Oligomeric Complexes Link Rab5 Effectors with NSF and Drive Membrane Fusion via Interactions between EEA1 and Syntaxin 13

SNAREpins: Minimal Machinery for Membrane Fusion

Weber, T., Zemelman, B. V., McNew, J. A., Westermann, B., Gmachl, M., Parlati, F., Söllner, T. H., & Rothman, J. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81404-x · Cited by 2,481

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution

Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417

Mechanisms of intracellular protein transport

Rothman, J. E. (1994) · Nature · doi:10.1038/372055a0 · Cited by 2,267

EEA1 links PI(3)K function to Rab5 regulation of endosome fusion

Simonsen, A., Lippe, R., Christoforidis, S., Gaullier, J.-M., Brech, A., Callaghan, J., Toh, B.-H., Murphy, C., Zerial, M., & Stenmark, H. (1998) · Nature · doi:10.1038/28879 · Cited by 1,133

The Rab5 effector EEA1 is a core component of endosome docking

Christoforidis, S., McBride, H. M., Burgoyne, R. D., & Zerial, M. (1999) · Nature · doi:10.1038/17618 · Cited by 854

Structure and Conformational Changes in NSF and Its Membrane Receptor Complexes Visualized by Quick-Freeze/Deep-Etch Electron Microscopy

Hanson, P. I., Roth, R. A., Morisaki, H., Jahn, R., & Heuser, J. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80512-7 · Cited by 797

The diversity of Rab proteins in vesicle transport

Novick, P., & Zerial, M. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80025-7 · Cited by 757

EEA1, an Early Endosome-Associated Protein.

Mu, F., Callaghan, J. M., Steele‐Mortimer, O., Stenmark, H., Parton, R. G., Campbell, P. L., McCluskey, J., Yeo, J.-P., Tock, E. P. C., & Toh, B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13503 · Cited by 713

The syntaxin family of vesicular transport receptors

Bennett, M. K., Garcia-Arrarás, J., Elferink, L. A., Peterson, K., Fleming, A. M., Hazuka, C. D., & Scheller, R. H. (1993) · Cell · doi:10.1016/0092-8674(93)90466-4 · Cited by 649

The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis

Guo, W., Roth, D., Walch-Solimena, C., & Novick, P. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.1071 · Cited by 627

The immunological aspects of latency in tuberculosis

Chan, J., & Flynn, J. L. (2003) · Clinical Immunology · doi:10.1016/s1521-6616(03)00210-9 · Cited by 176

Structural Mechanism of Endosome Docking by the FYVE Domain

Kutateladze, T. G., & Overduin, M. (2001) · Science · doi:10.1126/science.291.5509.1793 · Cited by 175

Selective Membrane Recruitment of EEA1 Suggests a Role in Directional Transport of Clathrin-coated Vesicles to Early Endosomes

Rubino, M., Miączyńska, M., Lippé, R., & Zerial, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.3745 · Cited by 174

ENDOCYTOTIC CYCLING OF PM PROTEINS

Murphy, A. S., Bandyopadhyay, A., Holstein, S. E. H., & Peer, W. A. (2005) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.56.032604.144150 · Cited by 176

Mechanisms of TfR-mediated transcytosis and sorting in epithelial cells and applications toward drug delivery

Widera, A., Norouziyan, F., & Shen, W. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.07.004 · Cited by 173

Mosaic Organization of the Endocytic Pathway

Miączyńska, M., & Zerial, M. (2002) · Experimental Cell Research · doi:10.1006/excr.2001.5401 · Cited by 173

A syntaxin 10–SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells

Ganley, I. G., Espinosa, E. J., & Pfeffer, S. R. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707136 · Cited by 171

The Role of the Tethering Proteins p115 and GM130 in Transport through the Golgi Apparatus In Vivo

Seemann, J., Jokitalo, E., & Warren, G. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.635 · Cited by 171

synaptotagminMutants Reveal Essential Functions for the C2B Domain in Ca2+-Triggered Fusion and Recycling of Synaptic VesiclesIn Vivo

Littleton, J. T., Bai, J., Vyas, B., Desai, R., Baltus, A. E., Garment, M. B., Carlson, S. D., Ganetzky, B., & Chapman, E. R. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-05-01421.2001 · Cited by 171

Caenorhabditis elegans RME-6 is a novel regulator of RAB-5 at the clathrin-coated pit

Sato, M., Sato, K., Fonarev, P., Huang, C.-J., Liou, W., & Grant, B. D. (2005) · Nature Cell Biology · doi:10.1038/ncb1261 · Cited by 170

Regulated exocytosis and SNARE function (Review)

Söllner, T. H. (2003) · Molecular Membrane Biology · doi:10.1080/0968768031000104953 · Cited by 169

Rab18 and Rab43 have key roles in ER-Golgi trafficking

Dejgaard, S. Y., Murshid, A., Erman, A., Mancini, Ö. K., Verbich, D., Lodge, R., Dejgaard, K., Ly-Hartig, T. B. N., Pepperkok, R., Simpson, J. C., et al. (2008) · Journal of Cell Science · doi:10.1242/jcs.021808 · Cited by 167

Syntaxin 7 Is Localized to Late Endosome Compartments, Associates with Vamp 8, and Is Required for Late Endosome–Lysosome Fusion

Mullock, B. M., Smith, C. W., Ihrke, G., Bright, N. A., Lindsay, M. R., Parkinson-Lawrence, E. J., Brooks, D. A., Parton, R. G., James, D. E., Luzio, J. P., et al. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.9.3137 · Cited by 166

The R-SNARE Endobrevin/VAMP-8 Mediates Homotypic Fusion of Early Endosomes and Late Endosomes

Antonin, W., Holroyd, C., Tikkanen, R., Höning, S., & Jahn, R. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.10.3289 · Cited by 156

The building BLOC(k)s of lysosomes and related organelles

Dell’Angelica, E. C. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.05.001 · Cited by 149

Biochemical analysis of distinct Rab5- and Rab11-positive endosomes along the transferrin pathway

Trischler, M., Stoorvogel, W., & Ullrich, O. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.24.4773 · Cited by 162

Lipid sorting and multivesicular endosome biogenesis

Bissig, C., & Gruenberg, J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016816 · Cited by 151

Cellular trafficking of lipoteichoic acid and Toll-like receptor 2 in relation to signaling; role of CD14 and CD36

Nilsen, N. J., Deininger, S., Nonstad, U., Skjeldal, F. M., Husebye, H., Rodionov, D., von Aulock, S., Härtung, T., Lien, E., Bakke, O., et al. (2008) · Journal of Leukocyte Biology · doi:10.1189/jlb.0907656 · Cited by 170

Sequential Roles for Phosphatidylinositol 3-Phosphate and Rab5 in Tethering and Fusion of Early Endosomes via Their Interaction with EEA1

Lawe, D. C., Chawla, A., Merithew, E., Dumas, J., Carrington, W., Fogarty, K., Lifshitz, L., Tuft, R., Lambright, D., & Corvera, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109239200 · Cited by 156

Homotypic fusion of early endosomes: SNAREs do not determine fusion specificity

Brandhorst, D., Zwilling, D., Rizzoli, S. O., Lippert, U., Lang, T., & Jahn, R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511138103 · Cited by 165

Ypt/Rab GTPases: Regulators of Protein Trafficking

Segev, N. (2001) · Science Signaling · doi:10.1126/stke.2001.100.re11 · Cited by 162

Vps9 domain-containing proteins: activators of Rab5 GTPases from yeast to neurons

Carney, D. S., Davies, B. A., & Horazdovsky, B. F. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.11.001 · Cited by 156

A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology

Kuronita, T., Eskelinen, E., Fujita, H., Säftig, P., Himeno, M., & Tanaka, Y. (2002) · Journal of Cell Science · doi:10.1242/jcs.00075 · Cited by 157

The Vtc proteins in vacuole fusion: coupling NSF activity to V0trans‐complex formation

Müller, O., Bayer, M. J., Peters, C., Andersen, J., Mann, M., & Mayer, A. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.259 · Cited by 148

The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking

Kauppi, M., Simonsen, A., Bremnes, B., Vieira, A. V., Callaghan, J. M., Stenmark, H., & Olkkonen, V. M. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.5.899 · Cited by 151

Priming in exocytosis: Attaining fusion-competence after vesicle docking

Klenchin, V. A., & Martin, T. F. J. (2000) · Biochimie · doi:10.1016/s0300-9084(00)00208-x · Cited by 151

Intracellular sorting and transport of proteins

van Vliet, C., Thomas, E. C., Merino‐Trigo, A., Teasdale, R. D., & Gleeson, P. A. (2003) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(03)00019-1 · Cited by 149

The syntaxins.

Teng, F. Y. H., Wang, Y., & Tang, B. L. (2001) · Genome biology · doi:10.1186/gb-2001-2-11-reviews3012 · Cited by 147

Structure of GATE-16, Membrane Transport Modulator and Mammalian Ortholog of Autophagocytosis Factor Aut7p

Paz, Y., Elazar, Z., & Fass, D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000307200 · Cited by 146

Subversion of a young phagosome: the survival strategies of intracellular pathogens. Microreview

Duclos, S., & Desjardins, M. (2000) · Cellular Microbiology · doi:10.1046/j.1462-5822.2000.00066.x · Cited by 144

Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport

Monier, S., Jollivet, F., Janoueix‐Lerosey, I., Johannes, L., & Goud, B. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.030406.x · Cited by 170

Interaction of the EEA1 FYVE Finger with Phosphatidylinositol 3-Phosphate and Early Endosomes

Gaullier, J., Rønning, E., Gillooly, D. J., & Stenmark, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m906554199 · Cited by 144

Dual Roles of the Mammalian GARP Complex in Tethering and SNARE Complex Assembly at the trans -Golgi Network

Pérez‐Victoria, F. J., & Bonifacino, J. S. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00495-09 · Cited by 143

The Phox homology (PX) domain, a new player in phosphoinositide signalling

Xu, Y., Seet, L., Hanson, B. J., & Hong, W. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3600513 · Cited by 143

SARA-Regulated Vesicular Targeting Underlies Formation of the Light-Sensing Organelle in Mammalian Rods

Chuang, J.-Z., Zhao, Y., & Sung, C.-H. (2007) · Cell · doi:10.1016/j.cell.2007.06.030 · Cited by 141

Syntaxin clusters assemble reversibly at sites of secretory granules in live cells

Barg, S., Knowles, M. K., Chen, X., Midorikawa, M., & Almers, W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014823107 · Cited by 139

Phagosome Maturation: A Few Bugs in the System

Scott, C. C., Botelho, R. J., & Grinstein, S. (2003) · The Journal of Membrane Biology · doi:10.1007/s00232-002-2008-2 · Cited by 138

Structural basis for Rab GTPase activation by VPS9 domain exchange factors

Delprato, A., & Lambright, D. G. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1232 · Cited by 138

Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing

Ungermann, C., & Langosch, D. (2005) · Journal of Cell Science · doi:10.1242/jcs.02561 · Cited by 139

Small G-protein networks:

Matozaki, T., Nakanishi, H., & Takai, Y. (2000) · Cellular Signalling · doi:10.1016/s0898-6568(00)00102-9 · Cited by 140

Biogenesis of the Sorting Endosome: The Role of Rab5

Woodman, P. G. (2000) · Traffic · doi:10.1034/j.1600-0854.2000.010902.x · Cited by 136

Cellular functions of NSF: Not just SNAPs and SNAREs

Zhao, C., Slevin, J. T., & Whiteheart, S. W. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.03.032 · Cited by 136

Phosphorylation of EEA1 by p38 MAP kinase regulates μ opioid receptor endocytosis

Macé‐Aimé, G., Miączyńska, M., Zerial, M., & Nebreda, Á. R. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600799 · Cited by 136

The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type specifically expressed and localised to the Golgi apparatus

Opdam, F. J. M., Échard, A., Croes, H. J. E., van den Hurk, J. A. J. M., van de Vorstenbosch, R. A., Ginsel, L. A., Goud, B., & Fransen, J. A. M. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.15.2725 · Cited by 135

Phosphoinositide-binding domains

Itoh, T., & Takenawa, T. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(02)00028-1 · Cited by 131

Regulation of Membrane Transport by rab GTPases

Deneka, M., Neeft, M., & van der Sluijs, P. (2003) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/713609214 · Cited by 132

Structural basis of Rab5-Rabaptin5 interaction in endocytosis

Zhu, G., Zhai, P. C., Liu, J., Terzyan, S. S., Li, G., & Zhang, X. C. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb832 · Cited by 132

Membrane identity and GTPase cascades regulated by toggle and cut‐out switches

Conte‐Zerial, P. D., Brusch, L., Rink, J. C., Collinet, C., Kalaidzidis, Y. L., Zerial, M., & Deutsch, A. (2008) · Molecular Systems Biology · doi:10.1038/msb.2008.45 · Cited by 133

A 56-kDa Selenium-binding Protein Participates in Intra-Golgi Protein Transport

Porat, A., Sagiv, Y., & Elazar, Z. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14457 · Cited by 129

Phosphatidylinositol 3-phosphate recognition and membrane docking by the FYVE domain

Kutateladze, T. G. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.03.011 · Cited by 128

PROTEIN AND LIPID REQUIREMENTS FOR ENDOCYTOSIS

D'Hondt, K., Heese-Peck, A., & Riezman, H. (2000) · Annual Review of Genetics · doi:10.1146/annurev.genet.34.1.255 · Cited by 128

Mammalian Late Vacuole Protein Sorting Orthologues Participate in Early Endosomal Fusion and Interact with the Cytoskeleton

Richardson, S. C. W., Winistorfer, S. C., Poupon, V., Luzio, J. P., & Piper, R. C. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-06-0358 · Cited by 127

Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy

Jung, C. (2000) · Journal of Molecular Recognition · doi:10.1002/1099-1352(200011/12)13:6 · Cited by 249

Homotypic Fusion of Immature Secretory Granules During Maturation Requires Syntaxin 6

Wendler, F., Page, L. J., Urbé, S., & Tooze, S. A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.6.1699 · Cited by 125

Phosphoinositides and vesicular membrane traffic

Mayinger, P. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.01.002 · Cited by 125

Endosomal Localization and Receptor Dynamics Determine Tyrosine Phosphorylation of Hepatocyte Growth Factor-Regulated Tyrosine Kinase Substrate

Urbé, S., Mills, I. G., Stenmark, H., Kitamura, N., & Clague, M. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.20.7685-7692.2000 · Cited by 124

Dynamics of SNARE Assembly and Disassembly during Sperm Acrosomal Exocytosis

Blas, G. A. D., Roggero, C. M., Tomes, C. N., & Mayorga, L. S. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030323 · Cited by 123

The SNAREs vti1a and vti1b have distinct localization and SNARE complex partners

Kreykenbohm, V., Wenzel, D., Antonin, W., Atlachkine, V., & von Mollard, G. F. (2002) · European Journal of Cell Biology · doi:10.1078/0171-9335-00247 · Cited by 122

Participation of Rab5, an Early Endosome Protein, in Hepatitis C Virus RNA Replication Machinery

Stone, M. C., Jia, S., Heo, W. D., Meyer, T., & Konan, K. V. (2007) · Journal of Virology · doi:10.1128/jvi.01366-06 · Cited by 123

Clathrin coat construction in endocytosis

Pearse, B. M. F. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00071-3 · Cited by 120

Mechanism and regulation of GLUT-4 vesicle fusion in muscle and fat cells

Foster, L. J., & Klip, A. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.279.4.c877 · Cited by 121

SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs

Lang, T., Margittai, M., Hölzler, H., & Jahn, R. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200203088 · Cited by 119

The C2b Domain of Synaptotagmin Is a Ca2+–Sensing Module Essential for Exocytosis

Desai, R. C., Vyas, B., Earles, C. A., Littleton, J., Kowalchyck, J. A., Martin, T., & Chapman, E. (2000) · Journal of Cell Biology · doi:10.1083/jcb.150.5.1125 · Cited by 126

Syntaxin 6: The Promiscuous Behaviour of a SNARE Protein

Wendler, F., & Tooze, S. A. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.20903.x · Cited by 117

Membrane Fusion in Eukaryotic Cells

Mayer, A. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.032202.114809 · Cited by 115

A FYVE-finger-containing protein, Rabip4, is a Rab4 effector involved in early endosomal traffic

Cormont, M., Mari, M. C., Galmiche, A., Hofman, P. M., & MARCHAND‐BRUSTEL, Y. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1637 · Cited by 115

A Role for the Adaptor Proteins TRAM and TRIF in Toll-like Receptor 2 Signaling

Nilsen, N. J., Vladimer, G. I., Stenvik, J., Ørning, P., Zeid-Kilani, M. V., Bugge, M., Bergstrøm, B., Conlon, J. E., Husebye, H., Hise, A. G., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.593426 · Cited by 114

Rab11-FIP2 Functions in Transferrin Recycling and Associates with Endosomal Membranes via Its COOH-terminal Domain

Lindsay, A. J., & McCaffrey, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200757200 · Cited by 114

Calcium and calmodulin in membrane fusion

Burgoyne, R. D., & Clague, M. J. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(03)00089-2 · Cited by 111

Endosomal and Phagosomal SNAREs

Dingjan, I., Linders, P. T. A., Verboogen, D. R. J., Revelo, N. H., ter Beest, M., & van den Bogaart, G. (2018) · Physiological Reviews · doi:10.1152/physrev.00037.2017 · Cited by 114

Phosphatidylinositol 3-phosphate is found in microdomains of early endosomes

Gillooly, D. J., Raiborg, C., & Stenmark, H. (2003) · Histochemistry and Cell Biology · doi:10.1007/s00418-003-0591-7 · Cited by 113

Membrane Tethering and Fusion in the Secretory and Endocytic Pathways

Waters, M. G., & Hughson, F. M. (2000) · Traffic · doi:10.1034/j.1600-0854.2000.010802.x · Cited by 113

Chaperone Suppression of Cellular Toxicity of Huntingtin Is Independent of Polyglutamine Aggregation

Zhou, H., Li, X., & Li, X. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104140200 · Cited by 112

Are Rab proteins the link between Golgi organization and membrane trafficking?

Liu, S., & Storrie, B. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1021-6 · Cited by 117

The septin Sept5/CDCrel-1 competes with α-SNAP for binding to the SNARE complex

Beites, C. L., CAMPBELL, K. A., & Trimble, W. S. (2005) · Biochemical Journal · doi:10.1042/bj20041090 · Cited by 111

Modulation of receptor cycling by neuron-enriched endosomal protein of 21 kD

Steiner, P., Sarria, J. ‐. F., Glauser, L., Magnin, S., Catsicas, S., & Hirling, H. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200202022 · Cited by 111

Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and recycling of the glutamate receptor subunit GluR2

Steiner, P., Alberi, S., Kulangara, K., Yersin, A., Sarria, J. ‐. F., Régulier, E., Kasas, S., Dietler, G., Müller, D., Catsicas, S., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600755 · Cited by 108

Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization and maturation of recycling endosomes

Hoogenraad, C. C., Popa, I., Futai, K., Sanchez-Martinez, E., Wulf, P. S., van Vlijmen, T., Dortland, B. R., Oorschot, V., Govers, R., Monti, M., et al. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000283 · Cited by 101

Relationships between EEA1 binding partners and their role in endosome fusion

Mills, I. G., Urbé, S., & Clague, M. J. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.10.1959 · Cited by 109

Identification of rabaptin‐5, rabex‐5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER

Valsdottir, R., Hashimoto, H., Ashman, K., Koda, T., Storrie, B., & Nilsson, T. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02993-3 · Cited by 107

Small GTPase Rab4 Regulates Ca2+-induced α-Granule Secretion in Platelets

Shirakawa, R., Yoshioka, A., Horiuchi, H., Nishioka, H., Tabuchi, A., & Kita, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002834200 · Cited by 107

SNARE Complex Assembly Is Required for Human Sperm Acrosome Reaction

Tomes, C. N., Michaut, M. A., Blas, G. A. D., Visconti, P. E., Matti, U., & Mayorga, L. S. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0567 · Cited by 106

Hermansky–Pudlak Syndrome: Vesicle Formation from Yeast to Man

Huizing, M., Boissy, R. E., & Gahl, W. A. (2002) · Pigment Cell Research · doi:10.1034/j.1600-0749.2002.02074.x · Cited by 106

Class III phosphatidylinositol 3–kinase and its catalytic product P tdIns3 P in regulation of endocytic membrane traffic

Raiborg, C., Schink, K. O., & Stenmark, H. (2013) · FEBS Journal · doi:10.1111/febs.12116 · Cited by 107

A Novel Binding Protein Composed of Homophilic Tetramer Exhibits Unique Properties for the Small GTPase Rab5

Saito, K., Murai, J., Kajiho, H., Kontani, K., Kurosu, H., & Katada, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106276200 · Cited by 104

A cycle of Vam7p release from and PtdIns 3-P–dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion

Boeddinghaus, C., Merz, A. J., Laage, R., & Ungermann, C. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200112098 · Cited by 104

Transcriptional profiling of native inner medullary collecting duct cells from rat kidney

Uawithya, P., Pisitkun, T., Ruttenberg, B. E., & Knepper, M. A. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00201.2007 · Cited by 101

Negative regulation of phosphatidylinositol 3-phosphate levels in early-to-late endosome conversion

Liu, K., Jian, Y., Sun, X., Yang, C., Gao, Z., Zhang, Z., Liu, X., Li, Y., Xu, J., Jing, Y., et al. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201506081 · Cited by 103

The p97 ATPase associates with EEA1 to regulate the size of early endosomes

Ramanathan, H. N., & Ye, Y. (2011) · Cell Research · doi:10.1038/cr.2011.80 · Cited by 104

Endosomal and lysosomal effects of desferrioxamine: protection of HeLa cells from hydrogen peroxide-induced DNA damage and induction of cell-cycle arrest

Doulias, P., Christoforidis, S., Brunk, U. T., & Galaris, D. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00396-4 · Cited by 96

Compartmental signal modulation: Endosomal phosphatidylinositol 3-phosphate controls endosome morphology and selective cargo sorting

Fili, N., Calleja, V., Woscholski, R., Parker, P. J., & Larijani, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607040103 · Cited by 96

Rab protein evolution and the history of the eukaryotic endomembrane system

Brighouse, A., Dacks, J. B., & Field, M. C. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0436-1 · Cited by 102

Sequential action of two GTPases to promote vacuole docking and fusion

Eitzen, G., Will, E., Gallwitz, D., Haas, A., & Wickner, W. T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.24.6713 · Cited by 95

The trypanosome transcriptome is remodelled during differentiation but displays limited responsiveness within life stages

Koumandou, V. L., Natesan, S. K. A., Sergeenko, T., & Field, M. C. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-298 · Cited by 96

Multiple aspects of Rab protein action in the secretory pathway: Focus on Rab3 and Rab6

Darchen, F. (2000) · Biochimie · doi:10.1016/s0300-9084(00)00219-4 · Cited by 95

Regulation of Early Endosomal Entry by theDrosophilaTumor Suppressors Rabenosyn and Vps45

Morrison, H. A., Dionne, H., Rusten, T. E., Brech, A., Fisher, W. W., Pfeiffer, B. D., Celniker, S., Stenmark, H., & Bilder, D. H. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0716 · Cited by 98

Calcium-triggered acrosomal exocytosis in human spermatozoa requires the coordinated activation of Rab3A and N -ethylmaleimide-sensitive factor

Michaut, M. A., Tomes, C. N., Blas, G. A. D., Yunes, R., & Mayorga, L. S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.180206197 · Cited by 94

Granuphilin Modulates the Exocytosis of Secretory Granules through Interaction with Syntaxin 1a

Torii, S., Zhao, S., Yi, Z., Takeuchi, T., & Izumi, T. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5518-5526.2002 · Cited by 94

Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex

Sun, W., Yan, Q., Vida, T. A., & Bean, A. J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302083 · Cited by 94

Proteins Needed for Vesicle Budding from the Golgi Complex Are Also Required for the Docking Step of Homotypic Vacuole Fusion

Price, A., Wickner, W. T., & Ungermann, C. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.6.1223 · Cited by 93

The Rab5 Effector EEA1 Interacts Directly with Syntaxin-6

Simonsen, A., Gaullier, J., D’Arrigo, A., & Stenmark, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28857 · Cited by 248

Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes

Ohya, T., Miączyńska, M., Coskun, Ü., Lommer, B. S., Runge, A., Drechsel, D. N., Kalaidzidis, Y. L., & Zerial, M. (2009) · Nature · doi:10.1038/nature08107 · Cited by 235

The Rab5 effector EEA1 is a core component of endosome docking

Christoforidis, S., McBride, H. M., Burgoyne, R. D., & Zerial, M. (1999) · Nature · doi:10.1038/17618 · Cited by 854

In brief

(2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2722

An endosomal tether undergoes an entropic collapse to bring vesicles together

Murray, D. H., Jahnel, M., Lauer, J. L., Avellaneda, M. J., Brouilly, N., Cezanne, A., Morales-Navarrete, H. A., Perini, E. D., Ferguson, C., Lupas, A. N., et al. (2016) · Nature · doi:10.1038/nature19326 · Cited by 161