Autophagy‐based unconventional secretory pathway for extracellular delivery of IL‐1β

Dupont, Nicolas; Jiang, Shanya; Pilli, Manohar; Ornatowski, Wojciech; Bhattacharya, Dhruva; Deretic, Vojo

doi:10.1038/emboj.2011.398

Cited by 968Autophagy in Disease and TherapyInflammasome and immune disordersCellular transport and secretion

Autophagy‐based unconventional secretory pathway for extracellular delivery of IL‐1β

Open access

Dupont, Nicolas, Jiang, Shanya, Pilli, Manohar, Ornatowski, Wojciech, Bhattacharya, Dhruva, Deretic, Vojo·2011·The EMBO Journal

DOI 10.1038/emboj.2011.398PMC PMC3243609

Open this paper in CoChat — free account Open PDF

Abstract

Autophagy controls the quality and quantity of the eukaryotic cytoplasm while performing two evolutionarily highly conserved functions: cell-autonomous provision of energy and nutrients by cytosol autodigestion during starvation, and removal of defunct organelles and large aggregates exceeding the capacity of other cellular degradative systems. In contrast to these autodigestive processes, autophagy in yeast has additional, biogenesis functions. However, no equivalent biosynthetic roles have been described for autophagy in mammals. Here, we show that in mammalian cells, autophagy has a hitherto unappreciated positive contribution to the biogenesis and secretion of the proinflammatory cytokine IL-1β via an export pathway that depends on Atg5, inflammasome, at least one of the two mammalian Golgi reassembly stacking protein (GRASP) paralogues, GRASP55 (GORASP2) and Rab8a. This process, which is a type of unconventional secretion, expands the functional manifestations of autophagy beyond autodigestive and quality control roles in mammals. It enables a subset of cytosolic proteins devoid of signal peptide sequences, and thus unable to access the conventional pathway through the ER, to enter an autophagy-based secretory pathway facilitating their exit from the cytoplasm.

Integrity signals

Registry

Crossref · 10.1038/emboj.2011.398

Cites

68 of 68 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Autophagy mediates the secretion of proteins such as IL-1β and IL-18 that lack a leader peptide.
“Autophagy has also been recognized to mediate the secretion of proteins (34) – such as IL-1β and IL-18 (35, 36) – that would otherwise not enter the classical secretory pathway due to lack of a leader peptide.”
From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [35]
IL-18 trafficking is similar to that of IL-1β, with secretory autophagy playing a major role in its release.
“IL-18 trafficking is similar to that of IL-1β, with secretory autophagy also playing a major role in its release (35, 36).”
From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [35]

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227 · see citing works
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452 · see citing works
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602 · see citing works
Gout-associated uric acid crystals activate the NALP3 inflammasome
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326 · see citing works
Methods in Mammalian Autophagy Research
Mizushima, N., Yoshimori, T., & Levine, B. (2010) · Cell · doi:10.1016/j.cell.2010.01.028 · Cited by 4,497 · see citing works
Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila
Moy, R. H., & Cherry, S. R. (2013) · Journal of Innate Immunity · doi:10.1159/000350326 · Cited by 3,549 · see citing works
Autophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506 · see citing works
Autophagy in immunity and inflammation
Levine, B., Mizushima, N., & Virgin, H. W. (2011) · Nature · doi:10.1038/nature09782 · Cited by 3,289 · see citing works
Mechanisms of mitophagy
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · see citing works
Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065 · see citing works
Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049 · see citing works
The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance
Vandanmagsar, B., Youm, Y.-H., Ravussin, A., Galgani, J. E., Stadler, K., Mynatt, R. L., Ravussin, E., Stephens, J. M., & Dixit, V. D. (2011) · Nature Medicine · doi:10.1038/nm.2279 · Cited by 2,655 · see citing works
Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600 · see citing works
The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441 · see citing works
In Vivo Analysis of Autophagy in Response to Nutrient Starvation Using Transgenic Mice Expressing a Fluorescent Autophagosome Marker
Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,323 · see citing works
Dissection of the Autophagosome Maturation Process by a Novel Reporter Protein, Tandem Fluorescent-Tagged LC3
Kimura, S., Noda, T., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4451 · Cited by 2,278 · see citing works
Cepharanthine potently enhances the sensitivity of anticancer agents in K562 cells
Ikeda, R., Che, X., Yamaguchi, T., Ushiyama, M., Zheng, C., Okumura, H., Takeda, Y., Shibayama, Y., Nakamura, K. T., Jeung, H., et al. (2005) · Cancer Science · doi:10.1111/j.1349-7006.2005.00057.x · Cited by 2,268 · see citing works
Fatty acid–induced NLRP3-ASC inflammasome activation interferes with insulin signaling
Wen, H., Gris, D., Lei, Y. L., Jha, S., Zhang, L., Huang, M. T.-H., Brickey, W. J., & Ting, J. P. ‐. (2011) · Nature Immunology · doi:10.1038/ni.2022 · Cited by 1,811 · see citing works
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,730 · see citing works
The Inflammasome NLRs in Immunity, Inflammation, and Associated Diseases
Davis, B. K., Wen, H., & Ting, J. P.-Y. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-031210-101405 · Cited by 1,618 · see citing works
Autophagy in mammalian development and differentiation
Mizushima, N., & Levine, B. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-823 · Cited by 1,555 · see citing works
Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants
Eisenbarth, S. C., Colegio, O. R., O’Connor, W., Sutterwala, F. S., & Flavell, R. A. (2008) · Nature · doi:10.1038/nature06939 · Cited by 1,542 · see citing works
Autophagic cell death: the story of a misnomer
Kroemer, G., & Levine, B. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2529 · Cited by 1,453 · see citing works
HMGB1 is a therapeutic target for sterile inflammation and infection
Andersson, U., & Tracey, K. J. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101323 · Cited by 1,437 · see citing works
A Core Complex of BBS Proteins Cooperates with the GTPase Rab8 to Promote Ciliary Membrane Biogenesis
Nachury, M. V., Loktev, A. V., Zhang, Q., Westlake, C. J., Peränen, J., Merdes, A., Slusarski, D. C., Scheller, R. H., Bazan, J. F., Sheffield, V. C., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.053 · Cited by 1,384 · see citing works
Activated Ras requires autophagy to maintain oxidative metabolism and tumorigenesis
Guo, J. Y., Chen, H.-Y., Mathew, R., Fan, J., Strohecker, A. M., Karsli-Uzunbas, G., Kamphorst, J. J., Chen, G., Lemons, J. M. S., Karantza, V., et al. (2011) · Genes & Development · doi:10.1101/gad.2016311 · Cited by 1,323 · see citing works
Endogenous HMGB1 regulates autophagy
Tang, D., Kang, R., Livesey, K. M., Cheh, C.-W., Farkas, A., Loughran, P., Hoppe, G., Bianchi, M. E., Tracey, K. J., Zeh, H. J., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911078 · Cited by 951 · see citing works
Autophagy gone awry in neurodegenerative diseases
Wong, E. S. P., & Cuervo, A. M. (2010) · Nature Neuroscience · doi:10.1038/nn.2575 · Cited by 883 · see citing works
Autophagy, Immunity, and Microbial Adaptations
Deretic, V. P., & Levine, B. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.05.016 · Cited by 868 · see citing works
Self-citation
Active Caspase-1 Is a Regulator of Unconventional Protein Secretion
Keller, M., Rüegg, A., Werner, S., & Beer, H. (2008) · Cell · doi:10.1016/j.cell.2007.12.040 · Cited by 851 · see citing works
Beclin–phosphatidylinositol 3‐kinase complex functions at the trans‐Golgi network
Kihara, A., Kabeya, Y., Ohsumi, Y., & Yoshimori, T. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve061 · Cited by 813 · see citing works
Autophagy Controls IL-1β Secretion by Targeting Pro-IL-1β for Degradation
Harris, J., Hartman, M., Roche, C., Zeng, S. G., O'Shea, A., Sharp, F. A., Lambe, E. M., Creagh, E. M., Golenbock, D. T., Tschopp, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202911 · Cited by 794 · see citing works
A novel secretory pathway for interleukin‐1 beta, a protein lacking a signal sequence.
Rubartelli, A., Cozzolino, F., Talio, M., & Sitia, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08268.x · Cited by 780 · see citing works
Mechanisms of regulated unconventional protein secretion
Nickel, W., & Rabouille, C. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2617 · Cited by 703 · see citing works
The Beclin 1 interactome
He, C., & Levine, B. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.01.001 · Cited by 659 · see citing works
Mitochondrial fission and remodelling contributes to muscle atrophy
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596 · see citing works
A molecular network for de novo generation of the apical surface and lumen
Bryant, D. M., Datta, A., Rodriguez-Fraticelli, A., Peränen, J., Martín‐Belmonte, F., & Mostov, K. E. (2010) · Nature Cell Biology · doi:10.1038/ncb2106 · Cited by 585 · see citing works
Inflammasome-Dependent Release of the Alarmin HMGB1 in Endotoxemia
Lamkanfi, M., Sarkar, A., Walle, L. V., Vitari, A. C., Amer, A. O., Wewers, M. D., Tracey, K. J., Kanneganti, T., & Dixit, V. M. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000803 · Cited by 468 · see citing works
Emerging inflammasome effector mechanisms
Lamkanfi, M. (2011) · Nature reviews. Immunology · doi:10.1038/nri2936 · Cited by 435 · see citing works
Unconventional secretion of Acb1 is mediated by autophagosomes
Duran, J. M., Anjard, C., Stefan, C., Loomis, W. F., & Malhotra, V. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911154 · Cited by 433 · see citing works
GRASP65, a Protein Involved in the Stacking of Golgi Cisternae
Barr, F. A., Puype, M., Vandekerckhove, J. S., & Warren, G. (1997) · Cell · doi:10.1016/s0092-8674(00)80407-9 · Cited by 422 · see citing works
p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding
Itakura, E., & Mizushima, N. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009067 · Cited by 415 · see citing works
Autophagosome-Independent Essential Function for the Autophagy Protein Atg5 in Cellular Immunity to Intracellular Pathogens
Zhao, Z., Fux, B., Goodwin, M., Dunay, I. R., Strong, D. W., Miller, B. C., Cadwell, K., Delgado, M. A., Ponpuak, M., Green, K. G., et al. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.10.003 · Cited by 413 · see citing works
Self-citation
Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan
Alavez, S., Vantipalli, M. C., Zucker, D. J. S., Klang, I. M., & Lithgow, G. J. (2011) · Nature · doi:10.1038/nature09873 · Cited by 370 · see citing works
Autophagy in immunity and cell‐autonomous defense against intracellular microbes
Deretic, V. P. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00995.x · Cited by 363 · see citing works
Self-citation
NLRP3 (NALP3, Cryopyrin) Facilitates In Vivo Caspase-1 Activation, Necrosis, and HMGB1 Release via Inflammasome-Dependent and -Independent Pathways
Willingham, S. B., Allen, I. C., Bergstralh, D. T., Brickey, W. J., Huang, M. T.-H., Taxman, D. J., Duncan, J. A., & Ting, J. P. ‐. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900138 · Cited by 348 · see citing works
Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation
Manjithaya, R. R., Anjard, C., Loomis, W. F., & Subramani, S. E. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911149 · Cited by 337 · see citing works
GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell‐free system
Shorter, J., Watson, R., Giannakou, M., Clarke, M., Warren, G., & Barr, F. A. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.4949 · Cited by 336 · see citing works
Rescue of ΔF508-CFTR Trafficking via a GRASP-Dependent Unconventional Secretion Pathway
Gee, H. Y., Noh, S. H., Tang, B. L., Kim, K. H., & Lee, M. G. (2011) · Cell · doi:10.1016/j.cell.2011.07.021 · Cited by 329 · see citing works
A CD36-initiated Signaling Cascade Mediates Inflammatory Effects of β-Amyloid
Moore, K. J., El Khoury, J., Medeiros, L. A., Terada, K., Geula, C., Luster, A. D., & Freeman, M. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208788200 · Cited by 327 · see citing works
RalB and the Exocyst Mediate the Cellular Starvation Response by Direct Activation of Autophagosome Assembly
Bodemann, B. O., Orvedahl, A., Cheng, T., Ram, R. R., Ou, Y.-H., Formstecher, É., Maiti, M., Hazelett, C. C., Wauson, E., Balakireva, M., et al. (2011) · Cell · doi:10.1016/j.cell.2010.12.018 · Cited by 317 · see citing works
The emerging role of autophagy in the pathophysiology of diabetes mellitus
González, C. D., Lee, M., Marchetti, P., Pietropaolo, M., Towns, R., Vaccaro, M. I., Watada, H., & Wiley, J. W. (2010) · Autophagy · doi:10.4161/auto.7.1.13044 · Cited by 317 · see citing works
Delivery of Cytosolic Components by Autophagic Adaptor Protein p62 Endows Autophagosomes with Unique Antimicrobial Properties
Ponpuak, M., Davis, A. S., Roberts, E. A., Delgado, M. A., Dinkins, C., Zhao, Z., Virgin, H. W., Kyei, G. B., Johansen, T., Vergne, I., et al. (2010) · Immunity · doi:10.1016/j.immuni.2010.02.009 · Cited by 308 · see citing works
Self-citation
Liver autophagy contributes to the maintenance of blood glucose and amino acid levels
Ezaki, J., Matsumoto, N., Takeda‐Ezaki, M., Komatsu, M., Takahashi, K., Hiraoka, Y., Taka, H., Fujimura, T., Takehana, K., Yoshida, M., et al. (2011) · Autophagy · doi:10.4161/auto.7.7.15371 · Cited by 282 · see citing works
MT1‐MMP proinvasive activity is regulated by a novel Rab8‐dependent exocytic pathway
Bravo‐Cordero, J. J., Marrero‐Diaz, R., Megı́as, D., Genı́s, L., García‐Grande, A., García, M. Á., Arroyo, A. G., & Montoya, M. C. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601606 · Cited by 269 · see citing works
The Golgi-Associated Protein GRASP Is Required for Unconventional Protein Secretion during Development
Kinseth, M. A., Anjard, C., Fuller, D., Guizzunti, G., Loomis, W. F., & Malhotra, V. (2007) · Cell · doi:10.1016/j.cell.2007.06.029 · Cited by 258 · see citing works
Human IRGM regulates autophagy and cell-autonomous immunity functions through mitochondria
Singh, S., Ornatowski, W., Vergne, I., Naylor, J., Delgado, M. A., Roberts, E. A., Ponpuak, M., Master, S. S., Pilli, M., White, E., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2119 · Cited by 257 · see citing works
Self-citation
Mitochondrial BCL‐2 inhibits AMBRA1‐induced autophagy
Strappazzon, F., Rudan, M. V., Campello, S., Nazio, F., Florenzano, F., Fimia, G. M., Piacentini, M., Levine, B., & Cecconi, F. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.49 · Cited by 246 · see citing works
Autophagy in Innate and Adaptive Immunity
Xu, Y., & Eissa, N. T. (2010) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200909-103js · Cited by 242 · see citing works
Mutant rab8 Impairs Docking and Fusion of Rhodopsin-bearing Post-Golgi Membranes and Causes Cell Death of TransgenicXenopusRods
Moritz, O. L., Tam, B. M., Hurd, L. L., Peränen, J., Deretic, D., & Papermaster, D. S. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2341 · Cited by 228 · see citing works
Chemical Inducers of Autophagy That Enhance the Clearance of Mutant Proteins in Neurodegenerative Diseases
Renna, M., Jiménez-Sánchez, M., Sarkar, S., & Rubinsztein, D. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.072181 · Cited by 206 · see citing works
Rab8A and Rab13 are activated by insulin and regulate GLUT4 translocation in muscle cells
Sun, Y., Bilan, P. J., Liu, Z., & Klip, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009523107 · Cited by 197 · see citing works
Unconventional secretion: a stress on GRASP
Giuliani, F., Grieve, A. G., & Rabouille, C. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.04.005 · Cited by 126 · see citing works
Syntaxin 3 and SNAP-25 pairing, regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments
Mazelova, J., Ransom, N. L., Astuto-Gribble, L. M., Wilson, M. C., & Deretic, D. (2009) · Journal of Cell Science · doi:10.1242/jcs.039982 · Cited by 126 · see citing works
The class IA phosphatidylinositol 3-kinase p110-β subunit is a positive regulator of autophagy
Dou, Z., Chattopadhyay, M., Pan, J.-A., Guerriero, J. L., Jiang, Y.-P., Ballou, L. M., Yue, Z., Lin, R. Z., & Zong, W. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201006056 · Cited by 92 · see citing works
Autophagy in innate and adaptive immunity.
Deretic, V. (2005) · Trends in immunology · doi:10.1016/j.it.2005.08.003 · Cited by 89 · see citing works
Self-citation
Positive or Negative Roles of Different Cyclin-Dependent Kinase Pho85-Cyclin Complexes Orchestrate Induction of Autophagy in Saccharomyces cerevisiae
Yang, Z., Geng, J., Yen, W.-L., Wang, K., & Klionsky, D. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.033 · Cited by 77 · see citing works

Flagged first, then by citations

Sorted by citations

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works
Autophagy and Viruses: Adversaries or Allies?
Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,441 · 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
Macrophage Cytokines: Involvement in Immunity and Infectious Diseases
Arango Duque, G., & Descoteaux, A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00491 · Cited by 2,708 · see citing works
“Lack of fever induction may be explained by the fact that IL-18 signals through the MAPK p38 pathway instead of the NF-κB pathway, which is used by IL-1β (54).”
BackgroundInfluential
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) <sup>1</sup>
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
Self-citation
Autophagy in Human Health and Disease
Choi, A. M. K., Ryter, S. W., & Levine, B. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1205406 · Cited by 2,583 · see citing works
Autophagy in infection, inflammation and immunity
Deretic, V., Saitoh, T., & Akira, S. (2013) · Nature Reviews Immunology · doi:10.1038/nri3532 · Cited by 1,919 · see citing works
Self-citation
Molecular definitions of autophagy and related processes
Galluzzi, L., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cecconi, F., Choi, A. M., Chu, C. T., Codogno, P., Colombo, M. I., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796697 · Cited by 1,646 · see citing works
Self-citation
Autophagy modulation as a potential therapeutic target for diverse diseases
Rubinsztein, D. C., Codogno, P., & Levine, B. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3802 · Cited by 1,429 · see citing works
Autophagy and autophagy-related pathways in cancer
Debnath, J., Gammoh, N., & Ryan, K. M. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00585-z · Cited by 1,443 · see citing works
PAMP s and DAMP s: signal 0s that spur autophagy and immunity
Tang, D., Kang, R., Coyne, C. B., Zeh, H. J., & Lotze, M. T. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01146.x · Cited by 1,250 · see citing works
Cargo recognition and trafficking in selective autophagy
Stolz, A., Ernst, A., & Dikic, I. (2014) · Nature Cell Biology · doi:10.1038/ncb2979 · Cited by 1,207 · see citing works
Emerging regulation and functions of autophagy
Boya, P., Reggiori, F., & Codogno, P. (2013) · Nature Cell Biology · doi:10.1038/ncb2788 · Cited by 1,216 · see citing works
Inflammasome Complexes: Emerging Mechanisms and Effector Functions
Rathinam, V. A. K., & Fitzgerald, K. A. (2016) · Cell · doi:10.1016/j.cell.2016.03.046 · Cited by 1,109 · see citing works
Autophagy at the crossroads of catabolism and anabolism
Kaur, J., & Debnath, J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4024 · Cited by 993 · see citing works
HMGB1 in health and disease
Kang, R., Chen, R., Zhang, Q., Hou, W., Wu, S., Cao, L., Huang, J., Yu, Y., Fan, X.-G., Yan, Z., et al. (2014) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.05.001 · Cited by 956 · see citing works
Regulation of inflammasome signaling
Rathinam, V. A. K., Vanaja, S. K., & Fitzgerald, K. A. (2012) · Nature Immunology · doi:10.1038/ni.2237 · Cited by 927 · 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
“Major cellular functions involving components of the autophagy machinery Functions Protein Autophagic Role References Related to membrane biology Cytokine secretion ATG7 Elongation Henault et al., 2012; Li et al., 2016 ULK1 Initiation Cytokinesis BECN1 Nucleation Thoresen et al., 2010; You et al., 2016 BIF-1 Nucleatio…”
BackgroundInfluential
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-citation
The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response
Baroja-Mazo, A., Martín-Sánchez, F., Gomez, A. I., Martínez, C. M., Amores-Iniesta, J., Compan, V., Barberà-Cremades, M., Yagüe, J., Ruiz-Ortiz, E., Antón, J., et al. (2014) · Nature Immunology · doi:10.1038/ni.2919 · Cited by 790 · see citing works
Human Monocytes Engage an Alternative Inflammasome Pathway
Gaidt, M. M., Ebert, T. S., Chauhan, D., Schmidt, T., Schmid-Burgk, J. L., Rapino, F. A., Robertson, A. A. B., Cooper, M. A., Graf, T., & Hornung, V. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.012 · Cited by 780 · see citing works
TBK-1 Promotes Autophagy-Mediated Antimicrobial Defense by Controlling Autophagosome Maturation
Pilli, M., Arko-Mensah, J., Ponpuak, M., Roberts, E., Master, S., Mandell, M. A., Dupont, N., Ornatowski, W., Jiang, S., Bradfute, S. B., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.04.015 · Cited by 655 · see citing works
Self-citation
Complexity of Danger: The Diverse Nature of Damage-associated Molecular Patterns
Schaefer, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.619304 · Cited by 618 · see citing works
Interplay Between NLRP3 Inflammasome and Autophagy
Biasizzo, M., & Kopitar‐Jerala, N. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.591803 · Cited by 620 · see citing works
Autophagy Links Inflammasomes to Atherosclerotic Progression
Razani, B., Feng, C., Coleman, T., Emanuel, R., Wen, H., Hwang, S., Ting, J. P., Virgin, H. W., Kastan, M. B., & Semenkovich, C. F. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.02.011 · Cited by 601 · see citing works
Autophagy and autophagy-related proteins in the immune system
Shibutani, S., Saitoh, T., Nowag, H., Münz, C., & Yoshimori, T. (2015) · Nature Immunology · doi:10.1038/ni.3273 · Cited by 581 · see citing works
Autophagy balances inflammation in innate immunity
Deretic, V., & Levine, B. (2018) · Autophagy · doi:10.1080/15548627.2017.1402992 · Cited by 563 · see citing works
Self-citation
Bacteria–autophagy interplay: a battle for survival
Huang, J., & Brumell, J. H. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3160 · Cited by 578 · see citing works
Pathways of Unconventional Protein Secretion
Rabouille, C. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.11.007 · Cited by 573 · see citing works
Astrocytic and microglial cells as the modulators of neuroinflammation in Alzheimer’s disease
Singh, D. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02565-0 · Cited by 569 · see citing works
Impaired macrophage autophagy increases the immune response in obese mice by promoting proinflammatory macrophage polarization
Liu, K., Zhao, E., Ilyas, G., Lalazar, G., Lin, Y., Haseeb, M., Tanaka, K. E., & Czaja, M. J. (2015) · Autophagy · doi:10.1080/15548627.2015.1009787 · Cited by 530 · see citing works
Autophagy as a Stress-Response and Quality-Control Mechanism: Implications for Cell Injury and Human Disease
Murrow, L. M., & Debnath, J. (2012) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-163918 · Cited by 526 · see citing works
Linking cellular stress responses to systemic homeostasis
Galluzzi, L., Yamazaki, T., & Kroemer, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0068-0 · Cited by 529 · see citing works
Secretory autophagy
Ponpuak, M., Mandell, M. A., Kimura, T., Chauhan, S., Cleyrat, C., & Deretic, V. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.04.016 · Cited by 509 · see citing works
Self-citation
HMGB1 in Cancer: Good, Bad, or Both?
Kang, R., Zhang, Q., Zeh, H. J., Lotze, M. T., & Tang, D. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0495 · Cited by 496 · see citing works
The LC3-conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles
Leidal, A. M., Huang, H. H., Marsh, T., Solvik, T. A., Zhang, D., Ye, J., Kai, F., Goldsmith, J., Liu, J. Y., Huang, Y.-H., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-019-0450-y · Cited by 480 · see citing works
Autophagy in cancer metastasis
Mowers, E. E., Sharifi, M. N., & Macleod, K. F. (2016) · Oncogene · doi:10.1038/onc.2016.333 · Cited by 476 · see citing works
Crosstalk between autophagy and inflammatory signalling pathways: balancing defence and homeostasis
Cadwell, K. (2016) · Nature reviews. Immunology · doi:10.1038/nri.2016.100 · Cited by 478 · see citing works
Autophagy protects against active tuberculosis by suppressing bacterial burden and inflammation
Castillo, E. F., Dekonenko, A., Arko‐Mensah, J., Mandell, M. A., Dupont, N., Jiang, S., Delgado-Vargas, M., Timmins, G. S., Bhattacharya, D., Yang, H., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210500109 · Cited by 451 · see citing works
Self-citation
N-GSDMD trafficking to neutrophil organelles facilitates IL-1β release independently of plasma membrane pores and pyroptosis
Karmakar, M., Minns, M. S., Greenberg, E., Diaz-Aponte, J., Pestonjamasp, K., Johnson, J., Rathkey, J., Abbott, D. W., Wang, K., Shao, F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16043-9 · Cited by 413 · see citing works
Exosomes and Autophagy: Coordinated Mechanisms for the Maintenance of Cellular Fitness
Baixauli, F., López-Otı́n, C., & Mittelbrunn, M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00403 · Cited by 443 · see citing works
Lysosomal Exocytosis, Exosome Release and Secretory Autophagy: The Autophagic- and Endo-Lysosomal Systems Go Extracellular
Buratta, S., Tancini, B., Sagini, K., Delo, F., Chiaradia, E., Urbanelli, L., & Emiliani, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072576 · Cited by 433 · see citing works
Autophagy in osteoblasts is involved in mineralization and bone homeostasis
Nollet, M., Santucci-Darmanin, S., Breuil, V., Al-Sahlanee, R., Cros, C., Topi, M., Momier, D., Samson, M., Pagnotta, S., Cailleteau, L., et al. (2014) · Autophagy · doi:10.4161/auto.36182 · Cited by 422 · see citing works
Regulation of autophagy by the Rab GTPase network
Ao, X., Zou, L., & Wu, Y. (2014) · Cell Death & Differentiation · doi:10.1038/cdd.2013.187 · Cited by 411 · see citing works
Paneth cells secrete lysozyme via secretory autophagy during bacterial infection of the intestine
Bel, S., Pendse, M., Wang, Y., Li, Y., Ruhn, K. A., Hassell, B., Leal, T., Winter, S. E., Xavier, R. J., & Hooper, L. V. (2017) · Science · doi:10.1126/science.aal4677 · Cited by 396 · see citing works
Autophagy and cancer therapy
Maycotte, P., & Thorburn, A. M. (2011) · Cancer Biology & Therapy · doi:10.4161/cbt.11.2.14627 · Cited by 394 · see citing works
Mitochondria-associated membranes (MAMs) and inflammation
Missiroli, S., Patergnani, S., Caroccia, N., Pedriali, G., Perrone, M., Previati, M., Wieckowski, M. R., & Giorgi, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0027-2 · Cited by 389 · see citing works
A Comprehensive Review on Factors Influences Biogenesis, Functions, Therapeutic and Clinical Implications of Exosomes
Gurunathan, S., Kang, M.-H., & Kim, J. (2021) · International Journal of Nanomedicine · doi:10.2147/ijn.s291956 · Cited by 388 · see citing works
The multifunctional protein HMGB1: 50 years of discovery
Tang, D., Kang, R., Zeh, H. J., & Lotze, M. T. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00894-6 · Cited by 387 · see citing works
Translocation of interleukin-1β into a vesicle intermediate in autophagy-mediated secretion
Zhang, M., Kenny, S. J., Ge, L., Xu, K., & Schekman, R. W. (2015) · eLife · doi:10.7554/elife.11205 · Cited by 377 · see citing works
Autophagy and Inflammation
Matsuzawa, Y., Hwang, S., & Cadwell, K. (2017) · Annual Review of Immunology · doi:10.1146/annurev-immunol-042617-053253 · Cited by 378 · see citing works
Autophagy, Inflammation, and Immune Dysfunction in the Pathogenesis of Pancreatitis
Gukovskaya, A. S., Gukovsky, I., Algül, H., & Habtezion, A. (2017) · Gastroenterology · doi:10.1053/j.gastro.2017.08.071 · Cited by 357 · see citing works
Western diet as a trigger of Alzheimer’s disease: From metabolic syndrome and systemic inflammation to neuroinflammation and neurodegeneration
Więckowska-Gacek, A., Mietelska-Porowska, A., Wydrych, M., & Wojda, U. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101397 · Cited by 343 · see citing works
Modulation of inflammation by autophagy: Consequences for human disease
Netea-Maier, R. T., Plantinga, T. S., van de Veerdonk, F. L., Smit, J. W., & Netea, M. G. (2016) · Autophagy · doi:10.1080/15548627.2015.1071759 · Cited by 349 · see citing works
Dedicated SNAREs and specialized TRIM cargo receptors mediate secretory autophagy
Kimura, T., Jia, J., Kumar, S. G., Choi, S. W., Gu, Y., Mudd, M. H., Dupont, N., Jiang, S., Peters, R. S., Farzam, F., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201695081 · Cited by 329 · see citing works
Self-citation
Interleukin-1β Maturation Triggers Its Relocation to the Plasma Membrane for Gasdermin-D-Dependent and -Independent Secretion
Monteleone, M. M., Stanley, A. C., Chen, K. W., Brown, D. L., Bezbradica, J. S., von Pein, J. B., Holley, C. L., Boucher, D., Shakespear, M. R., Kapétanovic, R., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.027 · Cited by 306 · see citing works
Autophagy as an innate immunity paradigm: expanding the scope and repertoire of pattern recognition receptors
Deretic, V. P. (2011) · Current Opinion in Immunology · doi:10.1016/j.coi.2011.10.006 · Cited by 294 · see citing works
Self-citation
A Translocation Pathway for Vesicle-Mediated Unconventional Protein Secretion
Zhang, M., Liu, L., Lin, X., Wang, Y., Li, Y., Guo, Q., Li, S., Sun, Y., Tao, X., Zhang, D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.031 · Cited by 295 · see citing works
The interplay between exosomes and autophagy – partners in crime
Xu, J., Camfield, R., & Gorski, S. M. (2018) · Journal of Cell Science · doi:10.1242/jcs.215210 · Cited by 288 · see citing works
Autophagy-Dependent Production of Secreted Factors Facilitates Oncogenic RAS-Driven Invasion
Lock, R., Kenific, C. M., Leidal, A. M., Salas, E., & Debnath, J. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0841 · Cited by 280 · see citing works
PIKfyve inhibition increases exosome release and induces secretory autophagy
Hessvik, N. P., Øverbye, A., Brech, A., Torgersen, M. L., Jakobsen, I. S., Sandvig, K., & Llorente, A. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2309-8 · Cited by 269 · see citing works
Autophagy and Cancer Therapy
Thorburn, A. M., Thamm, D. H., & Gustafson, D. L. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.091850 · Cited by 281 · see citing works
Diversity in unconventional protein secretion
Rabouille, C., Malhotra, V., & Nickel, W. (2012) · Journal of Cell Science · doi:10.1242/jcs.103630 · Cited by 278 · see citing works
Non‐autophagic roles of autophagy‐related proteins
Subramani, S. E., & Malhotra, V. (2013) · EMBO Reports · doi:10.1038/embor.2012.220 · Cited by 276 · see citing works
Caspase-1: The inflammasome and beyond
Sollberger, G., Strittmatter, G. E., Garstkiewicz, M., Sand, J., & Beer, H. (2013) · Innate Immunity · doi:10.1177/1753425913484374 · Cited by 275 · see citing works
A20 Restricts Ubiquitination of Pro-Interleukin-1β Protein Complexes and Suppresses NLRP3 Inflammasome Activity
Duong, B. H., Onizawa, M., Osés-Prieto, J. A., Advincula, R., Burlingame, A. L., Malynn, B. A., & Ma, A. I. (2015) · Immunity · doi:10.1016/j.immuni.2014.12.031 · Cited by 269 · see citing works
Autophagy inhibition promotes SNCA/alpha-synuclein release and transfer via extracellular vesicles with a hybrid autophagosome-exosome-like phenotype
Minakaki, G., Menges, S., Kittel, A., Emmanouilidou, E., Schaeffner, I., Barkovits, K., Bergmann, A., Rockenstein, E., Adame, A., Marxreiter, F., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1395992 · Cited by 272 · see citing works
Autophagy: shaping the tumor microenvironment and therapeutic response
Maes, H., Rubio, N., Garg, A. D., & Agostinis, P. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.04.005 · Cited by 266 · see citing works
Oxidative stress-mediated HMGB1 biology
Yan, Y. Q., Tang, D., & Kang, R. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00093 · Cited by 262 · see citing works
TLR4 (toll-like receptor 4) activation suppresses autophagy through inhibition of FOXO3 and impairs phagocytic capacity of microglia
Lee, J.-W., Nam, H., Kim, L. E., Jeon, Y., Min, H., Ha, S., Lee, Y., Kim, S.-Y., Lee, S. J., Kim, E.-K., et al. (2019) · Autophagy · doi:10.1080/15548627.2018.1556946 · Cited by 260 · see citing works
Nondegradative Role of Atg5-Atg12/ Atg16L1 Autophagy Protein Complex in Antiviral Activity of Interferon Gamma
Hwang, S., Maloney, N. S., Bruinsma, M. W., Goel, G., Duan, E., Zhang, L., Shrestha, B., Diamond, M., Dani, A., Sosnovtsev, S. V., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.03.002 · Cited by 249 · see citing works
Nonlytic viral spread enhanced by autophagy components
Bird, S. W., Maynard, N. D., Covert, M. W., & Kirkegaard, K. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401437111 · Cited by 250 · see citing works
The PI3K/Akt Pathway in Meta-Inflammation
Acosta‐Martínez, M., & Cabail, M. Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315330 · Cited by 250 · see citing works
The Impact of Autophagy on Cell Death Modalities
Ryter, S. W., Mizumura, K., & Choi, A. M. K. (2014) · International Journal of Cell Biology · doi:10.1155/2014/502676 · Cited by 248 · see citing works
Autophagy regulates endothelial cell processing, maturation and secretion of von Willebrand factor
Torisu, T., Torisu, K., Lee, I. H., Liu, J., Malide, D. A., Combs, C. A., Wu, X., Rovira, I. I., Fergusson, M. M., Weigert, R., et al. (2013) · Nature Medicine · doi:10.1038/nm.3288 · Cited by 246 · see citing works
Loop Between NLRP3 Inflammasome and Reactive Oxygen Species
Dominic, A., Le, N.-T., & Takahashi, M. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8257 · Cited by 252 · see citing works
Exploiting Intrinsic Nanoparticle Toxicity: The Pros and Cons of Nanoparticle-Induced Autophagy in Biomedical Research
Peynshaert, K., Manshian, B. B., Joris, F., Braeckmans, K., Smedt, S. C. D., Demeester, J., & Soenen, S. J. (2014) · Chemical Reviews · doi:10.1021/cr400372p · Cited by 245 · see citing works
Autophagy in endothelial cells and tumor angiogenesis
Schaaf, M. B. E., Houbaert, D., Meçe, O., & Agostinis, P. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0287-8 · Cited by 231 · see citing works
Autophagy-dependent secretion: mechanism, factors secreted, and disease implications
New, J., & Thomas, S. M. (2019) · Autophagy · doi:10.1080/15548627.2019.1596479 · Cited by 226 · see citing works
NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22
Spalinger, M. R., Kasper, S., Gottier, C., Lang, S., Atrott, K., Vavricka, S. R., Scharl, S., Gutte, P. M., Grütter, M. G., Beer, H., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci83669 · Cited by 225 · see citing works
Indirect regulation of HMGB1 release by gasdermin D
Volchuk, A., Ye, A. A., Chi, L., Steinberg, B. E., & Goldenberg, N. M. (2020) · Nature Communications · doi:10.1038/s41467-020-18443-3 · Cited by 228 · see citing works
Autophagy and kidney inflammation
Kimura, T., Isaka, Y., & Yoshimori, T. (2017) · Autophagy · doi:10.1080/15548627.2017.1309485 · Cited by 226 · see citing works
Autophagy and inflammasomes
Harris, J., Lang, T., Thomas, J., Sukkar, M. B., Nabar, N. R., & Kehrl, J. H. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.02.013 · Cited by 224 · see citing works
Neuronal Aggregates: Formation, Clearance, and Spreading
Lim, J., & Yue, Z. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.02.002 · Cited by 221 · see citing works
Functions of autophagy in the tumor microenvironment and cancer metastasis
Mowers, E. E., Sharifi, M. N., & Macleod, K. F. (2018) · FEBS Journal · doi:10.1111/febs.14388 · Cited by 221 · see citing works
Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation
Deretic, V. P., Jiang, S., & Dupont, N. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.04.008 · Cited by 218 · see citing works
Self-citation
Innate Immunity to Adenovirus
Hendrickx, R., Stichling, N., Koelen, J. A., Kuryk, Ł., Lipiec, A., & Greber, U. F. (2014) · Human Gene Therapy · doi:10.1089/hum.2014.001 · Cited by 212 · see citing works
Inflammaging: Implications in Sarcopenia
Antuña, E., Cachán-Vega, C., Bermejo-Millo, J. C., Potes, Y., Caballero, B., Vega‐Naredo, I., Coto‐Montes, A. M., & García-González, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315039 · Cited by 223 · see citing works
Interleukin-1 as Innate Mediator of T Cell Immunity
Eeckhout, B. V. D., Tavernier, J. H., & Gerlo, S. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.621931 · Cited by 211 · see citing works
Loss of autophagy in hypothalamic POMC neurons impairs lipolysis
Kaushik, S., Arias, E., Kwon, H., Lopez, N. M., Athonvarangkul, D., Sahu, S., Schwartz, G. J., Pessin, J. E., & Singh, R. (2012) · The EMBO Reports · doi:10.1038/embor.2011.260 · Cited by 212 · see citing works
Activation and targeting of ATG8 protein lipidation
Martens, S., & Fracchiolla, D. (2020) · Cell Discovery · doi:10.1038/s41421-020-0155-1 · Cited by 206 · see citing works
Autophagy Mediates the Delivery of Thrombogenic Tissue Factor to Neutrophil Extracellular Traps in Human Sepsis
Kambas, K., Mitroulis, I., Apostolidou, E., Girod, A., Chrysanthopoulou, A., Pneumatikos, I. A., Skendros, P., Kourtzelis, I., Koffa, M. D., Kotsianidis, Ι., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045427 · Cited by 209 · see citing works
Inflammasome and Autophagy Regulation: A Two-way Street
Sun, Q., Fan, J., Billiar, T. R., & Scott, M. J. (2017) · Molecular Medicine · doi:10.2119/molmed.2017.00077 · Cited by 203 · see citing works
Suppression of Autophagy in Osteocytes Mimics Skeletal Aging
Onal, M., Piemontese, M., Xiong, J., Wang, Y., Han, L., Ye, S., Komatsu, M., Selig, M., Weinstein, R. S., Zhao, H., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.444190 · Cited by 206 · see citing works
Dual roles for autophagy: Degradation and secretion of Alzheimer's disease Aβ peptide
Nilsson, P., & Saido, T. C. (2014) · BioEssays · doi:10.1002/bies.201400002 · Cited by 202 · see citing works
Therapeutic targeting of autophagy in neurodegenerative and infectious diseases
Rubinsztein, D. C., Bento, C. F., & Deretic, V. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20150956 · Cited by 202 · see citing works
Self-citation
SARS-CoV-2 spike promotes inflammation and apoptosis through autophagy by ROS-suppressed PI3K/AKT/mTOR signaling
Li, F., Li, J., Wang, P., Yang, N., Huang, J., Ou, J., Xu, T., Zhao, X., Liu, T., Huang, X., et al. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166260 · Cited by 209 · see citing works
Autophagy, cell death, and cancer
Lin, L., & Baehrecke, E. H. (2015) · Molecular & Cellular Oncology · doi:10.4161/23723556.2014.985913 · Cited by 200 · see citing works
Secretory Autophagy in Cancer-Associated Fibroblasts Promotes Head and Neck Cancer Progression and Offers a Novel Therapeutic Target
New, J., Arnold, L., Ananth, M., Alvi, S. A., Thornton, M. M., Werner, L. R., Tawfik, O. W., Dai, H. D., Shnayder, Y., Kakarala, K., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1077 · Cited by 198 · see citing works
Copa Syndrome: a Novel Autosomal Dominant Immune Dysregulatory Disease
Vece, T. J., Watkin, L. B., Nicholas, S. K., Canter, D. L., Braun, M., Guillerman, R. P., Eldin, K. W., Bertolet, G., McKinley, S. D., Guzman, M. D., et al. (2016) · Journal of Clinical Immunology · doi:10.1007/s10875-016-0271-8 · Cited by 197 · see citing works

Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1
Dupont, N., Jiang, S., Pilli, M., Ornatowski, W., Bhattacharya, D., & Deretic, V. (2011)
Self-citation
Secretory versus degradative autophagy: unconventional secretion of inflammatory mediators
Jiang, S., Dupont, N., Castillo, E. F., & Deretic, V. (2013) · Journal of Innate Immunity · doi:10.1159/000346707 · Cited by 129 · see citing works
Self-citation
MOLECULAR MECHANISM OF AUTOPHAGY-BASED UNCONVENTIONAL SECRETION OF IL-β
Jiang, S. (2014) · UNM’s Digital Repository (University of New Mexico)
Self-citation
Role of autophagy in IL-1β export and release from cells
Claude‐Taupin, A., Bissa, B., Jia, J., Gu, Y., & Deretic, V. P. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.03.012 · Cited by 86 · see citing works
Self-citation
Translocation of interleukin-1β into a vesicle intermediate in autophagy-mediated secretion
Zhang, M., Kenny, S. J., Ge, L., Xu, K., & Schekman, R. W. (2015) · eLife · doi:10.7554/elife.11205 · Cited by 377 · see citing works

Authors: Dupont, N., Jiang, S., Pilli, M., Ornatowski, W., Bhattacharya, D., & Deretic, V.
Affiliations: University of New Mexico Health Sciences Center (US)
University of New Mexico (US)
Corresponding author: Deretic, Vojo
ORCID: Dupont, Nicolas
Jiang, Shanya
Pilli, Manohar
Ornatowski, Wojciech
Bhattacharya, Dhruva
Deretic, Vojo
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2011-11-08
Volume: 30
Issue: 23
Pages: 4701-4711
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/emboj.2011.398
PMC: PMC3243609
OpenAlex: W2109070574
Cited by: 967
References: 68
Citations by year: 2026: 41 · 2025: 68 · 2024: 63 · 2023: 54 · 2022: 96 · 2021: 73 · 2020: 86 · 2019: 55 · 2018: 68 · 2017: 66 · 2016: 77 · 2015: 50 · 2014: 56 · 2013: 66 · 2012: 45
FWCI: 40.73
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (AI042999)
National Institute of Allergy and Infectious Diseases (RC1AI086845, R01AI042999, R01AI069345, R37AI042999)
Topics: Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: autophagy, unconventional secretion, IL-1β, proinflammatory cytokine secretion, ATG5, inflammasome, GRASP55, Rab8a
MeSH terms: Autophagy-Related Protein 5, Animals, Autophagy, Carrier Proteins, Cells, Cultured, Luminescent Proteins, Macrophages, Membrane Proteins, Microtubule-Associated Proteins, Nigericin, Protein Processing, Post-Translational, Macrolides, Interleukin-18, rab GTP-Binding Proteins, Protein Transport, HMGB1 Protein, Intracellular Signaling Peptides and Proteins, Mice, Interleukin-1beta, Secretory Pathway, Inflammasomes

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

Autophagy‐based unconventional secretory pathway for extracellular delivery of IL‐1β

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks