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

Rab GTPases as coordinators of vesicle traffic

Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413

Rab proteins as membrane organizers

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Role of Rab GTPases in Membrane Traffic and Cell Physiology

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Rabs and their effectors: achieving specificity in membrane traffic

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Distinct Membrane Domains on Endosomes in the Recycling Pathway Visualized by Multicolor Imaging of Rab4, Rab5, and Rab11

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

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The exocyst complex in polarized exocytosis

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New Component of the Vacuolar Class C-Vps Complex Couples Nucleotide Exchange on the Ypt7 Gtpase to Snare-Dependent Docking and Fusion

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The exocyst is a Ral effector complex

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Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p

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Cdc42 Interacts with the Exocyst and Regulates Polarized Secretion

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The exocyst defrocked, a framework of rods revealed

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Sec15 Is an Effector for the Rab11 GTPase in Mammalian Cells

Zhang, X.-M., Ellis, S., Sriratana, A., Mitchell, C. A., & Rowe, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402264200 · Cited by 257

The Exocyst at a Glance

Wu, B., & Guo, W. (2015) · Journal of Cell Science · doi:10.1242/jcs.156398 · Cited by 240

Ral GTPases Regulate Exocyst Assembly through Dual Subunit Interactions

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Exocytosis: The Many Masters of the Exocyst

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Mutations in the Exocyst Component Sec5 Disrupt Neuronal Membrane Traffic, but Neurotransmitter Release Persists

Murthy, M., Garza, D., Scheller, R. H., & Schwarz, T. L. (2003) · Neuron · doi:10.1016/s0896-6273(03)00031-x · Cited by 202

Rab10 Regulates Membrane Transport through Early Endosomes of Polarized Madin-Darby Canine Kidney Cells

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Mutations in Drosophila sec15 Reveal a Function in Neuronal Targeting for a Subset of Exocyst Components

Mehta, S. Q., Hiesinger, P. R., Beronja, S., Zhai, R. G., Schulze, K. L., Verstreken, P., Cao, Y., Zhou, Y., Tepass, U., Crair, M. C., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.02.029 · Cited by 136

Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex

Fukai, S., Matern, H. T., Jagath, J. R., Scheller, R. H., & Brunger, A. T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg329 · Cited by 126

Essential function of Drosophila Sec6 in apical exocytosis of epithelial photoreceptor cells

Beronja, S., Laprise, P., Papoulas, O., Pellikka, M., Sisson, J., & Tepass, U. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200410081 · Cited by 120

The TC10–Exo70 Complex Is Essential for Membrane Expansion and Axonal Specification in Developing Neurons

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Minireview: How Peptide Hormone Vesicles Are Transported to the Secretion Site for Exocytosis

Park, J. J., & Loh, Y. P. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0209 · Cited by 81

Rab10 associates with primary cilia and the exocyst complex in renal epithelial cells

Babbey, C. M., Bacallao, R. L., & Dunn, K. W. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00198.2010 · Cited by 81

Exocyst function regulated by effector phosphorylation

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RalA-Exocyst Interaction Mediates GTP-dependent Exocytosis

Wang, L., Li, G., & Sugita, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400522200 · Cited by 68

Regulation of Platelet Dense Granule Secretion by the Ral GTPase-Exocyst Pathway

Kawato, M., Shirakawa, R., Kondo, H., Higashi, T., Ikeda, T., Okawa, K., Fukai, S., Nureki, O., Kita, T., & Horiuchi, H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705340200 · Cited by 46

Structure of the GTPase-binding Domain of Sec5 and Elucidation of its Ral Binding Site

Mott, H. R., Nietlispach, D., Hopkins, L. J., Mirey, G., Camonis, J. H., & Owen, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300155200 · Cited by 39

Intracellular machinery for the transport of AMPA receptors.

Esteban, J. A. (2008) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707525 · Cited by 29

Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci

Barbosa, I. C. R., De Bellis, D., Flückiger, I., Bellani, E., Grangé-Guerment, M., Hématy, K., & Geldner, N. (2023) · Nature Communications · doi:10.1038/s41467-023-37265-7 · Cited by 28

Structure of a membrane tethering complex incorporating multiple SNAREs

DAmico, K. A., Stanton, A. E., Shirkey, J. D., Travis, S. M., Jeffrey, P. D., & Hughson, F. M. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01164-8 · Cited by 13

Benzothiourea Derivatives Target the Secretory Pathway of the Human Fungal Pathogen Cryptococcus neoformans

Beattie, S. R., Schnicker, N. J., Murante, T., Kettimuthu, K., Williams, N. S., Gakhar, L., & Krysan, D. J. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00478 · Cited by 10

Septins function in exocytosis via physical interactions with the exocyst complex in fission yeast cytokinesis

Singh, D., Liu, Y., Zhu, Y.-H., Zhang, S., Naegele, S. M., & Wu, J.-Q. (2025) · eLife · doi:10.7554/elife.101113 · Cited by 8

Continuum architecture dynamics of vesicle tethering in exocytosis

Puig-Tintó, M., Ortiz, S., Meek, S., Coray, R., Betancur, L. I., Hernández, A. C., Castellet, A., Kramer, E., Hoess, P., Mund, M., et al. (2026) · Cell · doi:10.1016/j.cell.2025.11.038 · Cited by 3

Septins function in exocytosis via physical interactions with the exocyst complex in fission yeast cytokinesis

Singh, D., Liu, Y., Zhu, Y.-H., Zhang, S., Naegele, S. M., & Wu, J.-Q. (2025) · eLife · doi:10.7554/elife.101113.3 · Cited by 3