De novo formation of early endosomes during Rab5-to-Rab7a transition
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Abstract
Rab5 and Rab7a are the main determinants of early and late endosomes and are important regulators of endosomal progression. The transport from early endosomes to late endosome seems to be regulated through an endosomal maturation switch, where Rab5 is gradually exchanged by Rab7a on the same endosome. Here, we provide new insight into the mechanism of endosomal maturation, for which we have discovered a stepwise Rab5 detachment, sequentially regulated by Rab7a. The initial detachment of Rab5 is Rab7a independent and demonstrates a diffusion-like first-phase exchange between the cytosol and the endosomal membrane, and a second phase, in which Rab5 converges into specific domains that detach as a Rab5 indigenous endosome. Consequently, we show that early endosomal maturation regulated through the Rab5-to-Rab7a switch induces the formation of new fully functional Rab5-positive early endosomes. Progression through stepwise early endosomal maturation regulates the direction of transport and, concomitantly, the homeostasis of early endosomes.
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Internalized cargo localizes to late endosomes approximately 10 minutes after uptake.
“previous studies established that internalized cargo localizes to late endosomes ~10 minutes after uptake29–31”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [30]
The Introduction describes transport of internalized material through early-to-late endosomal maturation, supporting the general destination. But the Results’ minute-scale measurements concern Rab5 detachment and Rab7a recruitment during maturation, not when cargo reaches late endosomes after uptake. The cited paper does not establish the approximately 10-minute timing. (LLM, conf=0.78)
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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 · see citing works
Huotari, J., & Helenius, A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.286 · Cited by 2,279 · see citing works
Rab Conversion as a Mechanism of Progression from Early to Late Endosomes
Rink, J. C., Ghigo, É., Kalaidzidis, Y. L., & Zerial, M. (2005) · Cell · doi:10.1016/j.cell.2005.06.043 · Cited by 1,680 · see citing works
Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
Pelkmans, L., Kartenbeck, J., & Helenius, A. (2001) · Nature Cell Biology · doi:10.1038/35074539 · Cited by 1,236 · see citing works
Studying protein dynamics in living cells
Lippincott‐Schwartz, J., Snapp, E. L., & Kenworthy, A. K. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35073068 · Cited by 1,192 · see citing works
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 · see citing works
Rab7: A Key to Lysosome Biogenesis
Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J., & van Deurs, B. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.467 · Cited by 1,084 · see citing works
Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis.
Stenmark, H., Parton, R. G., Steele‐Mortimer, O., Lütcke, A., Gruenberg, J., & Zerial, M. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06381.x · Cited by 968 · see citing works
Identification of the Switch in Early-to-Late Endosome Transition
Poteryaev, D., Datta, S., Ackema, K., Zerial, M., & Spang, A. (2010) · Cell · doi:10.1016/j.cell.2010.03.011 · Cited by 752 · see citing works
Stenmark, H., & Olkkonen, V. M. (2001) · Genome biology · doi:10.1186/gb-2001-2-5-reviews3007 · Cited by 714 · see citing works
Rab 7: an important regulator of late endocytic membrane traffic.
Feng, Y., Press, B., & Wandinger‐Ness, A. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.6.1435 · Cited by 637 · see citing works
Endosome maturation, transport and functions
Scott, C. C., Vacca, F., & Gruenberg, J. E. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.03.034 · Cited by 581 · see citing works
FRAP analysis of binding: proper and fitting
Sprague, B. L., & McNally, J. G. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.12.001 · Cited by 569 · see citing works
MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
Bakke, O., & Dobberstein, B. (1990) · Cell · doi:10.1016/0092-8674(90)90137-4 · Cited by 565 · see citing works
Self-citationRab 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 528 · see citing works
Organelle identity and the signposts for membrane traffic
Behnia, R., & Munro, S. (2005) · Nature · doi:10.1038/nature04397 · Cited by 525 · see citing works
Vanlandingham, P. A., & Ceresa, B. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809277200 · Cited by 441 · see citing works
Helenius, A., Mellman, I., Wall, D. A., & Hubbard, A. L. (1983) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(83)90350-x · Cited by 428 · see citing works
Barr, F. A., & Lambright, D. G. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.007 · Cited by 412 · see citing works
The Mon1-Ccz1 Complex Is the GEF of the Late Endosomal Rab7 Homolog Ypt7
Nordmann, M., Cabrera, M., Perz, A., Bröcker, C., Ostrowicz, C. W., Engelbrecht-Vandré, S., & Ungermann, C. (2010) · Current Biology · doi:10.1016/j.cub.2010.08.002 · Cited by 395 · see citing works
Rab GTPase Function in Endosome and Lysosome Biogenesis
Langemeyer, L., Fröhlich, F., & Ungermann, C. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.06.007 · Cited by 393 · see citing works
Rab GTPases: master regulators that establish the secretory and endocytic pathways
Pfeffer, S. R. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-10-0737 · Cited by 297 · see citing works
Rab proteins: The key regulators of intracellular vesicle transport
Bhuin, T., & Roy, J. K. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.07.027 · Cited by 280 · see citing works
Lateral mobility in membranes as detected by fluorescence recovery after photobleaching
Yguerabide, J., Schmidt, J. A., & Yguerabide, E. E. (1982) · Biophysical Journal · doi:10.1016/s0006-3495(82)84459-7 · Cited by 220 · see citing works
Lippé, R., Miączyńska, M., Rybin, V., Runge, A., & Zerial, M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.7.2219 · Cited by 216 · see citing works
Dunn, K., & Maxfield, F. R. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.117.2.301 · Cited by 195 · see citing works
Spinosa, M. R., Progida, C., Luca, A. D., Colucci, A. M. R., Alifano, P., & Bucci, C. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3677-07.2008 · Cited by 176 · see citing works
Maturation models for endosome and lysosome biogenesis
Murphy, R. F. (1991) · Trends in Cell Biology · doi:10.1016/0962-8924(91)90022-2 · Cited by 172 · see citing works
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 · see citing works
The arguments for pre-existing early and late endosomes
Griffiths, G., & Grüenberg, J. (1991) · Trends in Cell Biology · doi:10.1016/0962-8924(91)90047-d · Cited by 157 · see citing works
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 · see citing works
Romagnoli, P., Layet, C., Yewdell, J. W., Bakke, O., & Germain, R. N. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.3.583 · Cited by 146 · see citing works
Self-citationUltrastructural characterization of giant endosomes induced by GTPase-deficient Rab5
Wegner, C. S., Malerød, L., Pedersen, N. M., Progida, C., Bakke, O., Stenmark, H., & Brech, A. (2009) · Histochemistry and Cell Biology · doi:10.1007/s00418-009-0643-8 · Cited by 119 · see citing works
Self-citationCabrera, M., Nordmann, M., Perz, A., Schmedt, D., Gerondopoulos, A., Barr, F., Piehler, J., Engelbrecht-Vandré, S., & Ungermann, C. (2014) · Journal of Cell Science · doi:10.1242/jcs.140921 · Cited by 102 · see citing works
Mitotic partitioning of endosomes and lysosomes
Bergeland, T., Widerberg, J., Bakke, O., & Nordeng, T. W. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00177-4 · Cited by 93 · see citing works
Self-citationTBC-2 Regulates RAB-5/RAB-7-mediated Endosomal Trafficking in Caenorhabditis elegans
Chotard, L., Mishra, A. K., Sylvain, M.-A., Tuck, S., Lambright, D. G., & Rocheleau, C. E. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-11-0947 · Cited by 89 · see citing works
Duclos, S., Corsini, R., & Desjardins, M. (2003) · Journal of Cell Science · doi:10.1242/jcs.00259 · Cited by 86 · see citing works
A conserved and regulated mechanism drives endosomal Rab transition
Langemeyer, L., Borchers, A.-C., Herrmann, E., Füllbrunn, N., Han, Y., Perz, A., Auffarth, K., Kümmel, D., & Ungermann, C. (2020) · eLife · doi:10.7554/elife.56090 · Cited by 83 · see citing works
Rabex-5 Is a Rab22 Effector and Mediates a Rab22-Rab5 Signaling Cascade in Endocytosis
Zhu, H., Liang, Z., & Li, G. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-06-0453 · Cited by 78 · see citing works
The fusion of early endosomes induces molecular motor-driven tubule formation and fission.
Skjeldal, F. M., Strunze, S., Bergeland, T., Walseng, E., FGregers, T., & Bakke, O. (2012) · Journal of Cell Science · doi:10.1242/jcs.092569 · Cited by 71 · see citing works
Self-citationLi, W., Zou, W., Zhao, D., Yan, J., Zhu, Z., Lu, J., & Wang, X. (2009) · Development · doi:10.1242/dev.035949 · Cited by 65 · see citing works
Phosphoinositides in the control of lysosome function and homeostasis
Ebner, M., Koch, P. A., & Haucke, V. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190158 · Cited by 46 · see citing works
The Cytoplasmic Tail of Invariant Chain Regulates Endosome Fusion and Morphology
Nordeng, T. W., Gregers, T. F., Kongsvik, T. L., Méresse, S., Gorvel, J., Jourdan, F. L., Motta, A., & Bakke, O. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0478 · Cited by 45 · see citing works
Self-citationA non-linear system patterns Rab5 GTPase on the membrane
Cezanne, A., Lauer, J. L., Solomatina, A., Sbalzarini, I. F., & Zerial, M. (2020) · eLife · doi:10.7554/elife.54434 · Cited by 43 · see citing works
MHC Class II-Associated Invariant Chain-Induced Enlarged Endosomal Structures: A Morphological Study
Stang, E., & Bakke, O. (1997) · Experimental Cell Research · doi:10.1006/excr.1997.3617 · Cited by 42 · see citing works
Self-citationKamentseva, R., Kosheverova, V., Харченко, М. В., Zlobina, M., Salova, A. V., Belyaeva, T. N., Nikolsky, N. N., & Корнилова, Е. С. (2020) · PLoS ONE · doi:10.1371/journal.pone.0232532 · Cited by 37 · see citing works
The Lysosome and Intracellular Signalling.
Hesketh, G., Wartosch, L., Davis, L. J., Bright, N. A., & Luzio, J. P. (2018) · Progress in molecular and subcellular biology · doi:10.1007/978-3-319-96704-2_6 · Cited by 36 · see citing works
Cell‐cycle‐dependent binding kinetics for the early endosomal tethering factor EEA1
Bergeland, T., Haugen, L. H., Landsverk, O. J. B., Stenmark, H., & Bakke, O. (2008) · EMBO Reports · doi:10.1038/sj.embor.7401152 · Cited by 31 · see citing works
Self-citationInvariant chain increases the half‐life of MHC II by delaying endosomal maturation
Landsverk, O. J. B., Barois, N., Gregers, T. F., & Bakke, O. (2010) · Immunology and Cell Biology · doi:10.1038/icb.2010.143 · Cited by 29 · see citing works
Self-citationThe cytoplasmic tail of invariant chain modulates antigen processing and presentation
Gregers, T. F., Nordeng, T. W., Birkeland, H. C. G., Sandlie, I., & Bakke, O. (2003) · European Journal of Immunology · doi:10.1002/immu.200310001 · Cited by 28 · see citing works
Self-citationRabx-5 Regulates RAB-5 Early Endosomal Compartments and Synaptic Vesicles in C. elegans
Sann, S. B., Crane, M. M., Lu, H., & Jin, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037930 · Cited by 23 · see citing works
Engering, A. J. (1998) · International Immunology · doi:10.1093/intimm/10.11.1713 · Cited by 18 · see citing works
Margiotta, A., Frei, D. M., Sendstad, I. H., Janssen, L., Neefjes, J., & Bakke, O. (2020) · Journal of Cell Science · doi:10.1242/jcs.244624 · Cited by 16 · see citing works
Self-citationEndosomal binding kinetics of Eps15 and Hrs specifically regulate the degradation of RTKs
Haugen, L. H., Skjeldal, F. M., Bergeland, T., & Bakke, O. (2017) · Scientific Reports · doi:10.1038/s41598-017-17320-2 · Cited by 11 · see citing works
Self-citation
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Borchers, A.-C., Langemeyer, L., & Ungermann, C. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202105120 · Cited by 168 · see citing works
A novel live-cell imaging assay reveals regulation of endosome maturation
Podinovskaia, M., Prescianotto-Baschong, C., Buser, D. P., & Spang, A. (2021) · eLife · doi:10.7554/elife.70982 · Cited by 51 · see citing works
Liu, Y., Ma, J., Wang, X., Liu, P., Cai, C., Han, Y., Zeng, S., Feng, Z., & Shen, H. (2023) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2023.106862 · Cited by 32 · see citing works
Molecular insights into endolysosomal microcompartment formation and maintenance
Kümmel, D., Herrmann, E., Langemeyer, L., & Ungermann, C. (2022) · Biological Chemistry · doi:10.1515/hsz-2022-0294 · Cited by 21 · see citing works
Coordination between ESCRT function and Rab conversion during endosome maturation
Ott, D. P., Desai, S., Solinger, J. A., Kaech, A., & Spang, A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00367-7 · Cited by 21 · see citing works
Zheng, C., Liu, X., Kong, Y., Zhang, L., Song, Q., Zhao, H., Han, L., Jiao, J., Feng, Q., & Wang, L. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.02.026 · Cited by 19 · see citing works
Wang, Q., Wang, J., Huang, Z., Li, Y., Li, H., Huang, P., Cai, Y., Wang, J., Liu, X., Lin, F., et al. (2024) · New Phytologist · doi:10.1111/nph.20235 · Cited by 19 · see citing works
Spatial regulation of endosomes in growing dendrites
Yap, C. C., & Winckler, B. (2022) · Developmental Biology · doi:10.1016/j.ydbio.2022.03.004 · Cited by 14 · see citing works
Song, C., & Broadie, K. S. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2216887120 · Cited by 14 · see citing works
Mehta, K., Yentsch, H., Lee, J., Yook, Y., Lee, K. Y., Gao, T. T., Tsai, N., & Zhang, K. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2322422121 · Cited by 12 · see citing works
Differences in endosomal Rab gene expression between positive and negative COVID-19 patients
Atik, N., Wirawan, F., Amalia, R., Khairani, A. F., & Pradini, G. W. (2022) · BMC Research Notes · doi:10.1186/s13104-022-06144-7 · Cited by 10 · see citing works
Chen, X., Zuo, X., Becker, A., & Mobley, W. C. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70046 · Cited by 9 · see citing works
Grziwa, S., Schäfer, J.-H., Nicastro, R., Arens, A., VIRGILIO, C. D., Fröhlich, F., Moeller, A., Gao, J., Langemeyer, L., & Ungermann, C. (2023) · Journal of Cell Science · doi:10.1242/jcs.260889 · Cited by 5 · see citing works
Rab11-Rab8 cascade dynamics in primary cilia and membrane tubules
Saha, I., Insinna, C., & Westlake, C. J. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114955 · Cited by 6 · see citing works
Lteif, M., Pallardy, M. J., & Turbica, I. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1617395 · Cited by 5 · see citing works
CRABP1-complexes in exosome secretion
Nhieu, J., Wei, C.-W., Ludwig, M., Drake, J. M., & Wei, L. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01749-w · Cited by 5 · see citing works
Shariq, M., Ahmed, F., Ansari, O., Mursaleen, A., & Sheikh, J. A. (2025) · International Reviews of Immunology · doi:10.1080/08830185.2025.2531828 · Cited by 5 · see citing works
Endolysosomal transport at the crossroads of cellular signaling
Füllbrunn, N., Ungermann, C., & Langemeyer, L. (2026) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.12.002 · Cited by 4 · see citing works
Sodium proton exchanger NHE9 pHine-tunes exosome production by impairing Rab7 activity
Duhaini, M., Fares, P., Hafezi, L., El-Zein, H., & Kondapalli, K. C. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108264 · Cited by 4 · see citing works
Jin, S., Ahn, Y., Park, J., Park, M., Lee, S., Lee, W. J., & Seo, D. (2024) · Advanced Science · doi:10.1002/advs.202306849 · Cited by 4 · see citing works
INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia
Terzioglu, G., Karp, E. S., Heuer, S. E., Chadarevian, J. P., Ahsan, F. M., Haage, V. C., Davtyan, H., Fogo, G. M., Curle, A. J., Ashour, N., et al. (2025) · doi:10.1101/2025.10.27.684632 · Cited by 3 · see citing works
Shedenkova, M. O., Gurianova, A., Krasilnikova, I. A., Sudina, A. K., Karpulevich, E., Maksimov, Y., Samburova, M. V., Guguchkin, E., Nefedova, Z., Babenko, V. A., et al. (2025) · Cells · doi:10.3390/cells14231915 · Cited by 2 · see citing works
Tong, B., Zhang, X., Zhu, D., Wang, Y., Wei, J., Ou, Z., Liang, H., Xu, H., Zhang, Z., Lei, J., et al. (2026) · EMBO Molecular Medicine · doi:10.1038/s44321-025-00371-8 · Cited by 2 · see citing works
Role of Rab5b in the defense of Cynoglossus semilaevis against Vibrio vulnificus infection
Han, T., Liu, Y., He, Z., Zhang, Y., Cao, W., Ren, J., Wang, G., Ren, Y., Gong, C., & Hou, J. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.151386 · Cited by 2 · see citing works
Wang, J., Zhang, Q., Cao, Y., 王春波, & Hamzeh, S. (2026) · Discover Oncology · doi:10.1007/s12672-026-05151-5 · Cited by 2 · see citing works
TMEM184B modulates endolysosomal acidification via the vesicular proton pump
Wright, E. B., Larsen, E. G., Padilla‐Rodriguez, M., Langlais, P. R., & Bhattacharya, M. R. C. (2025) · Journal of Cell Science · doi:10.1242/jcs.263908 · Cited by 3 · see citing works
Chen, Y., Wen, Y., Zhang, M., Nie, J., & Sun, G. (2025) · Neural Plasticity · doi:10.1155/np/8895041 · Cited by 2 · see citing works
Borowiec, B. M., Blatkiewicz, M., Dyszkiewicz-Konwińska, M., Bukowska, D., Kempisty, B., Ruciński, M., Nowicki, M. O., & Budna, J. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47040256 · Cited by 1 · see citing works
A compendium of extracellular vesicle biogenesis inhibitors: From bench to bedside
Vecchione, S., Talamillo, A., & Falcón‐Pérez, J. M. (2026) · Interdisciplinary medicine · doi:10.1002/inmd.70144 · Cited by 1 · see citing works
Jain, M. S., Rohith, S., Gowda, J., & Mallamma, T. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12069-2 · Cited by 1 · see citing works
Baker, B., Emerson, S., Tran, T., Mohapatra, N., Wang, D., Zaw, T., Doshi, A. A., Lopez, J.-M., Hassan, D., Kumar, P., et al. (2026) · Nanomedicine · doi:10.1080/17435889.2026.2698782 · Cited by 1 · see citing works
Корнилова, Е. С., Kamentseva, R., & Харченко, М. В. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00107-3
Wright, E. B., Larsen, E. G., Padilla‐Rodriguez, M., Langlais, P. R., & Bhattacharya, M. R. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.01.635992
Liu, X., Wang, S., Feng, Q., Yu, C., Zhang, W., Li, C., Yang, W., Zong, Y., Guo, L., Wang, R., et al. (2025) · Journal of Molecular Medicine · doi:10.1007/s00109-025-02570-9
Chang, J., Alenizi, S., Milioli, H. H., Lay, W., Pounraj, S., Li, Y., Shiferaw, M. S., Beheshti, E. H., & Kovačević, Ž. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.15.682724
PIKI-1, a class II PI 3-kinase, functions in endocytic trafficking
Reimann, G. R., Edeen, P. T., Conquest, S., Grant, B. D., & Fay, D. S. (2026) · PLoS Genetics · doi:10.1371/journal.pgen.1011740 · Cited by 1 · see citing works
Chang, J., Alenizi, S., Milioli, H. H., Lay, W., Pounraj, S., Li, Y., Sisay, M., Hosseini-Beheshti, E., & Kovačević, Ž. (2026) · Journal of Extracellular Vesicles · doi:10.1002/jev2.70334
The endo-lysosomal system drives lumen formation in a human epiblast model
Rengarajan, A., Wang, S., Lin, C., Elberfeld, L. E., Wettstein, J. C., Carleton, A. E., Sekulovski, N., Taniguchi, L. E., Schultz, B. E., Duncan, M. C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-77140-9
Vesicular trafficking in vascular endothelial cells: Mechanisms and homeostatic control
ZHANG, L., Han, Y., Yao, L.-T., Ning-Jing, X. U., & Jia, S. (2026) · Shengming kexue · doi:10.3724/cbls.2026137
Radaic, A., Malone, E., Lin, S., Araújo, L. D. C., Tse, I., Ganther, S., Kamarajan, P., Fenno, J. C., & Kapila, Y. L. (2026) · Pharmaceuticals · doi:10.3390/ph19101585
- Authors
- Skjeldal, F. M., Haugen, L. H., Mateus, D., Frei, D. M., Rødseth, A. V., Hu, X., & Bakke, O.
- Affiliations
- University of Oslo (NO)
- Corresponding author
- Bakke, Oddmund
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2021-04-15
- Volume
- 134
- Issue
- 8
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- PMC
- PMC8106955
- OpenAlex
- W3136209092
- Cited by
- 41
- References
- 54
- Citations by year
- 2026: 12 · 2025: 12 · 2024: 6 · 2023: 3 · 2022: 6 · 2021: 2
- FWCI
- 2.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Cell Science (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- NORA - Norwegian Open Research Archives (submittedVersion, cc-by)
- Funders
- The Norwegian Cancer Scociety (grant 113472 to O.B)
- The Research Council of Norway (grants 214183 and 230770 to O.B)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- Rab5, Rab7, early endosomes, late endosomes, endosomal maturation, endosomal transport
- MeSH terms
- Endosomes, rab5 GTP-Binding Proteins, Transport Vesicles
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 ›
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