The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Distribution analysis of RAB11A and RAB11B, small GTP-binding proteins, in mice
Abstract
Background RAB11 is a small GTP-binding protein that regulates intracellular trafficking of recycling endosomes and is thereby involved in several neural functions. Highly similar RAB11 isoforms are encoded by RAB11A and RAB11B genes, and their pathogenic variants are associated with similar neurodevelopmental disorders, suggesting that RAB11A and RAB11B play similar and important roles in brain development. However, the detailed distribution patterns of these isoforms in various organs, including the brain, remain undetermined. Methods and results We generated an antibody against RAB11A and analyzed the distribution of RAB11A and RAB11B in mice. RAB11A was highly expressed in the ovary and the uterus but less abundant in the brain, whereas RAB11B was abundant in the brain, the testis, the ovary, and the uterus. In the developing cortex, RAB11A was enriched in the apical endfeet of apical radial glial cells, whereas RAB11B was abundantly expressed in postmigratory neurons of the cortical plate. In the adult mouse brain, RAB11A and RAB11B were similarly expressed in most neurons, with weak RAB11A signals also observed in the neuropil. In cultured neurons, RAB11A and RAB11B showed only partial co-localization and differential distribution in both soma and neurites. Notably, RAB11A appeared to be more abundant at presynapses than RAB11B. Conclusions RAB11A and RAB11B exhibit distinct and characteristic distributions in the brain and other organs, suggesting they play different roles throughout the body. In particular, our results suggest they make distinct contributions to cortical development and regulation of the synaptic vesicle cycle.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Citations
Cites
Prevalence and architecture of de novo mutations in developmental disorders
Study, D. D. D. (2017) · Nature · doi:10.1038/nature21062 · Cited by 1,480
Plasticity-induced growth of dendritic spines by exocytic trafficking from recycling endosomes
Park, M., Salgado, J. M., Ostroff, L., Helton, T. D., Robinson, C. G., Harris, K. M., & Ehlers, M. D. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.040 · Cited by 493
Coordination of Rab8 and Rab11 in primary ciliogenesis
Knödler, A., Feng, S., Zhang, J., Zhang, X., Das, A. K., Peränen, J., & Guo, W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002401107 · Cited by 491
Myosin Vb mobilizes recycling endosomes and AMPA receptors for postsynaptic plasticity
Wang, Z., Edwards, J. G., Riley, N., Provance, D. W., Karcher, R., Li, X.-D., Davison, I. G., Ikebe, M., Mercer, J. A., Kauer, J. A., et al. (2008) · Cell · doi:10.1016/j.cell.2008.09.057 · Cited by 470
High Rate of Recurrent De Novo Mutations in Developmental and Epileptic Encephalopathies
Hamdan, F. F., Myers, C. T., Cossette, P., Lemay, P., Spiegelman, D., Laporte, A. D., Nassif, C., Diallo, O., Monlong, J., Cadieux-Dion, M., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.09.008 · Cited by 445
Kawauchi, T., Sekine, K., Shikanai, M., Chihama, K., Tomita, K., Kubo, K., Nakajima, K., Nabeshima, Y.-I., & Hoshino, M. (2010) · Neuron · doi:10.1016/j.neuron.2010.07.007 · Cited by 340
Wilson, G. M., Fielding, A. B., Simon, G. C., Yu, X., Andrews, P. D., Hames, R. S., Frey, A. M., Peden, A. A., Gould, G. W., & Prekeris, R. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-10-0927 · Cited by 312
N-cadherin mediates cortical organization in the mouse brain
Kadowaki, M., Nakamura, S., Machoň, O., Krauss, S. J. K., Radice, G. L., & Takeichi, M. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.12.014 · Cited by 298
Rab11 Family Interacting Protein 2 Associates with Myosin Vb and Regulates Plasma Membrane Recycling
Hales, C. M., Vaerman, J., & Goldenring, J. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209270200 · Cited by 295
Synaptic Vesicle Pools and Dynamics
Alabi, A. A., & Tsien, R. W. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013680 · Cited by 284
The Synaptic Vesicle Cycle Revisited: New Insights into the Modes and Mechanisms
Chanaday, N. L., Cousin, M. A., Milosevic, I., Watanabe, S., & Morgan, J. R. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.1158-19.2019 · Cited by 255
Horgan, C. P., Hanscom, S. R., Jolly, R. S., Futter, C. E., & McCaffrey, M. (2009) · Journal of Cell Science · doi:10.1242/jcs.052670 · Cited by 209
Protrudin Induces Neurite Formation by Directional Membrane Trafficking
Shirane, M., & Nakayama, K. I. (2006) · Science · doi:10.1126/science.1134027 · Cited by 200
Dollar, G., Struckhoff, E. C., Michaud, J., & Cohen, R. S. (2002) · Development · doi:10.1242/dev.129.2.517 · Cited by 176
Goldenring, J. R., Shen, K. R., Vaughan, H. D., & Modlin, I. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46639-7 · Cited by 165
Divergent Functions of Neuronal Rab11b in Ca2+-Regulated versus Constitutive Exocytosis
Khvotchev, M. V., Ren, M., Takamori, S., Jahn, R., & Südhof, T. C. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-33-10531.2003 · Cited by 132
Positioning of AMPA receptor-containing endosomes regulates synapse architecture
Esteves da Silva, M., Adrian, M., Schätzle, P., Lipka, J., Watanabe, T., Cho, S., Futai, K., Wierenga, C. J., Kapitein, L. C., & Hoogenraad, C. C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.062 · Cited by 126
Synaptic Vesicle Clusters at Synapses: A Distinct Liquid Phase?
Milovanović, D., & Camilli, P. V. D. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.013 · Cited by 120
Neural Progenitor Cell Polarity and Cortical Development
Arai, Y., & Taverna, E. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00384 · Cited by 112
Pavlos, N. J., Grønborg, M., Riedel, D., Chua, J. J. E., Boyken, J., Kloepper, T. H., Urlaub, H., Rizzoli, S. O., & Jahn, R. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0907-10.2010 · Cited by 108
Lapierre, L. A., Dorn, M. C., Zimmerman, C. F., Navarre, J., Burnette, J. O., & Goldenring, J. R. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00340-9 · Cited by 97
Pasqualato, S., Senic-Matuglia, F., Renault, L., Goud, B., Salamero, J., & Cherfils, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310558200 · Cited by 95
Rab11a is required for apical protein localisation in the intestine
Sobajima, T., Yoshimura, S., Iwano, T., Kunii, M., Watanabe, M., Atik, N., Mushiake, S., Morii, E., Koyama, Y., Miyoshi, E., et al. (2014) · Biology Open · doi:10.1242/bio.20148532 · Cited by 90
Self-citationMolecular Analysis of Mouse Rab11b: A New Type of Mammalian YPT/Rab Protein
Lai, F., Stubbs, L. J., & Artzt, K. (1994) · Genomics · doi:10.1006/geno.1994.1434 · Cited by 76
LMTK1/AATYK1 Is a Novel Regulator of Axonal Outgrowth That Acts via Rab11 in a Cdk5-Dependent Manner
Takano, T., Tomomura, M., Yoshioka, N., Tsutsumi, K., Terasawa, Y., Saito, T., Kawano, H., Kamiguchi, H., Fukuda, M., & Hisanaga, S.-I. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5317-11.2012 · Cited by 71
Bertoli‐Avella, A. M., Kandaswamy, K. K., Khan, S., Ordonez‐Herrera, N., Tripolszki, K., Beetz, C., Rocha, M. E., Urzi, A., Hotakainen, R., Leubauer, A., et al. (2021) · Genetics in Medicine · doi:10.1038/s41436-021-01159-0 · Cited by 62
TBC1D9B functions as a GTPase-activating protein for Rab11a in polarized MDCK cells
Gallo, L. I., Liao, Y., Ruiz, W. G., Clayton, D. R., Li, M., Liu, Y., Jiang, Y., Fukuda, M., Apodaca, G., & Yin, X. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-10-0604 · Cited by 51
Lamers, I. J. C., Reijnders, M. R. F., Venselaar, H., Kraus, A., Jansen, S., Vries, B. B. A. D., Houge, G., Gradek, G. A., Seo, J., Choi, M., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.09.015 · Cited by 50
Kokotos, A. C., Peltier, J., Davenport, E. C., Trost, M., & Cousin, M. A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809189115 · Cited by 50
Structural determinants of Rab11 activation by the guanine nucleotide exchange factor SH3BP5
Jenkins, M. L., Margaria, J. P., Stariha, J. T., Hoffmann, R. M., McPhail, J. A., Hamelin, D. J., Boulanger, M. J., Hirsch, E., & Burke, J. E. (2018) · Nature Communications · doi:10.1038/s41467-018-06196-z · Cited by 48
Wu, H., Li, H., Bai, T., Han, L., Ou, J., Xun, G., Zhang, Y., Wang, Y., Duan, G., Zhao, N., et al. (2019) · Clinical Genetics · doi:10.1111/cge.13665 · Cited by 42
The LMTK1-TBC1D9B-Rab11A Cascade Regulates Dendritic Spine Formation via Endosome Trafficking
Nishino, H., Saito, T., Wei, R., Takano, T., Tsutsumi, K., Taniguchi, M., Ando, K., Tomomura, M., Fukuda, M., & Hisanaga, S. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.3209-18.2019 · Cited by 34
Rab11a drives adhesion molecules to the surface of endometrial epithelial cells
Kakar, R., Brahmbhatt, K., Chauhan, B., Katkam, R. R., Bashir, T., Gawde, H., Mayadeo, N., Chaudhari, U. K., & Sachdeva, G. (2018) · Human Reproduction · doi:10.1093/humrep/dey365 · Cited by 29
Primary cilia influence progenitor function during cortical development
Zaidi, D., Chinnappa, K., & Francis, F. (2022) · Cells · doi:10.3390/cells11182895 · Cited by 19
STK25 and MST3 Have Overlapping Roles to Regulate Rho GTPases during Cortical Development
Matsuki, T., Iio, A., Ueda, M., Tsuneura, Y., Howell, B. W., & Nakayama, A. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.0523-21.2021 · Cited by 14
Self-citationAhmad, N., Fazeli, W., Schließke, S., Lesca, G., Gokce‐Samar, Z., Mekbib, K. Y., Jin, S. C., Burton, J. E., Hoganson, G. E., Petersen, A. K., et al. (2023) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2023.08.023 · Cited by 4
Expression analysis of type I ARF small GTPases ARF1-3 during mouse brain development
Matsuki, T., Hamada, N., Ito, H., Sugawara, R., Iwamoto, I., Nakayama, A., & Nagata, K. (2024) · Molecular Biology Reports · doi:10.1007/s11033-023-09142-5 · Cited by 2
Self-citationCohort Expansion and Genotype-Phenotype Analysis of RAB11A-Associated Neurodevelopmental Disorder
Borroto, M. C., Patel, H., Srivastava, S., Swanson, L. C., Keren, B., Whalen, S., Mignot, C., Wang, X., Chen, Q., Rosenfeld, J. A., et al. (2024) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2024.07.010 · Cited by 2
Tsuneura, Y., Kawai, T., Yamada, K., Aoki, S., Nakashima, M., Eda, S., Matsuki, T., Nishikawa, M., Nagata, K., Enokido, Y., et al. (2023) · Human Mutation · doi:10.1155/2023/8126544 · Cited by 1
Self-citationEnrichment of rab11, a small GTP-binding protein, in gastric parietal cells
Goldenring, J. R., Soroka, C. J., Shen, K. R., Tang, L. H., Rodriguez, W., Vaughan, H. D., Stoch, S. A., & Modlin, I. M. (1994) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1994.267.2.g187
Flagged first, then by citations
Cited by
Still being checked.
Metadata
- Authors
- Tsuneura, Y., Matsuki, T., Eda, S., Hamada, N., Harada, A., Nagata, K.-I., & Nakayama, A.
- Affiliations
- Institute for Developmental Research (JP)
- The University of Osaka (JP)
- Corresponding author
- Nakayama, Atsuo
- Venue
- Molecular Biology Reports
- Published
- 2025-01-30
- Volume
- 52
- Issue
- 1
- Pages
- 178-178
- ISSN
- 0301-4851 (ISSN-L)
- 1573-4978
- OpenAlex
- W4406962293
- Cited by
- 0
- References
- 39
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Molecular Biology Reports (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (JP22K15912, JP20K08224)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- Rab11a, Rab11b, small GTPases, recycling endosomes, intracellular trafficking, cortical development, radial glia, presynaptic localization, synaptic vesicle recycling, brain development, neurodevelopmental disorders, tissue-specific gene expression
- MeSH terms
- rab11 GTP-Binding Proteins, Animals, Brain, Female, Male, Mice, Inbred C57BL, Neurons, Ovary, Uterus, rab GTP-Binding Proteins, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
