The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Role of Rab27 in synaptic transmission at the squid giant synapse
Abstract
Small GTPase Rab is a member of a large family of Ras-related proteins, highly conserved in eukaryotic cells, and thought to regulate specific type(s) and/or specific step(s) in intracellular membrane trafficking. Given our interest in synaptic transmission, we addressed the possibility that Rab27 (a close isoform of Rab3) could be involved in cytosolic synaptic vesicle mobilization. Indeed, preterminal injection of a specific antibody against squid Rab27 (anti-sqRab27 antibody) combined with confocal microscopy demonstrated that Rab27 is present on squid synaptic vesicles. Electrophysiological study of injected synapses showed that the anti-sqRab27 antibody inhibited synaptic release in a stimulation-dependent manner without affecting presynaptic action potentials or inward Ca 2+ current. This result was confirmed in in vitro synaptosomes by using total internal reflection fluorescence microscopy. Thus, synaptosomal Ca 2+ -stimulated release of FM1-43 dye was greatly impaired by intraterminal anti-sqRab27 antibody. Ultrastructural analysis of the injected giant preterminal further showed a reduced number of docked synaptic vesicles and an increase in nondocked vesicular profiles distant from the active zone. These results, taken together, indicate that Rab27 is primarily involved in the maturation of recycled vesicles and/or their transport to the presynaptic active zone in the squid giant synapse.
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“Rab27 is known to be critical for anterograde transport within neurites and synaptic vesicle exocytosis.65,66”
From Endosomal protein DENND10 promotes developmental competence of neurite extension (2025) · cites this paper as [66]
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Cites
Rab proteins as membrane organizers
Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381
Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome
Ménasché, G., Pastural, E., Feldmann, J., Certain, S., Ersoy, F., Dupuis, S., Wulffraat, N., Bianchi, D., Fischer, A., Le Deist, F., et al. (2000) · Nature Genetics · doi:10.1038/76024 · Cited by 962
Evolution of the rab family of small GTP-binding proteins
Pereira-Leal, J. B., & Seabra, M. C. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5072 · Cited by 774
A genomic perspective on membrane compartment organization
Bock, J. B., Matern, H. T., Peden, A. A., & Scheller, R. H. (2001) · Nature · doi:10.1038/35057024 · Cited by 696
Rab GTPases: specifying and deciphering organelle identity and function
Pfeffer, S. R. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02147-x · Cited by 527
Shirataki, H., Kaibuchi, K., Sakoda, T., Kishida, S., Yamaguchi, T., Wada, K., Miyazaki, M., & Takai, Y. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2061 · Cited by 398
Fukuda, M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8351-4 · Cited by 393
Self-citationA Complete Genetic Analysis of Neuronal Rab3 Function
Schlüter, O. M., Schmitz, F., Jahn, R., Rosenmund, C., & Südhof, T. C. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1610-04.2004 · Cited by 302
Ypt and Rab GTPases: insight into functions through novel interactions
Segev, N. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00242-8 · Cited by 293
RAB3 AND SYNAPTOTAGMIN: The Yin and Yang of Synaptic Membrane Fusion
Geppert, M., & Südhof, T. C. (1998) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.21.1.75 · Cited by 254
Research works printed but not linked: 1
- 10.1128/mcb.13.4.2061-2068.1993 · DOI · Paper page
Cited by
Endosomal protein DENND10 promotes developmental competence of neurite extension
Li, A., Zhang, J., Ma, C., Qi, L., Hu, Q., Li, Q., Fang, Y., Song, J., Liu, Y., & Zhang, Y. (2025) · iScience · doi:10.1016/j.isci.2025.112385
Metadata
- Authors
- Yu, E., Kanno, E., Choi, S., Sugimori, M., Moreira, J. E., Llinás, R. R., & Fukuda, M.
- Affiliations
- *Department of Physiology and Neuroscience, New York University School of Medicine, 550 First Avenue, New York, NY 10016;
- Department of Developmental Biology and Neurosciences, Graduate School of Life Sciences, Tohoku University, Aobayama, Aoba-ku, Sendai, Miyagi 980-8578, Japan; and
- Marine Biological Laboratory, Woods Hole, MA 02543;
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-10-14
- Volume
- 105
- Issue
- 41
- Pages
- 16003-16008
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 31
- References
- 47
- Language
- en
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