ATG9A protects the plasma membrane from programmed and incidental permeabilization
Open accessAbstract
The integral membrane protein ATG9A plays a key role in autophagy. It displays a broad intracellular distribution and is present in numerous compartments, including the plasma membrane (PM). The reasons for the distribution of ATG9A to the PM and its role at the PM are not understood. Here, we show that ATG9A organizes, in concert with IQGAP1, components of the ESCRT system and uncover cooperation between ATG9A, IQGAP1 and ESCRTs in protection from PM damage. ESCRTs and ATG9A phenocopied each other in protection against PM injury. ATG9A knockouts sensitized the PM to permeabilization by a broad spectrum of microbial and endogenous agents, including gasdermin, MLKL and the MLKL-like action of coronavirus ORF3a. Thus, ATG9A engages IQGAP1 and the ESCRT system to maintain PM integrity. Claude-Taupin et al. show that ATG9A mediates protection against plasma membrane damage in diverse biological contexts through a mechanism involving IQGAP1 and ESCRTs.
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ATG9A, together with IQGAP1 and ESCRT proteins, protects against plasma membrane damage.
“Together with IQGAP1 and ESCRT proteins, ATG9A has further been shown to protect against plasma membrane damage [52].”
From miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A (2026) · cites this paper as [52]
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Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y., Cai, T., Wang, F., & Shao, F. (2015) · Nature · doi:10.1038/nature15514 · Cited by 6,659 · see citing works
Self-citationImproved vectors and genome-wide libraries for CRISPR screening
Sanjana, N. E., Shalem, O., & Zhang, F. (2014) · Nature Methods · doi:10.1038/nmeth.3047 · Cited by 5,239 · see citing works
Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686 · see citing works
Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
Liu, X., Zhang, Z., Ruan, J., Pan, Y., Magupalli, V. G., Wu, H., & Lieberman, J. (2016) · Nature · doi:10.1038/nature18629 · Cited by 3,202 · see citing works
Biological Functions of Autophagy Genes: A Disease Perspective
Levine, B., & Kroemer, G. (2019) · Cell · doi:10.1016/j.cell.2018.09.048 · Cited by 2,832 · see citing works
Pore-forming activity and structural autoinhibition of the gasdermin family
Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D.-C., & Shao, F. (2016) · Nature · doi:10.1038/nature18590 · Cited by 2,771 · see citing works
Gutierrez, M. G., Master, S. S., Singh, S. B., Taylor, G. A., Colombo, M. I., & Deretic, V. (2004) · Cell · doi:10.1016/j.cell.2004.11.038 · Cited by 2,252 · see citing works
Self-citationNecroptosis and its role in inflammation
Pasparakis, M., & Vandenabeele, P. (2015) · Nature · doi:10.1038/nature14191 · Cited by 2,148 · see citing works
The gasdermins, a protein family executing cell death and inflammation
Broz, P., Pelegrín, P., & Shao, F. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-019-0228-2 · Cited by 1,641 · see citing works
Wang, H., Sun, L., Su, L., Rizo, J., Liu, L., Wang, L., Wang, F., & Wang, X. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.003 · Cited by 1,564 · see citing works
Self-citationDirected evolution of APEX2 for electron microscopy and proximity labeling
Lam, S. S., Martell, J. D., Kamer, K. J., Deerinck, T. J., Ellisman, M. H., Mootha, V. K., & Ting, A. Y. (2014) · Nature Methods · doi:10.1038/nmeth.3179 · Cited by 1,404 · see citing works
Nuclear envelope rupture and repair during cancer cell migration
Denais, C. M., Gilbert, R. M., Isermann, P., McGregor, A. L., te Lindert, M., Weigelin, B., Davidson, P. M., Friedl, P., Wolf, K., & Lammerding, J. (2016) · Science · doi:10.1126/science.aad7297 · Cited by 1,318 · see citing works
Mizushima, N., & Levine, B. (2020) · New England Journal of Medicine · doi:10.1056/nejmra2022774 · Cited by 1,140 · see citing works
Necroptosis in development, inflammation and disease
Weinlich, R., Oberst, A., Beere, H. M., & Green, D. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.149 · Cited by 1,016 · see citing works
Autophagy-Independent Functions of the Autophagy Machinery
Galluzzi, L., & Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.05.026 · Cited by 863 · see citing works
Autophagy in inflammation, infection, and immunometabolism
Deretic, V. (2021) · Immunity · doi:10.1016/j.immuni.2021.01.018 · Cited by 862 · see citing works
Self-citationStarvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
Young, A. R. J., Chan, E. Y. W., Hu, X. W., Köchl, R., Crawshaw, S. G., High, S., Hailey, D. W., Lippincott-Schwartz, J., & Tooze, S. A. (2006) · Journal of Cell Science · doi:10.1242/jcs.03172 · Cited by 815 · see citing works
Self-citationESCRT-dependent membrane repair negatively regulates pyroptosis downstream of GSDMD activation
Rühl, S., Shkarina, K., Demarco, B., Heilig, R., Santos, J. C., & Brož, P. (2018) · Science · doi:10.1126/science.aar7607 · Cited by 740 · see citing works
Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
Morita, E., Sandrin, V., Chung, H., Morham, S. G., Gygi, S. P., Rodesch, C. K., & Sundquist, W. I. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601850 · Cited by 724 · see citing works
ESCRT-III Acts Downstream of MLKL to Regulate Necroptotic Cell Death and Its Consequences
Gong, Y.-N., Guy, C., Olauson, H., Becker, J. U., Yang, M., Fitzgerald, P., Linkermann, A., & Green, D. R. (2017) · Cell · doi:10.1016/j.cell.2017.03.020 · Cited by 689 · see citing works
Hurley, J. H. (2015) · The EMBO Journal · doi:10.15252/embj.201592484 · Cited by 668 · see citing works
ESCRT Machinery Is Required for Plasma Membrane Repair
Jiménez, A. J., Maiuri, P., Lafaurie-Janvore, J., Divoux, S., Piel, M., & Perez, F. (2014) · Science · doi:10.1126/science.1247136 · Cited by 656 · see citing works
β-Coronaviruses Use Lysosomes for Egress Instead of the Biosynthetic Secretory Pathway
Ghosh, S., Dellibovi-Ragheb, T. A., Kerviel, A., Pak, E., Qiu, Q., Fisher, M., Takvorian, P. M., Bleck, C. K. E., Hsu, V. W., Fehr, A. R., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.039 · Cited by 615 · see citing works
A fluorescent membrane tension probe
Colom, A., Derivery, E., Soleimanpour, S., Tomba, C., Molin, M. D., Sakai, N., González‐Gaitán, M., Matile, S., & Roux, A. (2018) · Nature Chemistry · doi:10.1038/s41557-018-0127-3 · Cited by 579 · see citing works
Orsi, A., Razi, M., Dooley, H. C., Robinson, D. J., Weston, A., Collinson, L., & Tooze, S. A. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0746 · Cited by 570 · see citing works
Self-citationATG2 transports lipids to promote autophagosome biogenesis
Valverde, D. P., Yu, S., Boggavarapu, V., Kumar, N., Lees, J. A., Walz, T., Reinisch, K. M., & Melia, T. J. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201811139 · Cited by 537 · see citing works
Fast, single-molecule localization that achieves theoretically minimum uncertainty
Smith, C., Joseph, N., Rieger, B., & Lidke, K. A. (2010) · Nature Methods · doi:10.1038/nmeth.1449 · Cited by 523 · see citing works
Self-citationCellular Functions and Molecular Mechanisms of the ESCRT Membrane-Scission Machinery
Christ, L., Raiborg, C., Wenzel, E. M., Campsteijn, C., & Stenmark, H. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.016 · Cited by 456 · see citing works
Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion
Matoba, K., Kotani, T., Tsutsumi, A., Tsuji, T., Mori, T., Noshiro, D., Sugita, Y., Nomura, N., Iwata, S., Ohsumi, Y., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00518-w · Cited by 430 · see citing works
Repair of injured plasma membrane by rapid Ca2+-dependent endocytosis
Idone, V. J., Tam, C. C., Goss, J. A., Toomre, D. K., Pypaert, M., & Andrews, N. W. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708010 · Cited by 429 · see citing works
Diverse Autophagosome Membrane Sources Coalesce in Recycling Endosomes
Puri, C., Renna, M., Bento, C. F., Moreau, K., & Rubinsztein, D. C. (2013) · Cell · doi:10.1016/j.cell.2013.08.044 · Cited by 423 · see citing works
TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes
Longatti, A., Lamb, C. A., Razi, M., Yoshimura, S., Barr, F. A., & Tooze, S. A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201111079 · Cited by 386 · see citing works
Self-citationHart, M. J., Callow, M. G., Souza, B., & Polakis, P. G. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00663.x · Cited by 384 · see citing works
Unique role for ATG5 in neutrophil-mediated immunopathology during M. tuberculosis infection
Kimmey, J. M., Huynh, J. P., Weiss, L. A., Park, S., Kambal, A., Debnath, J., Virgin, H. W., & Stallings, C. L. (2015) · Nature · doi:10.1038/nature16451 · Cited by 382 · see citing works
Diverse Cellular Roles of Autophagy
Morishita, H., & Mizushima, N. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125300 · Cited by 376 · see citing works
IQGAP1: a key regulator of adhesion and migration
Noritake, J., Watanabe, T., Sato, K., Wang, S., & Kaibuchi, K. (2005) · Journal of Cell Science · doi:10.1242/jcs.02379 · Cited by 368 · see citing works
Mycobacterium tuberculosis evades macrophage defenses by inhibiting plasma membrane repair
Divangahi, M., Chen, M., Gan, H., Desjardins, D., Hickman, T. T., Lee, D. M., Fortune, S. M., Behar, S. M., & Remold, H. G. (2009) · Nature Immunology · doi:10.1038/ni.1758 · Cited by 363 · see citing works
Autophagosome maturation: An epic journey from the ER to lysosomes
Zhao, Y. G., & Zhang, H. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201810099 · Cited by 362 · see citing works
Mechanism of Ca2+-triggered ESCRT assembly and regulation of cell membrane repair
Scheffer, L., Sreetama, S. C., Sharma, N., Medikayala, S., Brown, K. J., Defour, A., & Jaiswal, J. K. (2014) · Nature Communications · doi:10.1038/ncomms6646 · Cited by 358 · see citing works
The autophagic membrane tether ATG2A transfers lipids between membranes
Maeda, S., Otomo, C., & Otomo, T. (2019) · eLife · doi:10.7554/elife.45777 · Cited by 336 · see citing works
Galli, T., Zahraoui, A., Vaidyanathan, V. V., Raposo, G., Tian, J. M., Karin, M., Niemann, H., & Louvard, D. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.6.1437 · Cited by 313 · see citing works
Simultaneous multiple-emitter fitting for single molecule super-resolution imaging
Huang, F., Schwartz, S. L., Byars, J. M., & Lidke, K. A. (2011) · Biomedical Optics Express · doi:10.1364/boe.2.001377 · Cited by 312 · see citing works
Self-citationAutophagy initiation by ULK complex assembly on ER tubulovesicular regions marked by ATG9 vesicles
Karanasios, E., Walker, S. A., Okkenhaug, H., Manifava, M., Hummel, E., Zimmermann, H., Ahmed, Q., Domart, M., Collinson, L., & Ktistakis, N. T. (2016) · Nature Communications · doi:10.1038/ncomms12420 · Cited by 308 · see citing works
Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy
Yamano, K., Fogel, A. I., Wang, C., van der Bliek, A. M., & Youle, R. J. (2014) · eLife · doi:10.7554/elife.01612 · Cited by 307 · see citing works
Structure, lipid scrambling activity and role in autophagosome formation of ATG9A
Maeda, S., Yamamoto, H., Kinch, L. N., Garza, C. M., Takahashi, S., Otomo, C., Grishin, N. V., Forli, S., Mizushima, N., & Otomo, T. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00520-2 · Cited by 305 · see citing works
Galectins Control mTOR in Response to Endomembrane Damage
Jia, J., Abudu, Y. P., Claude‐Taupin, A., Gu, Y., Kumar, S. G., Choi, S. W., Peters, R. S., Mudd, M. H., Allers, L., Salemi, M., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.009 · Cited by 288 · see citing works
Self-citationWatch What You (Self-) Eat: Autophagic Mechanisms that Modulate Metabolism
Lahiri, V., Hawkins, W. D., & Klionsky, D. J. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.03.003 · Cited by 286 · see citing works
Beckwith, K. S., Beckwith, M. S., Ullmann, S., Sætra, R. S., Kim, H., Marstad, A., Åsberg, S. E., Strand, T. A., Haug, M., Niederweis, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16143-6 · Cited by 282 · see citing works
Atg9 establishes Atg2-dependent contact sites between the endoplasmic reticulum and phagophores
Gómez‐Sánchez, R., Rose, J., Guimarães, R. S., Mari, M. C., Papinski, D., Rieter, E., Geerts, W. J. C., Hardenberg, R., Kraft, C., Ungermann, C., et al. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201710116 · Cited by 271 · see citing works
Self-citationBrill, S., Li, S., Lyman, C. W., Church, D. M., Wasmuth, J. J., Weissbach, L., Bernards, A., & Snijders, A. J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4869 · Cited by 261 · see citing works
Sequential Engagement of Distinct MLKL Phosphatidylinositol-Binding Sites Executes Necroptosis
Quarato, G., Guy, C. S., Grace, C. R., Llambi, F., Nourse, A., Rodríguez, D. A., Wakefield, R., Frase, S., Moldoveanu, T., & Green, D. R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.011 · Cited by 242 · see citing works
The biology of IQGAP proteins: beyond the cytoskeleton
Hedman, A. C., Smith, J. M., & Sacks, D. B. (2015) · EMBO Reports · doi:10.15252/embr.201439834 · Cited by 240 · see citing works
SARS-Coronavirus Open Reading Frame-3a drives multimodal necrotic cell death
Yue, Y., Nabar, N. R., Shi, C.-S., Kamenyeva, O., Xiao, X., Hwang, I., Wang, M., & Kehrl, J. H. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0917-y · Cited by 228 · see citing works
IQGAP1 Promotes Cell Motility and Invasion
Mataraza, J., Briggs, M. W., Li, Z., Entwistle, A., Ridley, A. J., & Sacks, D. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304838200 · Cited by 205 · see citing works
ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ
Judith, D., Jefferies, H. B. J., Boeing, S., Frith, D., Snijders, A. P., & Tooze, S. A. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201901115 · Cited by 204 · see citing works
Self-citationZhou, C., Ma, K., Gao, R., Mu, C., Chen, L., Liu, Q., Luo, Q., Feng, D., Zhu, Y., & Chen, Q. (2016) · Cell Research · doi:10.1038/cr.2016.146 · Cited by 202 · see citing works
IQGAP1 Integrates Ca2+/Calmodulin and Cdc42 Signaling
Ho, Y.-D., Joyal, J. L., Li, Z., & Sacks, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.464 · Cited by 197 · see citing works
Electron microscopy using the genetically encoded APEX2 tag in cultured mammalian cells
Martell, J. D., Deerinck, T. J., Lam, S. S., Ellisman, M. H., & Ting, A. Y. (2017) · Nature Protocols · doi:10.1038/nprot.2017.065 · Cited by 190 · see citing works
IQGAP1 Integrates Ca2+/Calmodulin and B-Raf Signaling
Ren, J.-G., Li, Z., & Sacks, D. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804626200 · Cited by 188 · see citing works
TBC1D5 and the AP2 complex regulate ATG9 trafficking and initiation of autophagy
Popovic, D., & Đikić, I. (2014) · EMBO Reports · doi:10.1002/embr.201337995 · Cited by 166 · see citing works
Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery
Guardia, C. M., Tan, X.-F., Lian, T., Rana, M. S., Zhou, W., Christenson, E. T., Lowry, A. J., Faraldo-Gómez, J. D., Bonifacino, J. S., Jiang, J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107837 · Cited by 163 · see citing works
AP-4 mediates export of ATG9A from the trans -Golgi network to promote autophagosome formation
Mattera, R., Park, S. Y., Pace, R. D., Guardia, C. M. A., & Bonifacino, J. S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717327114 · Cited by 162 · see citing works
Calmodulin Modulates the Interaction between IQGAP1 and Cdc42
Joyal, J. L., Annan, R. S., Ho, Y.-D., Huddleston, M. E., Carr, S. A., Hart, M. J., & Sacks, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.24.15419 · Cited by 141 · see citing works
Keyel, P. A., Loultcheva, L., Roth, R. A., Salter, R. D., Watkins, S. C., Yokoyama, W. M., & Heuser, J. E. (2011) · Journal of Cell Science · doi:10.1242/jcs.076182 · Cited by 133 · see citing works
The ESCRT-machinery: closing holes and expanding roles
Gatta, A. T., & Carlton, J. G. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.04.005 · Cited by 126 · see citing works
<i>Atg9a</i> deficiency causes axon-specific lesions including neuronal circuit dysgenesis
Yamaguchi, J., Suzuki, C., Nanao, T., Kakuta, S., Ozawa, K., Tanida, I., Saitoh, T., Sunabori, T., Komatsu, M., Tanaka, K., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1314897 · Cited by 109 · see citing works
Self-citationSmall GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation
Kakuta, S., Yamaguchi, J., Suzuki, C., Sasaki, M., Kazuno, S., & Uchiyama, Y. (2017) · The FASEB Journal · doi:10.1096/fj.201601052r · Cited by 74 · see citing works
Self-citationSequential Superresolution Imaging of Multiple Targets Using a Single Fluorophore
Valley, C. C., Liu, S., Lidke, D. S., & Lidke, K. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123941 · Cited by 64 · see citing works
Self-citationZhou, X., Cong, Y., Veenendaal, T., Klumperman, J., Shi, D., Mari, M. C., & Reggiori, F. (2017) · Viruses · doi:10.3390/v9090251 · Cited by 40 · see citing works
Self-citationDynamic Remodeling of the Host Cell Membrane by Virulent Mycobacterial Sulfoglycolipid-1
Mishra, M., Adhyapak, P., Dadhich, R., & Kapoor, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-49343-2 · Cited by 38 · see citing works
A Plasma Membrane Wound Proteome
Mellgren, R. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110015 · Cited by 34 · see citing works
Atcheson, E., Hamilton, E., Pathmanathan, S., Greer, B., Harriott, P., & Timson, D. J. (2011) · Bioscience Reports · doi:10.1042/bsr20100123 · Cited by 33 · see citing works
Claude‐Taupin, A., Fonderflick, L., Gauthier, T., Mansi, L., Pallandre, J., Borg, C., Perez, V., Monnien, F., Algros, M., Vigneron, M., et al. (2018) · Cells · doi:10.3390/cells7120248 · Cited by 30 · see citing works
Self-citationSequential super-resolution imaging using DNA strand displacement
Lidke, D. S., Martin, C., Farzam, F., Edwards, J. S., Pallikkuth, S., Lakin, M. R., & Lidke, K. A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0203291 · Cited by 19 · see citing works
Self-citationA new twist on plasma membrane repair
Mellgren, R. L. (2011) · Communicative & Integrative Biology · doi:10.4161/cib.4.2.14384 · Cited by 11 · see citing works
Flagged first, then by citations
1 of the 76 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Autophagy genes in biology and disease
Yamamoto, H., Zhang, S., & Mizushima, N. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-022-00562-w · Cited by 631 · see citing works
The autophagy protein ATG9A enables lipid mobilization from lipid droplets
Mailler, É., Guardia, C. M. A., Bai, X., Jarník, M., Williamson, C. D., Li, Y., Maio, N., Golden, A., & Bonifacino, J. S. (2021) · Nature Communications · doi:10.1038/s41467-021-26999-x · Cited by 123 · see citing works
ATG9 vesicles comprise the seed membrane of mammalian autophagosomes
Olivas, T. J., Wu, Y., Yu, S., Luan, L., Choi, P., Guinn, E. D., Nag, S., Camilli, P. V. D., Gupta, K., & Melia, T. J. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202208088 · Cited by 108 · see citing works
Stress granules and mTOR are regulated by membrane atg8ylation during lysosomal damage
Jia, J., Wang, F., Bhujabal, Z., Peters, R. S., Mudd, M. H., Duque, T. L. A., Allers, L., Javed, R., Salemi, M., Behrends, C., et al. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202207091 · Cited by 100 · see citing works
Self-citationMammalian hybrid pre-autophagosomal structure HyPAS generates autophagosomes
Kumar, S. G., Javed, R., Mudd, M. H., Pallikkuth, S., Lidke, K. A., Jain, A., Tangavelou, K., Gudmundsson, S. R., Ye, C., Rusten, T. E., et al. (2021) · Cell · doi:10.1016/j.cell.2021.10.017 · Cited by 98 · see citing works
Self-citationTurning cold tumors into hot tumors to ignite immunotherapy
Liu, Y., Wang, Y., Wang, S., Li, J., He, W. A., Fan, X.-J., & Wan, X. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02477-6 · Cited by 107 · see citing works
Autophagy in muscle regeneration: potential therapies for myopathies
Chen, W., Chen, Y., Liu, Y., & Wang, X. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13000 · Cited by 77 · see citing works
A guide to membrane atg8ylation and autophagy with reflections on immunity
Deretic, V. P., & Lazarou, M. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202203083 · Cited by 78 · see citing works
Self-citationFluorescent Flippers: Small‐Molecule Probes to Image Membrane Tension in Living Systems
Chen, X., Bayard, F., Gonzalez‐Sanchis, N., Pamungkas, K. K. P., Sakai, N., & Matile, S. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202217868 · Cited by 68 · see citing works
Structural basis for ATG9A recruitment to the ULK1 complex in mitophagy initiation
Ren, X., Nguyen, T. N., Lam, W. K., Buffalo, C. Z., Lazarou, M., Yokom, A. L., & Hurley, J. H. (2023) · Science Advances · doi:10.1126/sciadv.adg2997 · Cited by 68 · see citing works
Atg8ylation as a general membrane stress and remodeling response
Kumar, S. G., Jia, J., & Deretic, V. P. (2021) · Cell Stress · doi:10.15698/cst2021.09.255 · Cited by 63 · see citing works
Self-citationAutophagy-dependent versus autophagy-independent ferroptosis
Zhu, Y., Fujimaki, M., & Rubinsztein, D. C. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.01.005 · Cited by 63 · see citing works
Melia, T. J., & Reinisch, K. M. (2022) · Journal of Cell Science · doi:10.1242/jcs.259357 · Cited by 61 · see citing works
The Role of ATG9 Vesicles in Autophagosome Biogenesis
Holzer, E., Martens, S., & Tulli, S. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168489 · Cited by 56 · see citing works
Wang, F., Peters, R. S., Jia, J., Mudd, M. H., Salemi, M., Allers, L., Javed, R., Duque, T. L. A., Paddar, M. A., Trosdal, E. S., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.03.014 · Cited by 51 · see citing works
Self-citationThe expanding repertoire of ESCRT functions in cell biology and disease
Hurley, J. H., Coyne, A. N., Miączyńska, M., & Stenmark, H. (2025) · Nature · doi:10.1038/s41586-025-08950-y · Cited by 62 · see citing works
Ramirez, S. C., Gómez‐Sánchez, R., Verlhac, P., Hardenberg, R., Margheritis, E. G., Cosentino, K., Reggiori, F., & Ungermann, C. (2022) · Autophagy · doi:10.1080/15548627.2022.2136340 · Cited by 52 · see citing works
Self-citationPark, D., Wu, Y., Wang, X., Gowrishankar, S., Baublis, A., & Camilli, P. V. D. (2023) · Nature Communications · doi:10.1038/s41467-023-36081-3 · Cited by 53 · see citing works
AP-4-mediated axonal transport controls endocannabinoid production in neurons
Davies, A. K., Alecu, J. E., Ziegler, M., Vasilopoulou, C. G., Merciai, F., Jumo, H., Saber, W. A., Şahin, M., Ebrahimi‐Fakhari, D., & Borner, G. H. H. (2022) · Nature Communications · doi:10.1038/s41467-022-28609-w · Cited by 51 · see citing works
Mammalian ATG8 proteins maintain autophagosomal membrane integrity through ESCRTs
Javed, R., Jain, A., Duque, T. L. A., Hendrix, E., Paddar, M. A., Khan, S. A., Claude‐Taupin, A., Jia, J., Allers, L., Wang, F., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112845 · Cited by 53 · see citing works
Self-citationLipid Dynamics at Membrane Contact Sites
Reinisch, K. M., Camilli, P. V. D., & Melia, T. J. (2025) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-083024-122821 · Cited by 51 · see citing works
ATG9A prevents TNF cytotoxicity by an unconventional lysosomal targeting pathway
Huyghe, J., Priem, D., Hove, L. V., Gilbert, B., Fritsch, J. H., Uchiyama, Y., Hoste, E., Loo, G., & Bertrand, M. J. M. (2022) · Science · doi:10.1126/science.add6967 · Cited by 45 · see citing works
Self-citationGuo, Y., Cui, Y., Li, Y., Jin, X., Wang, D., Lei, M., Chen, F.-Z., Liu, Y., Xu, J., Yao, G., et al. (2023) · 癌症:英文版 · doi:10.1002/cac2.12417 · Cited by 42 · see citing works
SHIP164 is a chorein motif lipid transfer protein that controls endosome–Golgi membrane traffic
Hanna, M. G., Suen, P. H., Wu, Y., Reinisch, K. M., & De Camilli, P. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202111018 · Cited by 39 · see citing works
Liao, Y., Chen, X., Miller-Little, W. A., Wang, H., Willard, B. B., Bulek, K., Zhao, J., & Li, X. (2022) · The EMBO Journal · doi:10.15252/embj.2022110780 · Cited by 40 · see citing works
Zhen, W., Luo, T., Wang, Z., Jiang, X., Yuan, E., Weichselbaum, R. R., & Lin, W. (2023) · Small · doi:10.1002/smll.202305440 · Cited by 39 · see citing works
ATG9A and ARFIP2 cooperate to control PI4P levels for lysosomal repair
Tito, S. D., Almacellas, E., Yu, D. D., Millard, E., Zhang, W., de Heus, C., Queval, C. J., Hervás, J. H., Pellegrino, E., Panagi, I., et al. (2025) · Developmental Cell · doi:10.1016/j.devcel.2025.05.007 · Cited by 32 · see citing works
Self-citationChemically engineered antibodies for autophagy-based receptor degradation
Cheng, B., Li, M., Zheng, J., Liang, J., Li, Y., Liang, R., Tian, H., Zhou, Z., Ding, L., Ren, J., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-024-01803-1 · Cited by 31 · see citing works
Emerging roles of ATG9/ATG9A in autophagy: implications for cell and neurobiology
Choi, J., Jang, H., Xuan, Z., & Park, D. (2024) · Autophagy · doi:10.1080/15548627.2024.2384349 · Cited by 28 · see citing works
Nondegradable ubiquitinated ATG9A organizes Golgi integrity and dynamics upon stresses
Luo, Q., Liu, Q., Cheng, H., Wang, J., Zhao, T., Zhang, J., Mu, C., Meng, Y., Chen, L., Zhou, C., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111195 · Cited by 30 · see citing works
Liu, C., Wu, Z., Wang, L., Yang, Q., Huang, J., & Huang, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012123 · Cited by 30 · see citing works
Regulation of autophagy by SARS‐CoV‐2: The multifunctional contributions of ORF3a
Shariq, M., Malik, A. A., Sheikh, J. A., Hasnain, S. E., & Ehtesham, N. Z. (2023) · Journal of Medical Virology · doi:10.1002/jmv.28959 · Cited by 29 · see citing works
Exploring the ATG9A interactome uncovers interaction with VPS13A
van Vliet, A. R., Jefferies, H. B. J., Faull, P. A., Chadwick, J., Ibrahim, F., Skehel, M. J., & Tooze, S. A. (2024) · Journal of Cell Science · doi:10.1242/jcs.261081 · Cited by 29 · see citing works
Self-citationLysosomal Repair in Health and Disease
Xun, J., & Tan, J. X. (2025) · Journal of Cellular Physiology · doi:10.1002/jcp.70044 · Cited by 23 · see citing works
ATG9A facilitates the closure of mammalian autophagosomes
Javed, R., Mari, M. C., Trosdal, E. S., Duque, T. L. A., Paddar, M. A., Allers, L., Mudd, M. H., Claude‐Taupin, A., Akepati, P. R., Hendrix, E., et al. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202404047 · Cited by 22 · see citing works
Self-citationA chaperone-proteasome-based fragmentation machinery is essential for aggrephagy
Mauthe, M., van de Beek, N., Mari, M. C., Korsten, G., Nobari, P., Castelino, K. B., de Mattos, E. P., Ouhida, I., Dijkstra, J. L., Schipper-Krom, S., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01747-1 · Cited by 21 · see citing works
Self-citationVale-Costa, S., Etibor, T. A., Brás, D., Sousa, A. L., Ferreira, M., Martins, G. G., Mello, V. H., & Amorim, M. J. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002290 · Cited by 21 · see citing works
The autophagy protein ATG-9 regulates lysosome function and integrity.
Peng, K., Zhao, G., Zhao, H.-Y., Noda, N., & Zhang, H. (2025) · Journal of Cell Biology · doi:10.1083/jcb.202411092 · Cited by 17 · see citing works
ATG9 Not Just an Autophagy Related Protein
Millard, E., & Tooze, S. A. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169288 · Cited by 18 · see citing works
Self-citationChilds, E., Henry, C. M., Canton, J., & Sousa, C. R. E. (2021) · Open Biology · doi:10.1098/rsob.210194 · Cited by 17 · see citing works
Autophagy-independent role of ATG9A vesicles as carriers for galectin-9 secretion
Zhang, W., Ji, C., Li, X., He, T., Jiang, W., Liu, Y., Wu, M., Zhao, Y., Chen, X., Wang, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59605-5 · Cited by 15 · see citing works
Makar, A. N., Boraman, A., Mosen, P., Simpson, J. E., Júnior, J. G. M., Michelberger, T., Aitken, S., Wheeler, A. P., Winter, D., von Kriegsheim, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52049-3 · Cited by 14 · see citing works
Hu, G., Hauk, P. J., Zhang, N., Elsegeiny, W. A. W., Guardia, C. M. A., Kullas, A. L., Crosby, K., Deterding, R. R., Schedel, M., Reynolds, P. R., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2093028 · Cited by 12 · see citing works
Fluorescent Flippers: Small‐Molecule Probes to Image Membrane Tension in Living Systems
Chen, X., Bayard, F., Gonzalez‐Sanchis, N., Pamungkas, K. K. P., Sakai, N., & Matile, S. (2023) · Angewandte Chemie · doi:10.1002/ange.202217868 · Cited by 11 · see citing works
Propagation of neuronal micronuclei regulates microglial characteristics
Yano, S., Asami, N., Kishi, Y., Takeda, I., Kubotani, H., Hattori, Y., Kitazawa, A., Hayashi, K., Kubo, K., Saeki, M., et al. (2025) · Nature Neuroscience · doi:10.1038/s41593-024-01863-5 · Cited by 11 · see citing works
ATG9A vesicles are a subtype of intracellular nanovesicle
Fesenko, M., Moore, D. J., Ewbank, P., Courthold, E., & Royle, S. (2025) · Journal of Cell Science · doi:10.1242/jcs.263852 · Cited by 9 · see citing works
Biogenesis of omegasomes and autophagosomes in mammalian autophagy
Norell, P. N., Campisi, D., Mohan, J., & Wollert, T. (2024) · Biochemical Society Transactions · doi:10.1042/bst20240015 · Cited by 8 · see citing works
Lysosomal homeostasis at the crossroads of neurodegeneration
Tito, S. D., & Tooze, S. A. (2026) · Journal of Clinical Investigation · doi:10.1172/jci199845 · Cited by 7 · see citing works
Self-citationNoncanonical roles of ATG5 and membrane atg8ylation in retromer assembly and function
Paddar, M. A., Wang, F., Trosdal, E. S., Hendrix, E., He, Y. J., Salemi, M., Mudd, M. H., Jia, J., Duque, T. L. A., Javed, R., et al. (2025) · eLife · doi:10.7554/elife.100928.3 · Cited by 7 · see citing works
Self-citationmiRNA family miR-29 inhibits PINK1-PRKN dependent mitophagy via ATG9APreprint
Markham, B. N., Ramnarine, C., Kim, S., Grever, W. E., Soto‐Beasley, A. I., Heckman, M. G., Ren, Y., Osborne, A. C., Bhagwate, A. V., Liu, Y., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.17.576122 · Cited by 7 · see citing works
Exploitable mechanisms of antibody and CAR mediated macrophage cytotoxicity
Liu, T., Zhang, M., Farsh, T., Li, H., Kishishita, A., Barpanda, A., Leung, S. G., Zhu, J., Jung, H., Hua, J. T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60745-x · Cited by 6 · see citing works
Progress on multifunctional transmembrane protein ATG9A
Lin, X., Liang, L., Liao, S., Li, Y., & Zhou, Y. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02317-6 · Cited by 6 · see citing works
Atg8ylation as a host-protective mechanism against Mycobacterium tuberculosis
Deretic, V. P. (2023) · Frontiers in Tuberculosis · doi:10.3389/ftubr.2023.1275882 · Cited by 6 · see citing works
Self-citationATG9A and ARFIP2 cooperate to regulate PI4P levels for lysosomal repairPreprint
Tito, S. D., Almacellas, E., Yu, D. D., Zhang, W., Millard, E., Hervás, J. H., Pellegrino, E., Panagi, I., Fodge, D., Thurston, T. L. M., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.23.604321 · Cited by 6 · see citing works
Self-citationKhalko, R. K., Pandeya, A., Saxena, S., & Gosipatala, S. B. (2024) · International Reviews of Immunology · doi:10.1080/08830185.2023.2296488 · Cited by 4 · see citing works
Noncanonical roles of ATG5 and membrane atg8ylation in retromer assembly and functionPreprint
Paddar, M. A., Wang, F., Trosdal, E. S., Hendrix, E., He, Y. J., Salemi, M., Mudd, M. H., Jia, J., Duque, T. L. A., Javed, R., et al. (2024) · eLife · doi:10.7554/elife.100928 · Cited by 4 · see citing works
Self-citationBraun, S., Knackfuß, K., Ziesmann, T., Mlinzk, L., Goerg, A., Frankenheim, J., Walter, A., Schneider‐Brachert, W., Distler, U., & Fritsch, J. H. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02530-3 · Cited by 3 · see citing works
Thaprawat, P., Zhang, Z., Rentchler, E. C., Wang, F., Chalasani, S., Giuliano, C. J., Lourido, S., Cristina, M. D., Klionsky, D. J., & Carruthers, V. B. (2024) · Autophagy Reports · doi:10.1080/27694127.2024.2418256 · Cited by 3 · see citing works
Self-citationImaging ATG9A, a Multi-Spanning Membrane Protein
van Vliet, A. R., Tito, S. D., Almacellas, E., & Tooze, S. A. (2023) · Journal of Visualized Experiments · doi:10.3791/65349 · Cited by 3 · see citing works
Self-citationATG9A supports Chlamydia trachomatis infection via autophagy-independent mechanisms
Suzuki, M., Funakoshi, T., Kumagai, K., Komatsu, M., & Waguri, S. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.02774-23 · Cited by 3 · see citing works
Letter to Cell Death Pathways in Ischemic Stroke and Targeted Pharmacotherapy
Li, H., & Chen, G. (2021) · Translational Stroke Research · doi:10.1007/s12975-021-00965-7 · Cited by 3 · see citing works
Mechanisms of scramblases in regulating hepatic lipoprotein secretion and autophagy
Chen, A., Zhang, C., Ding, W., & Ni, H. (2026) · Journal of Lipid Research · doi:10.1016/j.jlr.2026.100979 · Cited by 2 · see citing works
ATG9A-mediated plasma membrane repair is linked to Vps13A and regulated by glycosylation
Muskat, N. H., Nevo-Yassaf, I., Chaurasia, M., Reiss, S., Goliand, I., Kupervaser, M., Addadi, Y., Levin, Y., Fraiberg, M., & Elazar, Z. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2508391123 · Cited by 2 · see citing works
Singh, A., Johnson, D. J., Kuhn, J. F., Johnson, K. L., Williams, J. G., Vancini, R. G., Sutton, D., Sharma, K., Lončarek, J., Borgnia, M. J., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-75742-x · Cited by 2 · see citing works
Scavone, F., Lian, S., Eskelinen, E., Cohen, R. E., & Yao, T. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-12-0535 · Cited by 2 · see citing works
ATG9 vesicles are a subtype of intracellular nanovesiclePreprint
Fesenko, M., Moore, D. J., Ewbank, P., Courthold, E., & Royle, S. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.12.612637 · Cited by 2 · see citing works
Braun, M. M., Sheehan, B. K., Shapiro, S. L., Ding, Y., Rubinstein, C. D., Lehman, B. P., & Puglielli, L. (2024) · Scientific Reports · doi:10.1038/s41598-024-76854-4 · Cited by 1 · see citing works
Chen, C., Liu, G., Xu, K., Chen, A., Cheng, Z., Yan, X., Zhang, T., Sun, Y., Tian, Y., Wang, J., et al. (2025) · Autophagy · doi:10.1080/15548627.2025.2496363 · Cited by 1 · see citing works
Liver-specific loss of Atg9a perturbs lipid metabolism and hepatocyte integrity
Mailler, É., Singh, A., Jarník, M., Li, Y., Holtzclaw, L. A., Hoffmann, V. J., Mine, S., Stallcup, P., Ordoubadinia, L., & Guardia, C. M. A. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2551028 · Cited by 1 · see citing works
From Hero to Hijacker: Autophagy’s Double Life in Immune Patrols and Cancer Escape
Garampon, F., & Claude‐Taupin, A. (2026) · Cells · doi:10.3390/cells15020102 · Cited by 1 · see citing works
Self-citationATG9B regulates mitochondrial integrity and apoptotic tumor cell death
Cao, H., Guo, L., Chen, J., Krueger, E. W., Razidlo, G. L., & McNiven, M. A. (2026) · Molecular Biology of the Cell · doi:10.1091/mbc.e25-07-0334 · Cited by 1 · see citing works
Cell Death by Holocrine Secretion: The Final Step of Epithelial Differentiation in Sebaceous Glands
Eckhart, L., Sukseree, S., & Fischer, H. (2026) · Cells · doi:10.3390/cells15121058 · Cited by 1 · see citing works
Wang, H., Gu, Y., Liu, J., Tan, H., Li, J., Li, J., Shi, W., & Zhang, Y. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.117007 · Cited by 1 · see citing works
Self-citationCasanova-Martín, C., Boaru, D. L., Fraile‐Μartinez, O., Montero, C. G., León-Oliva, D. D., Castro-Martinez, P. D., Gimeno, M. J., Buján, J., García‐Honduvilla, N., Guijarro, L. G., et al. (2025) · PubMed · doi:10.14670/hh-18-846 · Cited by 1 · see citing works
Response to Letter to Cell Death Pathways in Ischemic Stroke and Targeted Pharmacotherapy
Datta, A., Sarmah, D., & Bhattacharya, P. (2021) · Translational Stroke Research · doi:10.1007/s12975-021-00967-5 · Cited by 1 · see citing works
Nondegradable Ubiquitinated ATG9A Organizes Golgi Integrity and Dynamics Upon StressesPreprint
Luo, Q., Liu, Q., Cheng, H., Wang, J., Zhao, T., Zhang, J., Mu, C., Chen, L., Zhou, C., Yang, J., et al. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4009227 · Cited by 1 · see citing works
Propagation of neuronal micronuclei regulates microglial statesPreprint
Yano, S., Asami, N., Kishi, Y., Kubotani, H., Hattori, Y., Kitazawa, A., Hayashi, K., Kubo, K., Saeki, M., Maeda, C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.31.551211 · Cited by 1 · see citing works
Jia, J., Duran, J., Chen, L., Pu, J., & Ivanov, P. V. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.27.672666 · Cited by 1 · see citing works
Self-citationmiRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A
Markham, B. N., Ramnarine, C., Kim, S., Grever, W. E., Soto-Beasley, A. I., Heckman, M. G., Ren, Y., Osborne, A. C., Kehili, M., Bhagwate, A. V., et al. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00029-w
Autophagy activity is inhibited by hnRNP RPreprint
Ji, C. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.20.496848
Vale-Costa, S., Etibor, T. A., Brás, D., Sousa, A. L., Ferreira, M., Martins, G. G., Mello, V. H., & Amorim, M. J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.21.521536
van Vliet, A. R., Tito, S. D., Almacellas, E., & Tooze, S. A. (2023) · doi:10.3791/65349-v
Self-citationPublications from Juntendo University Graduate School of Medicine, 2021 [6/6]
(2024) · Juntendō Igaku/Juntendo igaku · doi:10.14789/jmj.jmj24-70.2-pl
Noncanonical roles of ATG5 and membrane atg8ylation in retromer assembly and functionPreprint
Paddar, M. A., Wang, F., Trosdal, E. S., Hendrix, E., He, Y. J., Salemi, M., Mudd, M. H., Jia, J., Duque, T. L. A., Javed, R., et al. (2024) · eLife · doi:10.7554/elife.100928.1
Self-citationNoncanonical roles of ATG5 and membrane atg8ylation in retromer assembly and functionPreprint
Paddar, M. A., Wang, F., Trosdal, E. S., Hendrix, E., He, Y. J., Salemi, M., Mudd, M. H., Jia, J., Duque, T. L. A., Javed, R., et al. (2024) · eLife · doi:10.7554/elife.100928.2
Self-citationTargeting membrane fragility in LGMD R2 through pharmacological autophagy inductionPreprint
Grossi, N., Pellier, E., Miagoux, Q., Benabidès, M., Polentes, J., Leteur, C., Bruge, C., & Nissan, X. (2025) · Research Square · doi:10.21203/rs.3.rs-6671973/v1
Paul, S., Tomsick, P. L., Milner, J. P., Biswas, S. R., Brindley, S., DeFoor, N., Zavar, L., Wright, G., Soto, Y., & Pickrell, A. M. (2026) · Autophagy · doi:10.1080/15548627.2026.2617844
Decoding ATG9A Variation: A Comprehensive Structural Investigation of All Missense VariantsPreprint
Utichi, M., Marjault, H., Tiberti, M., & Papaleo, E. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.03.703515
Autophagy in the interplay between shear stress and kidney epithelium homeostasis
Roccio, F. (2021) · theses.fr (ABES) · doi:10.70675/899d5d97z1062z453cza091zcae756198817
Ozkocak, D. C., Santavanond, J. P., Tanzer, M. C., & Poon, I. K. H. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03099-7
Physiological implications of phase separation in vesicle organization and trafficking
Liu, C., Cheng, J., & Wu, X. (2026) · BMC Biology · doi:10.1186/s12915-026-02607-6
Liu, D. Q., Cheng, Y., Huang, C., Xie, K., Jie, J., Zhang, Q., Lan, L., Chen, P., Xie, J. X., Wang, H., et al. (2026) · Autophagy · doi:10.1080/15548627.2026.2674714
Initial Molecular Detection of Membrane Damage in Post-Golgi Compartments
Shiba, Y., & Saito, N. (2026) · Cells · doi:10.3390/cells15151375
- Authors
- Claude-Taupin, A., Jia, J., Bhujabal, Z., Garfa-Traoré, M., Kumar, S., da Silva, G. P. D., Javed, R., Gu, Y., Allers, L., Peters, R., Wang, F., da Costa, L. J., Pallikkuth, S., Lidke, K. A., Mauthe, M., Verlhac, P., Uchiyama, Y., Salemi, M., Phinney, B., Tooze, S. A., Mari, M. C., Johansen, T., Reggiori, F., & Deretic, V.
- Affiliations
- University of New Mexico (US)
- UiT The Arctic University of Norway (NO)
- University Medical Center Groningen (NL)
- Juntendo University (JP)
- University of California, Davis (US)
- The Francis Crick Institute (GB)
- Corresponding author
- Deretic, Vojo
- ORCID
- Claude-Taupin, Aurore
- Jia, Jingyue
- Bhujabal, Zambarlal
- Kumar, Suresh
- da Silva, Gustavo Peixoto Duarte
- Javed, Ruheena
- Gu, Yuexi
- Allers, Lee
- Wang, Fulong
- Pallikkuth, Sandeep
- Lidke, Keith A.
- Mauthe, Mario
- Verlhac, Pauline
- Uchiyama, Yasuo
- Salemi, Michelle
- Phinney, Brett
- Tooze, Sharon A.
- Mari, Muriel C.
- Johansen, Terje
- Reggiori, Fulvio
- Deretic, Vojo
- Venue
- Nature Cell Biology
- Published
- 2021-07-12
- Volume
- 23
- Issue
- 8
- Pages
- 846-858
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC8276549
- OpenAlex
- W3177552861
- Cited by
- 92
- References
- 76
- Citations by year
- 2026: 15 · 2025: 23 · 2024: 16 · 2023: 16 · 2022: 15 · 2021: 7
- FWCI
- 9.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature Cell Biology (publishedVersion, other-oa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- NORA - Norwegian Open Research Archives (submittedVersion, other-oa)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
- Funders
- U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (R37AI042999, R01AI042999)
- U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (P20GM121176)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- ATG9A, plasma membrane integrity, membrane permeabilization, IQGAP1, autophagy, gasdermin, MLKL, membrane repair, programmed cell death
- MeSH terms
- Autophagosomes, Autophagy-Related Proteins, Cell Membrane, HeLa Cells, Humans, Membrane Proteins, Immunoblotting, Microscopy, Confocal, Protein Transport, Vesicular Transport Proteins, Immunoprecipitation, HEK293 Cells
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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