., Gaillard, J., John, K., Blanchoin, L., & Théry, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3406 · Cited by 181

Autoinhibition and cooperative activation mechanisms of cytoplasmic dynein

Torisawa, T., Ichikawa, M., Furuta, A., Saito, K., Oiwa, K., Kojima, H., Toyoshima, Y. Y., & Furuta, K. (2014) · Nature Cell Biology · doi:10.1038/ncb3048 · Cited by 177

Mutations in BICD2, which Encodes a Golgin and Important Motor Adaptor, Cause Congenital Autosomal-Dominant Spinal Muscular Atrophy

Neveling, K., Martinez-Carrera, L. A., Hölker, I., Heister, A. J. G. M., Verrips, A., Hosseinibarkooie, S., Gilissen, C., Vermeer, S., Pennings, M., Meijer, R. P. P., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.04.011 · Cited by 175

The nano-architecture of the axonal cytoskeleton

Leterrier, C., Dubey, P., & Roy, S. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.129 · Cited by 175

A microtubule bestiary: structural diversity in tubulin polymers

Chaaban, S., & Brouhard, G. J. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-05-0271 · Cited by 174

A dynamic formin-dependent deep F-actin network in axons

Ganguly, A., Tang, Y., Wang, L., Ladt, K. C., Loi, J., Dargent, B., Leterrier, C., & Roy, S. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201506110 · Cited by 173

End-binding proteins EB3 and EB1 link microtubules to ankyrin G in the axon initial segment

Leterrier, C., Vacher, H., Fache, M., d'Ortoli, S. A., Castets, F., Autillo‐Touati, A., & Dargent, B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018671108 · Cited by 171

Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin

Hendershott, M. C., & Vale, R. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404133111 · Cited by 170

Autophagy in the presynaptic compartment in health and disease

Vijayan, V., & Verstreken, P. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611113 · Cited by 170

Complete morphologies of basal forebrain cholinergic neurons in the mouse

Wu, H., Williams, J., & Nathans, J. (2014) · eLife · doi:10.7554/elife.02444 · Cited by 167

Progressive Decrease of Mitochondrial Motility during Maturation of Cortical Axons In Vitro and In Vivo

Lewis, T. L., Turi, G. F., Kwon, S., Losonczy, A., & Polleux, F. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.064 · Cited by 167

MAP7 family proteins regulate kinesin-1 recruitment and activation

Hooikaas, P. J., Martin, M., Mühlethaler, T., Kuijntjes, G.-J., Peeters, C. A. E., Katrukha, E. A., Ferrari, L., Stucchi, R., Verhagen, D. G. F., van Riel, W. E., et al. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201808065 · Cited by 166

Neuropeptide Delivery to Synapses by Long-Range Vesicle Circulation and Sporadic Capture

Wong, M. Y., Zhou, C., Shakiryanova, D. M., Lloyd, T. E., Deitcher, D. L., & Levitan, E. S. (2012) · Cell · doi:10.1016/j.cell.2011.12.036 · Cited by 164

De Novo Mutations in the Motor Domain of KIF1A Cause Cognitive Impairment, Spastic Paraparesis, Axonal Neuropathy, and Cerebellar Atrophy

Lee, J.-R., Srour, M., Kim, D., Hamdan, F. F., Lim, S.-H., Brunel‐Guitton, C., Décarie, J., Rossignol, E., Mitchell, G. A., Schreiber, A., et al. (2014) · Human Mutation · doi:10.1002/humu.22709 · Cited by 160

Separating the effects of nucleotide and EB binding on microtubule structure

Zhang, R., LaFrance, B., & Nogales, E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1802637115 · Cited by 160

Septin-Driven Coordination of Actin and Microtubule Remodeling Regulates the Collateral Branching of Axons

Hu, J., Bai, X., Bowen, J. R., Dolat, L., Korobova, F. V., Yu, W., Baas, P. W., Svitkina, T., Gallo, G., & Spiliotis, E. T. (2012) · Current Biology · doi:10.1016/j.cub.2012.04.019 · Cited by 157

Preferential binding of a kinesin-1 motor to GTP-tubulin–rich microtubules underlies polarized vesicle transport

Nakata, T., Niwa, S., Okada, Y., Perez, F., & Hirokawa, N. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201104034 · Cited by 156

Excessive tubulin polyglutamylation causes neurodegeneration and perturbs neuronal transport

Magiera, M. M., Bodakuntla, S., Žiak, J., Lacomme, S., Sousa, P. M., Leboucher, S., Hausrat, T. J., Bosc, C., Andrieux, A., Kneussel, M., et al. (2018) · The EMBO Journal · doi:10.15252/embj.2018100440 · Cited by 155

Microtubule Organization Determines Axonal Transport Dynamics

Yogev, S., Cooper, R. C., Fetter, R. D., Horowitz, M., & Shen, K. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.036 · Cited by 154

KIF1A is the primary anterograde motor protein required for the axonal transport of dense-core vesicles in cultured hippocampal neurons

Lo, K. Y., Kuzmin, A., Unger, S. M., Petersen, J. D., & Silverman, M. A. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.01.018 · Cited by 153

Kinesin-3 responds to local microtubule dynamics to target synaptic cargo delivery to the presynapse

Guedes-Dias, P., Nirschl, J. J., Abreu, N., Tokito, M. K., Janke, C., Magiera, M. M., & Holzbaur, E. L. F. (2019) · Current Biology · doi:10.1016/j.cub.2018.11.065 · Cited by 153

Syntabulin–Kinesin-1 Family Member 5B-Mediated Axonal Transport Contributes to Activity-Dependent Presynaptic Assembly

Cai, Q., Pan, P., & Sheng, Z. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0731-07.2007 · Cited by 152

An assay to image neuronal microtubule dynamics in mice

Kleele, T., Marinković, P., Williams, P. R., Stern, S., Weigand, E. E., Engerer, P., Naumann, R., Hartmann, J., Karl, R. M., Bradke, F., et al. (2014) · Nature Communications · doi:10.1038/ncomms5827 · Cited by 147

The Balance between Capture and Dissociation of Presynaptic Proteins Controls the Spatial Distribution of Synapses

Wu, Y., Huo, L., Maeder, C. I., Feng, W., & Shen, K. (2013) · Neuron · doi:10.1016/j.neuron.2013.04.035 · Cited by 144

Mice Lacking α-Tubulin Acetyltransferase 1 Are Viable but Display α-Tubulin Acetylation Deficiency and Dentate Gyrus Distortion

Kim, G.-W., Li, L., Gorbani, M., You, L., & Yang, X.-J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.464792 · Cited by 141

Impaired JIP3-dependent axonal lysosome transport promotes amyloid plaque pathology

Gowrishankar, S., Wu, Y., & Ferguson, S. M. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612148 · Cited by 138

Degradation of dendritic cargos requires Rab7-dependent transport to somatic lysosomes

Yap, C. C., Digilio, L. C., McMahon, L. P., Garcia, A. D. R., & Winckler, B. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201711039 · Cited by 138

Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility

Grotjahn, D. A., Chowdhury, S., Xu, Y., McKenney, R. J., Schroer, T. A., & Lander, G. C. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0027-7 · Cited by 136

Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin

Szyk, A., Deaconescu, A. M., Piszczek, G., & Roll‐Mecak, A. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2148 · Cited by 135

Miro1‐dependent mitochondrial positioning drives the rescaling of presynaptic Ca2+ signals during homeostatic plasticity

Vaccaro, V., Devine, M. J., Higgs, N., & Kittler, J. T. (2016) · EMBO Reports · doi:10.15252/embr.201642710 · Cited by 133

The Microtubule-Associated Protein Tau Mediates the Organization of Microtubules and Their Dynamic Exploration of Actin-Rich Lamellipodia and Filopodia of Cortical Growth Cones

Biswas, S., & Kalil, K. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2281-17.2017 · Cited by 133

Tubulin genes and malformations of cortical development

Romaniello, R., Arrigoni, F., Fry, A. E., Bassi, M. T., Rees, M. I., Borgatti, R., Pilz, D. T., & Cushion, T. D. (2018) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2018.07.012 · Cited by 133

Molecular Defects in the Motor Adaptor BICD2 Cause Proximal Spinal Muscular Atrophy with Autosomal-Dominant Inheritance

Peeters, K., Litvinenko, I., Asselbergh, B., Almeida-Souza, L., Chamova, T., Geuens, T., Ydens, E., Zimoń, M., Irobi, J., Vriendt, E. D., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.04.013 · Cited by 132

Dynein Regulator NDEL1 Controls Polarized Cargo Transport at the Axon Initial Segment

Kuijpers, M., van de Willige, D., Freal, A., Chazeau, A., Franker, M. A. M., Hofenk, J., Rodrigues, R. J. C., Kapitein, L. C., Akhmanova, A. S., Jaarsma, D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.022 · Cited by 129

Loss of tubulin deglutamylase CCP1 causes infantile‐onset neurodegeneration

Shashi, V., Magiera, M. M., Klein, D., Zaki, M. S., Schoch, K., Rudnik‐Schöneborn, S., Norman, A. M., Neto, O. L. A., Dusl, M., Yuan, X., et al. (2018) · The EMBO Journal · doi:10.15252/embj.2018100540 · Cited by 129

Autoinhibition of a Neuronal Kinesin UNC-104/KIF1A Regulates the Size and Density of Synapses

Niwa, S., Lipton, D. M., Morikawa, M., Zhao, C. L., Hirokawa, N., Lu, H., & Shen, K. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.043 · Cited by 128

Regulation of Axonal Transport by Protein Kinases

Gibbs, K. L., Greensmith, L., & Schiavo, G. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.08.003 · Cited by 126

Dynamic Palmitoylation Targets MAP6 to the Axon to Promote Microtubule Stabilization during Neuronal Polarization

Tortosa, E., Adolfs, Y., Fukata, M., Pasterkamp, R. J., Kapitein, L. C., & Hoogenraad, C. C. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.042 · Cited by 125

Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport

Shima, T., Morikawa, M., Kaneshiro, J., Kambara, T., Kamimura, S., Yagi, T., Iwamoto, H., Uemura, S., Shigematsu, H., Shirouzu, M., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711178 · Cited by 125

Myosin II Activity Facilitates Microtubule Bundling in the Neuronal Growth Cone Neck

Burnette, D. T., Ji, L., Schaefer, A. W., Medeiros, N. A., Danuser, G. M., & Forscher, P. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.05.016 · Cited by 123

The Dynamic Localization of Cytoplasmic Dynein in Neurons Is Driven by Kinesin-1

Twelvetrees, A. E., Pernigo, S., Sanger, A., Guedes-Dias, P., Schiavo, G., Steiner, R. A., Dodding, M. P., & Holzbaur, E. L. F. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.046 · Cited by 122

Newly produced synaptic vesicle proteins are preferentially used in synaptic transmission

Truckenbrodt, S., Viplav, A., Jähne, S., Vogts, A., Denker, A., Wildhagen, H., Fornasiero, E. F., & Rizzoli, S. O. (2018) · The EMBO Journal · doi:10.15252/embj.201798044 · Cited by 122

Mitochondrial dynamics and quality control in Huntington's disease

Guedes-Dias, P., Pinho, B. R., Soares, T. R., de Proença, J., Duchen, M. R., & Oliveira, J. M. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.09.008 · Cited by 119

De novo mutations in KIF1A cause progressive encephalopathy and brain atrophy

Nieh, S. E., Madou, M. R. Z., Sirajuddin, M., Fregeau, B., McKnight, D., Lexa, K. W., Strober, J. B., Spaeth, C. G., Hallinan, B. E., Smaoui, N., et al. (2015) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.198 · Cited by 119

Mechanistic Logic Underlying the Axonal Transport of Cytosolic Proteins

Scott, D. A., Das, U., Tang, Y., & Roy, S. (2011) · Neuron · doi:10.1016/j.neuron.2011.03.022 · Cited by 119

Deacetylation of Miro1 by HDAC6 blocks mitochondrial transport and mediates axon growth inhibition

Kalinski, A. L., Kar, A. N., Craver, J., Tosolini, A. P., Sleigh, J. N., Lee, S. J., Hawthorne, A. L., Brito‐Vargas, P., Miller-Randolph, S., Passino, R., et al. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201702187 · Cited by 119

Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams

Chaudhary, A. R., Berger, F., Berger, C. L., & Hendricks, A. G. (2018) · Traffic · doi:10.1111/tra.12537 · Cited by 118

Structural basis for kinesin-1:cargo recognition

Pernigo, S., Lamprecht, A., Steiner, R. A., & Dodding, M. P. (2013) · Science · doi:10.1126/science.1234264 · Cited by 117

Spastin is a dual-function enzyme that severs microtubules and promotes their regrowth to increase the number and mass of microtubules

Kuo, Y., Trottier, O., Mahamdeh, M., & Howard, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818824116 · Cited by 113

Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins

Atherton, J., Farabella, I., Yu, I.-M., Rosenfeld, S. S., Houdusse, A., Topf, M., & Moores, C. A. (2014) · eLife · doi:10.2210/pdb4uxr/pdb · Cited by 110

Kinesin-Binding Protein Controls Microtubule Dynamics and Cargo Trafficking by Regulating Kinesin Motor Activity

Kevenaar, J. T., Bianchi, S., van Spronsen, M., Olieric, N., Lipka, J., Frias, C. P., Mikhaylova, M., Harterink, M., Keijzer, N., Wulf, P. S., et al. (2016) · Current Biology · doi:10.1016/j.cub.2016.01.048 · Cited by 110

Tubulins and brain development – The origins of functional specification

Breuss, M. W., Leca, I., Gstrein, T., Hansen, A. H., & Keays, D. A. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.03.002 · Cited by 107

Kinesin expands and stabilizes the GDP-microtubule lattice

Peet, D. R., Burroughs, N. J., & Cross, R. A. (2018) · Nature Nanotechnology · doi:10.1038/s41565-018-0084-4 · Cited by 106

Branch-Specific Microtubule Destabilization Mediates Axon Branch Loss during Neuromuscular Synapse Elimination

Brill, M. S., Kleele, T., Ruschkies, L., Wang, M., Marahori, N. A., Reuter, M. S., Hausrat, T. J., Weigand, E. E., Fisher, M., Ahles, A., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.049 · Cited by 105

The impact of cytoskeletal organization on the local regulation of neuronal transport

Nirschl, J., Ghiretti, A. E., & Holzbaur, E. L. F. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.100 · Cited by 102

Microtubule plus-end tracking proteins in neuronal development

van de Willige, D., Hoogenraad, C. C., & Akhmanova, A. S. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2168-3 · Cited by 100

Defective Axonal Transport of Rab7 GTPase Results in Dysregulated Trophic Signaling

Zhang, K., Kenan, R. F. B., Osakada, Y., Xu, W. L., Sinit, R. S., Chen, L., Zhao, X., Chen, J.-Y., Cui, B., & Wu, C. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.4322-12.2013 · Cited by 99

Dynactin regulates bidirectional transport of dense-core vesicles in the axon and dendrites of cultured hippocampal neurons

Kwinter, D. M., Lo, K. Y., Mafi, P., & Silverman, M. A. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.05.038 · Cited by 98

Feedback-Driven Mechanisms between Microtubules and the Endoplasmic Reticulum Instruct Neuronal Polarity

Farı́as, G. G., Freal, A., Tortosa, E., Stucchi, R., Pan, X., Portegies, S., Will, L., Altelaar, M. A. F., & Hoogenraad, C. C. (2019) · Neuron · doi:10.1016/j.neuron.2019.01.030 · Cited by 96

The structured core of human β tubulin confers isotype-specific polymerization properties

Pamula, M. C., Ti, S.-C., & Kapoor, T. M. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201603050 · Cited by 95

Seeing the Unseen

Roy, S. (2013) · The Neuroscientist · doi:10.1177/1073858413498306 · Cited by 88

Mitochondrial Dynamics in Visual Cortex Are Limited In Vivo and Not Affected by Axonal Structural Plasticity

Smit‐Rigter, L. A., Rajendran, R., Silva, C. A., Spierenburg, L., Groeneweg, F. L., Ruimschotel, E., van Versendaal, D., van der Togt, C., Eysel, U. T., Heimel, J. A., et al. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.033 · Cited by 88

Dynein activator Hook1 is required for trafficking of BDNF-signaling endosomes in neurons

Olenick, M. A., Domínguez, R., & Holzbaur, E. L. F. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201805016 · Cited by 87

THE CYTOSKELETON IN MYELINATED AXONS: SERIAL SECTION STUDY

Tsukita, S., & Ishikawa, H. (1981) · Biomedical Research · doi:10.2220/biomedres.2.424 · Cited by 86

Polyglutamylation of tubulin's C-terminal tail controls pausing and motility of kinesin-3 family member KIF1A

Lessard, D. V., Zinder, O. J., Hotta, T., Verhey, K. J., Ohi, R., & Berger, C. L. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005765 · Cited by 85

Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles

Prezel, E., Elie, A., Delaroche, J., Stoppin-Mellet, V., Bosc, C., Serre, L., Fourest-Lieuvin, A., Andrieux, A., Vantard, M., & Arnal, I. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0429 · Cited by 83

Lysosomal dysfunction disrupts presynaptic maintenance and restoration of presynaptic function prevents neurodegeneration in lysosomal storage diseases

Sambri, I., D’Alessio, R., Ezhova, Y., Giuliano, T., Sorrentino, N. C., Cacace, V., Risi, M. D., Cataldi, M., Annunziato, L., Leonibus, E. D., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606965 · Cited by 81

CAMSAP3 maintains neuronal polarity through regulation of microtubule stability

Pongrakhananon, V., Saito, H., Hiver, S., Abe, T., Shioi, G., Meng, W., & Takeichi, M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803875115 · Cited by 80

The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors

Soppina, V., & Verhey, K. J. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-01-0696 · Cited by 79

MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules

Chaudhary, A. R., Lu, H., Krementsova, E. B., Bookwalter, C. S., Trybus, K. M., & Hendricks, A. G. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008052 · Cited by 79

Motor reattachment kinetics play a dominant role in multimotor-driven cargo transport

Feng, Q., Mickolajczyk, K. J., Chen, G.-Y., & Hancock, W. O. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.016 · Cited by 76

α-Tubulin Acetylation Restricts Axon Overbranching by Dampening Microtubule Plus-End Dynamics in Neurons

Wei, D., Gao, N., Li, L., Zhu, J.-X., Diao, L., Huang, J., Han, Q., Wang, S., Xue, H., Wang, Q., et al. (2017) · Cerebral Cortex · doi:10.1093/cercor/bhx225 · Cited by 76

TRIM46 Organizes Microtubule Fasciculation in the Axon Initial Segment

Harterink, M., Vocking, K., Pan, X., Soriano, E., Slenders, L., Freal, A., Tas, R. P., van de Wetering, W. J., Timmer, K., Motshagen, J., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.3105-18.2019 · Cited by 75

Direct induction of microtubule branching by microtubule nucleation factor SSNA1

Basnet, N., Nedozrálová, H., Crevenna, Á. H., Bodakuntla, S., Schlichthaerle, T., Taschner, M. J., Giovanni Cardone, A., Janke, C., Jungmann, R., Magiera, M. M., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0199-8 · Cited by 70

Rab7 and the CMT2B disease

Cogli, L., Piro, F., & Bucci, C. (2009) · Biochemical Society Transactions · doi:10.1042/bst0371027 · Cited by 65

Tau mediates microtubule bundle architectures mimicking fascicles of microtubules found in the axon initial segment

Chung, P. J., Song, C., Deek, J., Miller, H. P., Li, Y., Choi, M. C., Wilson, L., Feinstein, S. C., & Safinya, C. R. (2016) · Nature Communications · doi:10.1038/ncomms12278 · Cited by 65

Multivesicular bodies mediate long-range retrograde NGF-TrkA signaling

Ye, M., Lehigh, K. M., & Ginty, D. D. (2018) · eLife · doi:10.7554/elife.33012 · Cited by 65

Islands Containing Slowly Hydrolyzable GTP Analogs Promote Microtubule Rescues

Tropini, C., Roth, E. A., Žanić, M., Gardner, M. K., & Howard, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030103 · Cited by 63

The tubulin code in neuronal polarity

Park, J. H., & Roll‐Mecak, A. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.03.001 · Cited by 61

A novel mutation in the β‐tubulin gene TUBB2B associated with complex malformation of cortical development and deficits in axonal guidance

Romaniello, R., Tonelli, A., Arrigoni, F., Baschirotto, C., Triulzi, F. M., Bresolin, N., Bassi, M. T., & Borgatti, R. (2012) · Developmental Medicine & Child Neurology · doi:10.1111/j.1469-8749.2012.04316.x · Cited by 58

TUBA1A mutations identified in lissencephaly patients dominantly disrupt neuronal migration and impair dynein activity

Aiken, J., Moore, J. K., & Bates, E. A. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy416 · Cited by 57

Intracellular Ca 2+ Release and Synaptic Plasticity: A Tale of Many Stores

Padamsey, Z., Foster, W. J., & Emptage, N. J. (2018) · The Neuroscientist · doi:10.1177/1073858418785334 · Cited by 56

MTCL1 plays an essential role in maintaining Purkinje neuron axon initial segment

Satake, T., Yamashita, K., Hayashi, K., Miyatake, S., Tamura‐Nakano, M., Doi, H., Furuta, Y., Shioi, G., Miura, E., Takeo, Y. H., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201695630 · Cited by 55

MAP7D2 Localizes to the Proximal Axon and Locally Promotes Kinesin-1-Mediated Cargo Transport into the Axon

Pan, X., Cao, Y., Stucchi, R., Hooikaas, P. J., Portegies, S., Will, L., Martin, M., Akhmanova, A. S., Harterink, M., & Hoogenraad, C. C. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.084 · Cited by 55

The many disguises of the signalling endosome

Villarroel‐Campos, D., Schiavo, G., & Lazo, O. M. (2018) · FEBS Letters · doi:10.1002/1873-3468.13235 · Cited by 53

Two kinesins drive anterograde neuropeptide transport

Lim, A. P. C., Rechtsteiner, A., & Saxton, W. M. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-12-0820 · Cited by 49

CDK5‐dependent activation of dynein in the axon initial segment regulates polarized cargo transport in neurons

Klinman, E., Tokito, M. K., & Holzbaur, E. L. F. (2017) · Traffic · doi:10.1111/tra.12529 · Cited by 47

Drebrin coordinates the actin and microtubule cytoskeleton during the initiation of axon collateral branches

Ketschek, A., Spillane, M., Dun, X., Hardy, H., Chilton, J. K., & Gallo, G. (2016) · Developmental Neurobiology · doi:10.1002/dneu.22377 · Cited by 46

Expression of kinesin superfamily genes in cultured hippocampal neurons

Silverman, M. A., Kaech, S., Ramser, E. M., Lu, X., Lasarev, M. R., Nagalla, S. R., & Banker, G. A. (2010) · Cytoskeleton · doi:10.1002/cm.20487 · Cited by 38

Microtubules of frog olfactory axons: their length and number/axon

Burton, P. R. (1987) · Brain Research · doi:10.1016/0006-8993(87)90742-6 · Cited by 35

Quantifying Protein Copy Number in Super Resolution Using an Imaging-Invariant Calibration

Zanacchi, F. C., Manzo, C., Magrassi, R., Derr, N. D., & Lakadamyali, M. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.04.026 · Cited by 34

Understanding mRNA trafficking: Are we there yet?

Czaplinski, K. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.04.025 · Cited by 31

Goldberg–Shprintzen megacolon syndrome with associated sensory motor axonal neuropathy

Dafsari, H. S., Byrne, S., Lin, J., Pitt, M. C., Jongbloed, J. D. H., Flinter, F. A., & Jungbluth, H. (2015) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.36873 · Cited by 29

Activity Induces Fmr1-Sensitive Synaptic Capture of Anterograde Circulating Neuropeptide Vesicles

Cavolo, S. L., Bulgari, D., Deitcher, D. L., & Levitan, E. S. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2212-16.2016 · Cited by 29

Non-invasive force measurement reveals the number of active kinesins on a synaptic vesicle precursor in axonal transport regulated by ARL-8

Hayashi, K., Hasegawa, S., Sagawa, T., Tasaki, S., & Niwa, S. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp05890j · Cited by 28

An Essential Postdevelopmental Role for Lis1 in Mice

Hines, T. J., Gao, X., Sahu, S., Lange, M. M., Turner, J. R., Twiss, J. L., & Smith, D. S. (2018) · eNeuro · doi:10.1523/eneuro.0350-17.2018 · Cited by 16

Occurrence of fasciculated microtubules at nodes of Ranvier in rat spinal roots

Nakazawa, E., & Ishikawa, H. (1995) · Journal of Neurocytology · doi:10.1007/bf01189066 · Cited by 12

Differential effect of multiple kinesin motors on run length, force and microtubule binding rate

Gutiérrez–Medina, B., Buendía-Padilla, M., Gutiérrez-Esparza, A. J., & Camacho, A. R. O. (2018) · Biophysical Chemistry · doi:10.1016/j.bpc.2018.08.007 · Cited by 10

Native kinesin‐1 does not bind preferentially to GTP‐tubulin‐rich microtubules in vitro

Li, Q., King, S. J., & Xu, J. (2017) · Cytoskeleton · doi:10.1002/cm.21386 · Cited by 8

Cytoplasmic dynein dysfunction and neurodegenerative disease

Moughamian, A. J., & Holzbaur, E. L. F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809470-9.00013-8 · Cited by 7

The tubulin code and its role in controlling microtubule properties and functions

Janke, C., & Magiera, M. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0214-3 · Cited by 956

Mechanisms of microtubule organization in differentiated animal cells

Akhmanova, A., & Kapitein, L. C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00473-y · Cited by 233

Mechanism of STMN2 cryptic splice-polyadenylation and its correction for TDP-43 proteinopathies

Baughn, M. W., Melamed, Z., López‐Erauskin, J., Beccari, M. S., Ling, K., Zuberi, A. R., Presa, M. F., Gonzalo-Gil, E., Maimon, R., Vazquez‐Sanchez, S., et al. (2023) · Science · doi:10.1126/science.abq5622 · Cited by 252

Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction

Deniston, C. K., Salogiannis, J., Mathea, S., Snead, D., Lahiri, I., Matyszewski, M., Donosa, O., Watanabe, R., Böhning, J., Shiau, A. K., et al. (2020) · Nature · doi:10.1038/s41586-020-2673-2 · Cited by 253

Oligodendrocytes support axonal transport and maintenance via exosome secretion

Frühbeis, C., Kuo, W. P., Müller, C., Barth, K., Peris, L., Tenzer, S., Möbius, W., Werner, H. B., Nave, K., Fröhlich, D., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000621 · Cited by 201

Axonal transport and the delivery of pre-synaptic components

Goldstein, A. Y. N., Wang, X., & Schwarz, T. L. (2008) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2008.10.003 · Cited by 155

Nanocarriers and Intracellular Transport: Moving Along the Cytoskeletal Matrix

Woolf, N. J., Priel, A., & Tuszyński, J. A. (2009) · Biological and medical physics series · doi:10.1007/978-3-642-03584-5_4 · Cited by 1

Axon and dendritic trafficking

Maeder, C. I., Shen, K., & Hoogenraad, C. C. (2014) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2014.03.015 · Cited by 116

Presynaptic Precursor Vesicles—Cargo, Biogenesis, and Kinesin-Based Transport across Species

Petzoldt, A. G. (2023) · Cells · doi:10.3390/cells12182248 · Cited by 18

Neurexin and Frizzled intercept axonal-transport at microtubule minus-ends to control synapse formationPreprint

Balseiro-Gómez, S., Park, J., Yue, Y., Ding, C., Shao, L., Ҫetinkaya, S., Kuzoian, C., Hammarlund, M., Verhey, K. J., & Yogev, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.22.436477