The DOI matches its Crossref record; 233 of the 233 references it cites were found in a registry or an index.
Spoiled for Choice: Diverse Endocytic Pathways Function at the Cell Surface
Open accessAbstract
Endocytosis has long been identified as a key cellular process involved in bringing in nutrients, in clearing cellular debris in tissue, in the regulation of signaling, and in maintaining cell membrane compositional homeostasis. While clathrin-mediated endocytosis has been most extensively studied, a number of clathrin-independent endocytic pathways are continuing to be delineated. Here we provide a current survey of the different types of endocytic pathways available at the cell surface and discuss a new classification and plausible molecular mechanisms for some of the less characterized pathways. Along with an evolutionary perspective of the origins of some of these pathways, we provide an appreciation of the distinct roles that these pathways play in various aspects of cellular physiology, including the control of signaling and membrane tension.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Given the physiological size of melanosomes (0.3–0.5 μm in diameter), only macropinocytosis and phagocytosis are predicted to allow the internalization of such large cargo [ 51 , 52 , 53 , 54 ].”
From Melanin's Journey from Melanocytes to Keratinocytes: Uncovering the Molecular Mechanisms of Melanin Transfer and Processing (2023) · cites this paper as [54]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929
Regulated portals of entry into the cell
Conner, S. D., & Schmid, S. L. (2003) · Nature · doi:10.1038/nature01451 · Cited by 3,958
Doherty, G. J., & McMahon, H. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.110540 · Cited by 3,075
Phosphoinositides in cell regulation and membrane dynamics
Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790
Huotari, J., & Helenius, A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.286 · Cited by 2,448
Caveolin, a protein component of caveolae membrane coats
Rothberg, K. G., Heuser, J. E., Donzell, W. C., Ying, Y., Glenney, J. R., & Anderson, R. G. W. (1992) · Cell · doi:10.1016/0092-8674(92)90143-z · Cited by 2,259
Molecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223
Maxfield, F. R., & McGraw, T. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1315 · Cited by 1,729
Mechanisms of clathrin-mediated endocytosis
Kaksonen, M., & Roux, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.132 · Cited by 1,698
Macropinocytosis of protein is an amino acid supply route in Ras-transformed cells
Commisso, C., Davidson, S. M., Soydaner-Azeloglu, R. G., Parker, S. J., Kamphorst, J. J., Hackett, S., Grabocka, E., Nofal, M., Drebin, J. A., Thompson, C. B., et al. (2013) · Nature · doi:10.1038/nature12138 · Cited by 1,683
Research works printed but not linked: 1
- Palade GE., 1953, J. Appl. Phys., 24, 1424
Cited by
Sorted by citations
Key principles and methods for studying the endocytosis of biological and nanoparticle therapeutics
Rennick, J. J., Johnston, A. P. R., & Parton, R. G. (2021) · Nature Nanotechnology · doi:10.1038/s41565-021-00858-8 · Cited by 1,566
TLR4 and CD14 trafficking and its influence on LPS-induced pro-inflammatory signaling
Ciesielska, A., Matyjek, M., & Kwiatkowska, K. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03656-y · Cited by 1,420
Targeted protein degradation: advances in drug discovery and clinical practice
Zhong, G., Chang, X., Xie, W., & Zhou, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02004-x · Cited by 326
Endocytosis in cancer and cancer therapy
Banushi, B., Joseph, S. R., Lum, B., Lee, J. J., & Simpson, F. (2023) · Nature reviews. Cancer · doi:10.1038/s41568-023-00574-6 · Cited by 252
Gandek, T. B., van der Koog, L., & Nagelkerke, A. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202300319 · Cited by 256
Endocytosis in the context-dependent regulation of individual and collective cell properties
Sigismund, S., Lanzetti, L., Scita, G., & Di Fiore, P. P. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00375-5 · Cited by 132
Endocytosis of abiotic nanomaterials and nanobiovectors: Inhibition of membrane trafficking
Makvandi, P., Chen, M., Sartorius, R., Zarrabi, A., Ashrafizadeh, M., Moghaddam, F. D., Ma, J., Mattoli, V., & Tay, F. R. (2021) · Nano Today · doi:10.1016/j.nantod.2021.101279 · Cited by 131
Endocytosis and Organelle Targeting of Nanomedicines in Cancer Therapy
Wang, X., Qiu, Y., Wang, M., Zhang, C.-H., Zhang, T., Zhou, H., Zhao, W., Zhao, W., Xia, G., & Shao, R. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s274289 · Cited by 128
Molecular mechanism of Fast Endophilin-Mediated Endocytosis
Casamento, A., & Boucrot, E. (2020) · Biochemical Journal · doi:10.1042/bcj20190342 · Cited by 110
Unconventional endocytic mechanisms
Renard, H., & Boucrot, E. (2021) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2021.03.001 · Cited by 102
Nanoparticle entry into cells; the cell biology weak link
Griffiths, G. W., Grüenberg, J., Marsh, M., Wohlmann, J., Jones, A. T., & Parton, R. G. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114403 · Cited by 101
Bento-Lopes, L., Cabaço, L. C., Charneca, J., Neto, M. V., Seabra, M. C., & Barral, D. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411289 · Cited by 114
Multiple roles for actin in secretory and endocytic pathways
Chakrabarti, R., Lee, M., & Higgs, H. N. (2021) · Current Biology · doi:10.1016/j.cub.2021.03.038 · Cited by 87
Lysosomal microautophagy: an emerging dimension in mammalian autophagy
Kuchitsu, Y., & Taguchi, T. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.11.005 · Cited by 93
Prabhakara, C., Godbole, R. K., Sil, P., Jahnavi, S., Gulzar, S.-E.-J., van Zanten, T. S., Sheth, D., Subhash, N., Chandra, A., Shivaraj, A., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009706 · Cited by 82
Self-citationThe Biology of Endosomal Escape: Strategies for Enhanced Delivery of Therapeutics
Chahal, G., Helbig, K. J., Parton, R. G., & Monson, E. A. (2026) · ACS Nano · doi:10.1021/acsnano.5c18112 · Cited by 89
Divecha, Y. A., Rampes, S., Tromp, S., Boyanova, S., Fleckney, A. L., Fidanboylu, M., & Thomas, S. A. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100052 · Cited by 83
The role of lipid species in membranes and cancer-related changes
Skotland, T., Kavaliauskiene, S., & Sandvig, K. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09872-z · Cited by 69
Cai, W.-Q., Liang, W., Li, D., Dai, W., Li, Z., Wei, X., Cheng, L., Zhang, B., & Yang, Q.-Q. (2025) · ACS Nano · doi:10.1021/acsnano.4c14373 · Cited by 81
Mechanical Regulation of Endocytosis: New Insights and Recent Advances
Joseph, J. G., & Liu, A. P. (2020) · Advanced Biosystems · doi:10.1002/adbi.201900278 · Cited by 67
Cargo-specific recruitment in clathrin- and dynamin-independent endocytosis
Moreno‐Layseca, P., Jäntti, N. Z., Godbole, R. K., Sommer, C., Jacquemet, G., Al‐Akhrass, H., Conway, J. R. W., Kronqvist, P., Kallionpää, R., Oliveira‐Ferrer, L., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00767-x · Cited by 73
Self-citationExploiting cancer’s drinking problem: regulation and therapeutic potential of macropinocytosis
Puccini, J., Badgley, M. A., & Bar‐Sagi, D. (2021) · Trends in cancer · doi:10.1016/j.trecan.2021.09.004 · Cited by 67
Cholera Toxin as a Probe for Membrane Biology
Kenworthy, A. K., Schmieder, S. S., Raghunathan, K., Tiwari, A., Wang, T., Kelly, C. V., & Lencer, W. I. (2021) · Toxins · doi:10.3390/toxins13080543 · Cited by 61
Balancing lysosome abundance in health and disease
Mutvei, A. P., Nagiec, M. J., & Blenis, J. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01197-7 · Cited by 62
Potential therapies and diagnosis based on Golgi-targeted nano drug delivery systems
Zhang, M., Xu, N., Xu, W., Ling, G., & Zhang, P. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105861 · Cited by 54
Wu, J., Zhao, R., Zhao, L., Xu, Q., Jin, L., & Ma, F. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.129963 · Cited by 49
Valsalakumari, R., Yadava, S. K., Szwed, M., Pandya, A. D., Mælandsmo, G. M., Torgersen, M. L., Iversen, T., Skotland, T., Sandvig, K., & Giri, J. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.120217 · Cited by 42
The endocytic pathway taken by cationic substances requires Rab14 but not Rab5 and Rab7
Trofimenko, E., Homma, Y., Fukuda, M., & Widmann, C. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109945 · Cited by 44
Glycans in autophagy, endocytosis and lysosomal functions
Reggiori, F., Gabius, H., Aureli, M., Römer, W., Sonnino, S., & Eskelinen, E. (2021) · Glycoconjugate Journal · doi:10.1007/s10719-021-10007-x · Cited by 37
Unconventional endocytosis and trafficking of transferrin receptor induced by iron
Gammella, E., Lomoriello, I. S., Conte, A., Freddi, S., Alberghini, A., Poli, M., Sigismund, S., Cairo, G., & Recalcati, S. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-02-0129 · Cited by 37
Endocytosis-like DNA uptake by cell wall-deficient bacteria
Kapteijn, R., Shitut, S., Aschmann, D., Zhang, L., de Beer, M. A., Daviran, D., Roverts, R., Akiva, A., van Wezel, G. P., Kros, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33054-w · Cited by 36
Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins
Tsai, F., Simunovic, M., Sorre, B., Bertin, A., Manzi, J., Callan-Jones, A., & Bassereau, P. M. (2021) · Soft Matter · doi:10.1039/d0sm01573c · Cited by 33
Membrane-actin interactions in morphogenesis: Lessons learned from Drosophila cellularization
Sokac, A. M., Biel, N., & Renzis, S. D. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.028 · Cited by 35
The Curie temperature: a key playmaker in self-regulated temperature hyperthermia
Niraula, G., Wu, C., Yu, X., Malik, S., Verma, D. S., Yang, R., Zhao, B., Ding, S., Zhang, W., & Sharma, S. K. (2023) · Journal of Materials Chemistry B · doi:10.1039/d3tb01437a · Cited by 33
Dynamin-Independent Mechanisms of Endocytosis and Receptor Trafficking
Gundu, C., Arruri, V. K., Yadav, P., Navik, U., Kumar, A., Amalkar, V. S., Vikram, A., & Gaddam, R. R. (2022) · Cells · doi:10.3390/cells11162557 · Cited by 32
Transcytosis in the development and morphogenesis of epithelial tissues
Serra, N. D., & Sundaram, M. V. (2021) · The EMBO Journal · doi:10.15252/embj.2020106163 · Cited by 29
Caveolae as Potential Hijackable Gates in Cell Communication
Dudău, M., Codrici, E., Tănase, C., Gherghiceanu, M., Enciu, A., & Hinescu, M. E. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.581732 · Cited by 28
Holland, S., & Roth, R. (2023) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-09-22-0189-fi · Cited by 26
The Kelch13 compartment contains highly divergent vesicle trafficking proteins in malaria parasites
Schmidt, S., Wichers-Misterek, J. S., Behrens, H. M., Birnbaum, J., Henshall, I. G., Dröge, J., Jonscher, E., Flemming, S., Castro-Peña, C., Mesén-Ramírez, P., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011814 · Cited by 23
Cell-surface glycosaminoglycans regulate the cellular uptake of charged polystyrene nanoparticles
Olivieri, P. H., de Jesus, M. B., Nader, H. B., Justo, G. Z., & Sousa, A. A. (2022) · Nanoscale · doi:10.1039/d1nr07279j · Cited by 22
Guo, H., Zhou, C. X., Zheng, M., Zhang, J., Wu, H., He, Q., Ding, L., & Yang, B. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107084 · Cited by 23
Anesthesia triggers drug delivery to experimental glioma in mice by hijacking caveolar transport
Spieth, L., Berghoff, S. A., Stumpf, S. K., Winchenbach, J., Michaelis, T., Watanabe, T., Gerndt, N., Düking, T., Hofer, S., Ruhwedel, T., et al. (2021) · Neuro-Oncology Advances · doi:10.1093/noajnl/vdab140 · Cited by 22
Biophysics of endocytic vesicle formation: A focus on liquid–liquid phase separation
Lomoriello, I. S., Sigismund, S., & Day, K. J. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.02.002 · Cited by 22
LncR26319/miR-2834/ EndophilinaA xis Regulates Oogenesis of the Silkworm, Bombyx Mori
Wang, Y., Fu, Y., Cheng, H., Zhao, C., Huang, Q., Chang, M., Qiu, W., Shen, Y., & Li, D. (2022) · Insect Science · doi:10.1111/1744-7917.13082 · Cited by 22
The Role and Advancement of Liposomes for Oral Diseases Therapy
Rahma, M. N., Suhandi, C., Mohammed, A. S., El‐Rayyes, A., Elamin, K. M., Sulastri, E., & Wathoni, N. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s492353 · Cited by 19
Ether lipids influence cancer cell fate by modulating iron uptake
Mansell, R. P., Müller, S., Yang, J.-S., Innes-Gold, S. N., Das, S., Reinhardt, F., Sigmund, K., Phadnis, V. V., Wan, Z., Stark, J. R., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-68547-5 · Cited by 23
Zheng, B., Pan, F., Shi, M., He, C., He, B., Wang, R., Ren, G., Yang, S., & Zhang, S. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s462374 · Cited by 21
Wayt, J., Cartagena‐Rivera, A. X., Dutta, D., Donaldson, J. G., & Waterman, C. M. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-07-0480 · Cited by 17
Kesharwani, A., Schwarz, K., Dembla, E., Dembla, M., & Schmitz, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910789 · Cited by 16
Endocytic trafficking of GAS6–AXL complexes is associated with sustained AKT activation
Poświata, A., Kozik, K., Miączyńska, M., & Zdżalik-Bielecka, D. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04312-3 · Cited by 17
Endomembranes: Unsung Heroes of Mechanobiology?
Phuyal, S., & Baschieri, F. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.597721 · Cited by 15
Endophilin-A2 dependent tubular endocytosis promotes plasma membrane repair and parasite invasion
Corrotte, M., Cerasoli, M., Maeda, F. Y., & Andrews, N. W. (2020) · Journal of Cell Science · doi:10.1242/jcs.249524 · Cited by 16
Ubiquitin and its relatives as wizards of the endolysosomal system
Berlin, I., Sapmaz, A., Stévenin, V., & Neefjes, J. (2023) · Journal of Cell Science · doi:10.1242/jcs.260101 · Cited by 13
Kryvenko, V., & Vadász, I. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1360370 · Cited by 16
Zhang, Y., Zhu, J., Xu, H., Qin, Y., Yan, L., Ye, L., Zhang, X., Xie, M., & Tan, B. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.674995 · Cited by 14
Signaling Pathways that Regulate Macropinocytosis in Mammalian Cells
Palm, W. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-94004-1_8 · Cited by 16
Hook, J. L., & Bhattacharya, J. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1328453 · Cited by 18
Chu, Y., Chen, M. J., Yeh, C., & Lai, M.-W. (2024) · Journal of Biomedical Science · doi:10.1186/s12929-024-01063-0 · Cited by 15
The roles of dynein and myosin VI motor proteins in endocytosis
Mayya, C., Hema Naveena, A., Sinha, P., Wunder, C., Johannes, L., & Bhatia, D. D. (2022) · Journal of Cell Science · doi:10.1242/jcs.259387 · Cited by 16
Sposini, S., Rosendale, M., Claverie, L., Van, T. N. N., Jullié, D., & Perrais, D. (2020) · Nature Protocols · doi:10.1038/s41596-020-0371-z · Cited by 17
N‐BAR and F‐BAR proteins—endophilin‐A3 and PSTPIP1—control clathrin‐independent endocytosis of L1CAM
Lemaigre, C., Ceuppens, A., Valades‐Cruz, C. A., Ledoux, B., Vanbeneden, B., Hassan, M., Zetterberg, F. R., Nilsson, U. J., Johannes, L., Wunder, C., et al. (2023) · Traffic · doi:10.1111/tra.12883 · Cited by 12
Li, S., Wang, D., He, J., Liao, C., Zuo, Z., Li, S., & Niu, X. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.70002 · Cited by 12
Hemifusomes and interacting proteolipid nanodroplets mediate multi-vesicular body formation
Tavakoli, A., Hu, S., Ebrahim, S., & Kachar, B. (2025) · Nature Communications · doi:10.1038/s41467-025-59887-9 · Cited by 12
Efficacy of Chitosan-N-Arginine Chitosomes in mRNA Delivery and Cell Viability Enhancement
Garcia, B. B. M., Douka, S., Mertins, O., Mastrobattista, E., & Han, S. W. (2024) · ACS Applied Bio Materials · doi:10.1021/acsabm.4c00983 · Cited by 11
Giangreco, G., Malabarba, M. G., & Sigismund, S. (2020) · Biology of the Cell · doi:10.1111/boc.202000129 · Cited by 13
Recent advances in the intracellular delivery of macromolecule therapeutics
Chen, S., Xu, X., Li, X., Yi, N.-B., Li, S., Xiang, X.-C., Cheng, D., & Sun, T. (2022) · Biomaterials Science · doi:10.1039/d2bm01348g · Cited by 10
Actin-membrane linkers: Insights from synthetic reconstituted systems
Tsai, F., Guérin, G., Pernier, J., & Bassereau, P. M. (2024) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2024.151402 · Cited by 10
Mandal, T., Biswas, A., Ghosh, T., Manikandan, S. K., Kundu, A., Banerjee, A., Mitra, D., & Sinha, B. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05072-4 · Cited by 8
Putar, D., Čizmar, A., Chao, X., Šimić, M., Šoštar, M., Ćutić, T., Mijanović, L., Smolko, A., Tu, H., Cosson, P., et al. (2024) · Open Biology · doi:10.1098/rsob.230372 · Cited by 8
Li, T., Xu, B., Li, W., Cheng, X., TanTai, W., Zheng, H., Zhao, L., Li, N., & Han, C. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107096 · Cited by 8
Endo, A., Komada, M., & Yoshida, Y. (2024) · BioEssays · doi:10.1002/bies.202400127 · Cited by 7
Hema Naveena, A., & Bhatia, D. D. (2023) · ChemBioChem · doi:10.1002/cbic.202300506 · Cited by 7
Evaluating Cell Membrane Localization and Intracellular Transport of Proteins by Biotinylation
Reyes-Alvarez, E., Walker, T. J., & Mulligan, L. M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2376-3_15 · Cited by 7
Aptamers and endocytosis: The path into tumor cells
Dzarieva, F., Pavlova, S., Pavlova, G. V., & Fab, L. V. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152960 · Cited by 6
Vasti, C., ́Alessandro, L. D., Bedoya, D. A., Valenti, L. E., & Giacomelli, C. E. (2025) · Hybrid Advances · doi:10.1016/j.hybadv.2025.100586 · Cited by 8
Li, T., Meng, H., Huang, X., Qin, Y., Sheng, S., Jiang, Y., & Ren, F. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5c03687 · Cited by 6
CYRI proteins: controllers of actin dynamics in the cellular ‘eat vs walk’ decision
Machesky, L. M. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221354 · Cited by 6
Dynein functions in galectin-3 mediated processes of clathrin-independent endocytosis
Mayya, C., Hema Naveena, A., Sinha, P., & Bhatia, D. D. (2024) · Journal of Biosciences · doi:10.1007/s12038-024-00432-z · Cited by 6
Dynamin independent endocytosis is an alternative cell entry mechanism for multiple animal viruses
Ojha, R., Jiang, A., Mäntylä, E., Quirin, T., Modhiran, N., Witte, R., Gaudin, A., Zanetti, L. D., Gormal, R. S., Vihinen‐Ranta, M., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012690 · Cited by 7
Roles of myosin 1e and the actin cytoskeleton in kidney functions and familial kidney disease
Liu, P., Sayeeda, K., Zhuang, C., & Krendel, M. (2024) · Cytoskeleton · doi:10.1002/cm.21861 · Cited by 5
STED Imaging of Vesicular Endocytosis in the Synapse
Hu, S., Xie, Z., Wang, B., Chen, Y., Jing, Z., Hao, Y., Yao, J., Wu, X., Huo, J., Wei, A., et al. (2024) · Neuroscience Bulletin · doi:10.1007/s12264-024-01254-7 · Cited by 5
Fei, J., Zheng, Y., LaLonde, C., Tao, Y., & Zhou, R. (2026) · Science Advances · doi:10.1126/sciadv.aeb0803 · Cited by 8
Subasic, C. N., Butcher, N. J., Simpson, F., Minchin, R. F., & Kaminskas, L. M. (2023) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c00102 · Cited by 4
From molecular mechanisms of glycosphingolipid function to bio-therapeutic applications
Saha, A., & Johannes, L. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06186-1 · Cited by 3
Guo, L., Sun, L., & Li, C. (2025) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2025.110387 · Cited by 3
Schmidt, S., Wichers-Misterek, J. S., Behrens, H. M., Birnbaum, J., Henshall, I. G., Dröge, J., Jonscher, E., Flemming, S., Castro-Peña, C., Mesén-Ramírez, P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.15.520209 · Cited by 3
Alfandari, D., Rosenhek‐Goldian, I., Kozela, E., Nevo, R., Senprún, M. B., Moisieiev, A. I., Sogauker, N., Azuri, I., Gelman, S., Kiper, E., et al. (2025) · ACS Nano · doi:10.1021/acsnano.4c07503 · Cited by 2
IFITM2 Modulates Endocytosis Maintaining Neural Stem Cells in Developing Neocortex
Lv, Y., Zou, W., Li, L., Zhang, S., Liang, J., Pu, J., & Jiao, J. (2025) · Advanced Science · doi:10.1002/advs.202501593 · Cited by 2
Sharma, P., Tanwar, M., Choudhary, E., Sundaram, N. M., Ojha, D., Mishra, L., Nain, M., Rode, A. B., Prasad, V. M., Vrati, S., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013790 · Cited by 2
Moraes-Lacerda, T., Garcia-Fóssa, F., & de Jesus, M. B. (2024) · Nanotechnology · doi:10.1088/1361-6528/ad4556 · Cited by 2
Kopach, O., Sindeeva, O. A., Zheng, K., McGowan, E., Sukhorukov, G. B., & Rusakov, D. A. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.101493 · Cited by 2
Galectin-3 Mediated Endocytosis of the Orphan G-Protein-Coupled Receptor GPRC5A
Boucheham, A., Franco, J. M., Bär, S., MacDonald, E., Zuttion, S., Blagec, L., Rinaldi, B., Chicher, J., Kühn, L., Hammann, P., et al. (2025) · Cells · doi:10.3390/cells14191571 · Cited by 2
Advances in vesicle trafficking of membrane proteins and their regulatory mechanisms
Xu, C., Qian, H., Luo, P., Yu, M., Xing, J., Zhang, L. N., Zhang, X., Cui, Y., & Lin, J. (2022) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2022-0968 · Cited by 2
Caveolin-1-dependent regulation of cell-matrix interphase in 3D collagen gels
Mazumdar, D., Kataria, S., Panda, G. P., Kulkarni, A., Patil, S., Dash, M., & Balasubramanian, N. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.11.015 · Cited by 1
Wang, T., & Osawa, S. (2025) · Macromolecular Materials and Engineering · doi:10.1002/mame.202500319 · Cited by 1
Enzyme-Loaded Microcapsules as Intracellular Organelles for the Degradation of Nanoplastics by Cells
Liu, X., Chow, J., Wang, W., Dierkes, R. F., Feliu, N., Schulz, F., Streit, W. R., & Parak, W. J. (2025) · ACS Nano · doi:10.1021/acsnano.5c15213 · Cited by 1
Zhang, Y., Wang, C., Zhou, B., Verma, P., Hamera, S., & Zeng, L. (2026) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-02-26-0015-r · Cited by 1
Protein Modifications for Cellular Protein Delivery
Arafiles, J. V. V., Franke, J., Dubatouka, P., Franz, L., & Hackenberger, C. P. R. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.6c00267 · Cited by 2
Decoding the uptake pathway of nanoparticles in tumor cells: mechanisms, developments and challenges
Chen, Z., Zhou, L., Li, S., & Zhang, X. (2026) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2026.104054 · Cited by 1
Early Circulating Edema Factor in Inhalational Anthrax Infection: Does It Matter?
Tessier, E., Cheutin, L., Garnier, A., Vigne, C., Tournier, J., & Rougeaux, C. (2024) · Microorganisms · doi:10.3390/microorganisms12020308 · Cited by 1
Metadata
- Authors
- Thottacherry, J. J., Sathe, M., Prabhakara, C., & Mayor, S.
- Affiliations
- Tata Institute of Fundamental Research (IN)
- Corresponding author
- Mayor, Satyajit
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2019-10-06
- Volume
- 35
- Issue
- 1
- Pages
- 55-84
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- PMC
- PMC6917507
- OpenAlex
- W2956919478
- Cited by
- 122
- References
- 232
- Citations by year
- 2026: 15 · 2025: 19 · 2024: 22 · 2023: 16 · 2022: 17 · 2021: 21 · 2020: 12
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- endocytosis, clathrin-independent endocytosis, clathrin-mediated endocytosis, cell surface, membrane tension, signal transduction regulation
- MeSH terms
- Animals, Cell Membrane, Endocytosis, Biological Evolution, Homeostasis, Humans, Signal Transduction
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
