The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Lysosomal Exocytosis, Exosome Release and Secretory Autophagy: The Autophagic- and Endo-Lysosomal Systems Go Extracellular
Abstract
Beyond the consolidated role in degrading and recycling cellular waste, the autophagic- and endo-lysosomal systems play a crucial role in extracellular release pathways. Lysosomal exocytosis is a process leading to the secretion of lysosomal content upon lysosome fusion with plasma membrane and is an important mechanism of cellular clearance, necessary to maintain cell fitness. Exosomes are a class of extracellular vesicles originating from the inward budding of the membrane of late endosomes, which may not fuse with lysosomes but be released extracellularly upon exocytosis. In addition to garbage disposal tools, they are now considered a cell-to-cell communication mechanism. Autophagy is a cellular process leading to sequestration of cytosolic cargoes for their degradation within lysosomes. However, the autophagic machinery is also involved in unconventional protein secretion and autophagy-dependent secretion, which are fundamental mechanisms for toxic protein disposal, immune signalling and pathogen surveillance. These cellular processes underline the crosstalk between the autophagic and the endosomal system and indicate an intersection between degradative and secretory functions. Further, they suggest that the molecular mechanisms underlying fusion, either with lysosomes or plasma membrane, are key determinants to maintain cell homeostasis upon stressing stimuli. When they fail, the accumulation of undigested substrates leads to pathological consequences, as indicated by the involvement of autophagic and lysosomal alteration in human diseases, namely lysosomal storage disorders, age-related neurodegenerative diseases and cancer. In this paper, we reviewed the current knowledge on the functional role of extracellular release pathways involving lysosomes and the autophagic- and endo-lysosomal systems, evaluating their implication in health and disease.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
LE is a calcium-regulated process that expels lysosomal contents into the extracellular space.
“LE is a calcium‐regulated process that expels lysosomal contents into the extracellular space (Buratta et al. 2020; Tancini et al. 2020).”
From The Alzheimer's Disease Gene SORL1 Regulates Lysosome Function in Human Microglia (2025) · cites this paper as Buratta et al. 2020
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
2 retracted
Martinez, J., Malireddi, R. K. S., Lu, Q., Cunha, L. D., Pelletier, S., Gingras, S., Orchard, R., Guan, J.-L., Tan, H., Peng, J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3192 · Cited by 758 · cited 1×
“LAP requires several components of the macroautophagic machinery, such as the Atg5-Atg12-Atg16L1 complex [105], the Atg3-Atg7 complex and the PI3K activity [106].”
RetractedMartinez, J., Almendinger, J., Oberst, A., Ness, R., Dillon, C. P., Fitzgerald, P., Hengartner, M. O., & Green, D. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113421108 · Cited by 655 · cited 1×
“LAP is involved in the response to pathogens [101], but also in the elimination of dead cells [108], including the finalization of the entotic process, by which cells engulf and cannibalize other cells [109].”
BackgroundRetractedThéry, C., Witwer, K. W., Aikawa, E., Alcaraz, M. J., Anderson, J. D., Andriantsitohaina, R., Antoniou, A., Arab, T., Archer, F., Atkin‐Smith, G. K., et al. (2018) · Journal of Extracellular Vesicles · doi:10.1080/20013078.2018.1535750 · Cited by 11,099
Self-citationKowal, J., Arras, G., Colombo, M., Jouve, M., Morath, J. P., Primdal-Bengtson, B., Dingli, F., Loew, D., Tkach, M., & Théry, C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521230113 · Cited by 3,426
Johnstone, R. M., Adam, M., Hammond, J. R., Orr, L., & Turbide, C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48095-7 · Cited by 2,931
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
Chloroquine inhibits autophagic flux by decreasing autophagosome-lysosome fusion
Mauthe, M., Orhon, I., Rocchi, C., Zhou, X., Luhr, M., Hijlkema, K.-J., Coppes, R. P., Engedal, N., Mari, M., & Reggiori, F. (2018) · Autophagy · doi:10.1080/15548627.2018.1474314 · Cited by 2,122
The machinery of macroautophagy
Feng, Y., He, D., Yao, Z., & Klionsky, D. J. (2014) · Cell Research · doi:10.1038/cr.2013.168 · Cited by 2,083
Secretory Mechanisms and Intercellular Transfer of MicroRNAs in Living Cells
Kosaka, N., Iguchi, H., Yoshioka, Y., Takeshita, F., Matsuki, Y., & Ochiya, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.107821 · Cited by 1,934
Autophagy in infection, inflammation and immunity
Deretic, V., Saitoh, T., & Akira, S. (2013) · Nature Reviews Immunology · doi:10.1038/nri3532 · Cited by 1,919
Termination of autophagy and reformation of lysosomes regulated by mTOR
Yu, L., McPhee, C. K., Zheng, L., Mardones, G. A., Rong, Y., Peng, J., Mi, N., Zhao, Y., Liu, Z., Wan, F., et al. (2010) · Nature · doi:10.1038/nature09076 · Cited by 1,544
A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
Cadwell, K., Liu, J. Y., Brown, S. L., Miyoshi, H., Loh, J., Lennerz, J. K., Kishi, C., Kc, W., Carrero, J. A., Hunt, S., et al. (2008) · Nature · doi:10.1038/nature07416 · Cited by 1,542
Autophagy‐based unconventional secretory pathway for extracellular delivery of IL‐1β
Dupont, N., Jiang, S., Pilli, M., Ornatowski, W., Bhattacharya, D., & Deretic, V. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.398 · Cited by 967
Aβ Secretion and Plaque Formation Depend on Autophagy
Nilsson, P., Loganathan, K., Sekiguchi, M., Matsuba, Y., Hui, K., Tsubuki, S., Tanaka, M., Iwata, N., Saito, T., & Saido, T. C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.042 · Cited by 459 · cited 1×
“On the other hand, it has been demonstrated that exosomes are not the only manner to release the amyloid β (Aβ) peptide extracellularly, as Aβ is generated in autophagic vacuoles [129] and Aβ secretion/plaque formation have been shown to depend on autophagy [130].”
BackgroundPaneth 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
Extracellular vesicles: lipids as key components of their biogenesis and functions
Record, M., Silvente-Poirot, S., Poirot, M., & Wakelam, M. O. (2018) · Journal of Lipid Research · doi:10.1194/jlr.e086173 · Cited by 328
Prelysosomal convergence of autophagic and endocytic pathways
Gordon, P. B., & Seglen, P. O. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(88)90556-6 · Cited by 281 · cited 1×
“In turn, amphisomes are either addressed to degradation by fusion with lysosomes or released extracellularly [139,140].”
BackgroundMinakaki, 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
Ca2+ and synaptotagmin VII–dependent delivery of lysosomal membrane to nascent phagosomes
Czibener, C., Sherer, N. M., Becker, S. M., Pypaert, M., Hui, E., Chapman, E. R., Mothes, W., & Andrews, N. W. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605004 · Cited by 165
Flagged first, then by citations
Research works printed but not linked: 130
- Andrews, 2000, Regulated secretion of conventional lysosomes, Trends Cell Biol., 10, 316, 10.1016/S0962-8924(00)01794-3 · DOI
- Medina, 2011, Transcriptional activation of lysosomal exocytosis promotes cellular clearance, Dev. Cell, 21, 421, 10.1016/j.devcel.2011.07.016 · DOI
- Blott, 2002, Secretory lysosomes, Nat. Rev. Mol. Cell Biol., 3, 122, 10.1038/nrm732 · DOI
- Lettau, 2007, Secretory lysosomes and their cargo in T and NK cells, Immunol. Lett., 108, 10, 10.1016/j.imlet.2006.10.001 · DOI
- Reddy, 2001, Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes, Cell, 106, 157, 10.1016/S0092-8674(01)00421-4 · DOI
- Corrotte, 2019, Lysosomes and plasma membrane repair, Curr. Top. Membr., 84, 1, 10.1016/bs.ctm.2019.08.001 · DOI
- Mostov, 1997, Journey across the osteoclast, Science, 276, 219, 10.1126/science.276.5310.219 · DOI
- Stinchcombe, 2004, Linking albinism and immunity: The secrets of secretory lysosomes, Science, 305, 55, 10.1126/science.1095291 · DOI
- Bossi, 2005, CTL secretory lysosomes: Biogenesis and secretion of a harmful organelle, Semin. Immunol., 17, 87, 10.1016/j.smim.2004.09.007 · DOI
- Logan, 2003, Understanding exocytosis in immune and inflammatory cells: The molecular basis of mediator secretion, J. Allergy Clin. Immunol., 111, 923, 10.1016/S0091-6749(03)80114-8 · DOI
- Zhang, 2007, Regulated ATP release from astrocytes through lysosome exocytosis, Nat. Cell Biol., 9, 945, 10.1038/ncb1620 · DOI
- Duan, 2006, P2X7/P2Z receptors: Properties and relevance to CNS functions, Glia, 54, 738, 10.1002/glia.20397 · DOI
- Li, 2019, Lysosome exocytosis is involved in astrocyte ATP release after oxidative stress induced by H2O2, Neurosci. Lett., 705, 251, 10.1016/j.neulet.2019.03.046 · DOI
- Dou, 2012, Microglial migration mediated by ATP-induced ATP release from lysosomes, Cell Res., 22, 1022, 10.1038/cr.2012.10 · DOI · Paper page
- Andrews, 2005, Membrane resealing: Synaptotagmin VII keeps running the show, Sci. Signal., 2005, pe19
- Arantes, 2006, A role for synaptotagmin VII-regulated exocytosis of lysosomes in neurite outgrowth from primary sympathetic neurons, J. Neurosci., 26, 4630, 10.1523/JNEUROSCI.0009-06.2006 · DOI
- Naegeli, 2017, Cell Invasion In Vivo via Rapid Exocytosis of a Transient Lysosome-Derived Membrane Domain, Dev. Cell, 43, 403, 10.1016/j.devcel.2017.10.024 · DOI
- Leong, 2014, Invadopodia are required for cancer cell extravasation and are a therapeutic target for metastasis, Cell Rep., 8, 1558, 10.1016/j.celrep.2014.07.050 · DOI
- Schoumacher, 2010, Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia, J. Cell Biol., 189, 541, 10.1083/jcb.200909113 · DOI
- Jaiswal, 2002, Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells, J. Cell Biol., 159, 625, 10.1083/jcb.200208154 · DOI
- Bandyopadhyay, D., Cyphersmith, A., Zapata, J.A., Kim, Y.J., and Payne, C.K. (2014). Lysosome transport as a function of lysosome diameter. PLoS ONE, 9. · DOI
- Rao, 2004, Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis, J. Biol. Chem., 279, 20471, 10.1074/jbc.M400798200 · DOI · Paper page
- Tucker, 2004, Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs, Science, 304, 435, 10.1126/science.1097196 · DOI
- Vieira, 2018, Rab3a and Rab10 are regulators of lysosome exocytosis and plasma membrane repair, Small GTPases, 9, 349, 10.1080/21541248.2016.1235004 · DOI
- Sbano, 2017, TFEB-mediated increase in peripheral lysosomes regulates store-operated calcium entry, Sci. Rep., 7, 40797, 10.1038/srep40797 · DOI
- Platt, 2019, Lysosomal storage diseases, Nat. Rev. Dis. Primers, 5, 34, 10.1038/s41572-019-0089-9 · DOI
- Spampanato, 2013, Transcription factor EB (TFEB) is a new therapeutic target for Pompe disease, EMBO Mol. Med., 5, 691, 10.1002/emmm.201202176 · DOI · Paper page
- Shen, 2012, Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release, Nat. Commun., 3, 731, 10.1038/ncomms1735 · DOI
- Grimm, 2012, Role of TRPML and two-pore channels in endolysosomal cation homeostasis, J. Pharmacol. Exp. Ther., 342, 236, 10.1124/jpet.112.192880 · DOI
- Turner, 2016, Drug induced exocytosis of glycogen in Pompe disease, Biochem. Biophys. Res. Commun., 479, 721, 10.1016/j.bbrc.2016.09.145 · DOI
- Samie, 2014, Lysosomal exocytosis and lipid storage disorders, J. Lipid Res., 55, 995, 10.1194/jlr.R046896 · DOI
- Tsunemi, 2019, Increased Lysosomal Exocytosis Induced by Lysosomal Ca2+ Channel Agonists Protects Human Dopaminergic Neurons from α-Synuclein Toxicity, J. Neurosci., 39, 5760, 10.1523/JNEUROSCI.3085-18.2019 · DOI
- Tancini, B., Buratta, S., Sagini, K., Costanzi, E., Delo, F., Urbanelli, L., and Emiliani, C. (2019). Insight into the Role of Extracellular Vesicles in Lysosomal Storage Disorders. Genes, 6. · DOI
- Kowal, 2014, Biogenesis and secretion of exosomes, Curr. Opin. Cell Biol., 29, 116, 10.1016/j.ceb.2014.05.004 · DOI · Paper page
- Hessvik, 2018, Current knowledge on exosome biogenesis and release, Cell Mol. Life Sci., 75, 193, 10.1007/s00018-017-2595-9 · DOI · Paper page
- Oorschot, 2002, Immunoelectron microscopic localization of cholesterol using biotinylated and non-cytolytic perfringolysin O, J. Histochem. Cytochem., 50, 43, 10.1177/002215540205000105 · DOI
- Skotland, 2017, Lipids in exosomes: Current knowledge and the way forward, Prog. Lipid Res., 66, 30, 10.1016/j.plipres.2017.03.001 · DOI · Paper page
- Hill, 2014, Minimal experimental requirements for definition of extracellular vesicles and their functions: A position statement from the International Society for Extracellular Vesicles, J. Extracell. Vesicles, 3, 26913, 10.3402/jev.v3.26913 · DOI · Paper page
- Mathieu, 2019, Specificities of secretion and uptake of exosomes and other extracellular vesicles for cell-to-cell communication, Nat. Cell Biol., 21, 9, 10.1038/s41556-018-0250-9 · DOI
- Baixauli, 2014, Exosomes and autophagy: Coordinated mechanisms for the maintenance of cellular fitness, Front. Immunol., 5, 403, 10.3389/fimmu.2014.00403 · DOI
- Hessvik, 2016, PIKfyve inhibition increases exosome release and induces secretory autophagy, Cell Mol. Life Sci., 73, 4717, 10.1007/s00018-016-2309-8 · DOI · Paper page
- Urbanelli, 2013, Signaling pathways in exosomes biogenesis, secretion and fate, Genes, 4, 152, 10.3390/genes4020152 · DOI
- Colombo, 2013, Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles, J. Cell Sci., 126, 5553
- Siljander, 2015, Biological properties of extracellular vesicles and their physiological functions, J. Extracell. Vesicles, 4, 27066, 10.3402/jev.v4.27066 · DOI · Paper page
- Escola, 1998, Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes, J. Biol. Chem., 273, 20121, 10.1074/jbc.273.32.20121 · DOI · Paper page
- Chairoungdua, 2010, Exosome release of β-catenin: A novel mechanism that antagonizes Wnt signaling, J. Cell Biol., 190, 1079, 10.1083/jcb.201002049 · DOI
- Hurwitz, 2016, Nanoparticle analysis sheds budding insights into genetic drivers of extracellular vesicle biogenesis, J. Extracell. Vesicles, 5, 31295, 10.3402/jev.v5.31295 · DOI
- Mittelbrunn, 2011, Unidirectional transfer of microRNA-loaded exosomes from T cells to antigen-presenting cells, Nat. Commun., 2, 282, 10.1038/ncomms1285 · DOI
- Trajkovic, 2008, Ceramide triggers budding of exosome vesicles into multivesicular endosomes, Science, 319, 1244, 10.1126/science.1153124 · DOI
- Zhukovsky, 2019, Phosphatidic acid in membrane rearrangements, FEBS Lett., 593, 2428, 10.1002/1873-3468.13563 · DOI
- Laulagnier, 2004, PLD2 is enriched on exosomes and its activity is correlated to the release of exosomes, FEBS Lett., 572, 11, 10.1016/j.febslet.2004.06.082 · DOI
- Ghossoub, 2014, Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2, Nat. Commun., 5, 3477, 10.1038/ncomms4477 · DOI
- Alonso, 2005, Diacylglycerol kinase alpha regulates the secretion of lethal exosomes bearing Fas ligand during activation-induced cell death of T lymphocytes, J. Biol. Chem., 280, 28439, 10.1074/jbc.M501112200 · DOI
- Alonso, 2011, Diacylglycerol kinase α regulates the formation and polarisation of mature multivesicular bodies involved in the secretion of Fas ligand-containing exosomes in T lymphocytes, Cell Death Differ., 18, 1161, 10.1038/cdd.2010.184 · DOI
- Seow, 2011, Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission, Neurobiol. Dis., 42, 360, 10.1016/j.nbd.2011.01.029 · DOI
- Vingtdeux, 2007, Alkalizing drugs induce accumulation of amyloid precursor protein by-products in luminal vesicles of multivesicular bodies, J. Biol. Chem., 282, 18197, 10.1074/jbc.M609475200 · DOI
- Eitan, 2016, Impact of lysosome status on extracellular vesicle content and release, Ageing Res. Rev., 32, 65, 10.1016/j.arr.2016.05.001 · DOI
- Strauss, 2010, Exosome secretion ameliorates lysosomal storage of cholesterol in Niemann-Pick type C disease, J. Biol. Chem., 285, 26279, 10.1074/jbc.M110.134775 · DOI
- Canonico, B., Cesarini, E., Salucci, S., Luchetti, F., Falcieri, E., Di Sario, G., Palma, F., and Papa, S. (2016). Defective Autophagy, Mitochondrial Clearance and Lipophagy in Niemann-Pick Type B Lymphocytes. PLoS ONE, 11. · DOI
- Riva, P., Battaglia, C., and Venturin, M. (2019). Emerging Role of Genetic Alterations Affecting Exosome Biology in Neurodegenerative Diseases. Int. J. Mol. Sci., 20. · DOI
- Bellingham, 2012, Exosomes: Vehicles for the transfer of toxic proteins associated with neurodegenerative diseases?, Front. Physiol., 3, 124, 10.3389/fphys.2012.00124 · DOI · Paper page
- Vella, L.J., Hill, A.F., and Cheng, L. (2016). Focus on Extracellular Vesicles: Exosomes and Their Role in Protein Trafficking and Biomarker Potential in Alzheimer’s and Parkinson’s Disease. Int. J. Mol. Sci., 17. · DOI
- Lai, 2012, Role of exosomes/microvesicles in the nervous system and use in emerging therapies, Front. Physiol., 3, 228, 10.3389/fphys.2012.00228 · DOI
- Chen, 2017, Potential Roles of Exosomal MicroRNAs as Diagnostic Biomarkers and Therapeutic Application in Alzheimer’s Disease, Neural Plast., 2017, 7027380, 10.1155/2017/7027380 · DOI · Paper page
- Vilaça-Faria, H., Salgado, A.J., and Teixeira, F.G. (2019). Mesenchymal Stem Cells-derived Exosomes: A New Possible Therapeutic Strategy for Parkinson’s Disease?. Cells, 8. · DOI
- Machado, 2015, Regulated lysosomal exocytosis mediates cancer progression, Sci. Adv., 1, e1500603, 10.1126/sciadv.1500603 · DOI
- Kim, 2019, Exosomal release through TRPML1-mediated lysosomal exocytosis is required for adipogenesis, Biochem. Biophys. Res. Commun., 51, 409, 10.1016/j.bbrc.2019.01.115 · DOI
- Tian, 2013, Dynamics of exosome internalization and trafficking, J. Cell Physiol., 228, 1487, 10.1002/jcp.24304 · DOI
- Chiba, 2016, Exosomes derived from SW480 colorectal cancer cells promote cell migration in HepG2 hepatocellular cancer cells via the mitogen-activated protein kinase pathway, Int. J. Oncol., 48, 305, 10.3892/ijo.2015.3255 · DOI
- Harnett, 2017, From Christian de Duve to Yoshinori Ohsumi: More to autophagy than just dining at home, Biomed. J., 40, 9, 10.1016/j.bj.2016.12.004 · DOI
- Yin, 2016, Autophagy: Machinery and regulation, Microb. Cell, 3, 588, 10.15698/mic2016.12.546 · DOI
- Galluzzi, 2017, Molecular definitions of autophagy and related processes, EMBO J., 36, 1811, 10.15252/embj.201796697 · DOI · Paper page
- Yu, 2018, Autophagy pathway: Cellular and molecular mechanisms, Autophagy, 14, 207, 10.1080/15548627.2017.1378838 · DOI
- Cadwell, 2018, Beyond self-eating: The control of nonautophagic functions and signaling pathways by autophagy-related proteins, J. Cell Biol., 217, 813, 10.1083/jcb.201706157 · DOI
- Galluzzi, 2014, Metabolic control of autophagy, Cell, 159, 1263, 10.1016/j.cell.2014.11.006 · DOI · Paper page
- Wei, 2018, Origin of the Autophagosome membrane in mammals, BioMed Res. Int., 2018, 1012789, 10.1155/2018/1012789 · DOI
- Wesselborg, 2015, Autophagy signal transduction by ATG proteins: From hierarchies to networks, Cell Mol. Life Sci., 72, 4721, 10.1007/s00018-015-2034-8 · DOI
- Klionsky, 2014, Autophagosomes, phagosomes, autolysosomes, phagolysosomes, autophagolysosomes. Wait, I’m confused, Autophagy, 10, 549, 10.4161/auto.28448 · DOI
- Chen, 2018, Development of Research into Autophagic Lysosome Reformation, Mol. Cells, 41, 45
- Tekirdag, 2018, Chaperone-mediated autophagy and endosomal microautophagy: Joint by a chaperone, J. Biol. Chem., 293, 5414, 10.1074/jbc.R117.818237 · DOI
- Olsvik, 2019, Endosomal microautophagy is an integrated part of the autophagic response to amino acid starvation, Autophagy, 15, 182, 10.1080/15548627.2018.1532265 · DOI
- Gudbergsson, 2019, Exosomes and autophagy: Rekindling the vesicular waste hypothesis, J. Cell Commun. Signal., 13, 443, 10.1007/s12079-019-00524-8 · DOI
- Rabouille, 2017, Pathways of Unconventional Protein Secretion, Trends Cell Biol., 27, 230, 10.1016/j.tcb.2016.11.007 · DOI
- Bissa, 2018, Role of autophagy in IL-1β export and release from cells, Semin. Cell Dev. Biol., 83, 36, 10.1016/j.semcdb.2018.03.012 · DOI
- Rubartelli, 1990, A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence, EMBO J., 9, 1503, 10.1002/j.1460-2075.1990.tb08268.x · DOI
- Diamond, 2016, Inflammasome-dependent IL-1β release depends upon membrane permeabilisation, Cell Death Differ., 23, 1219, 10.1038/cdd.2015.176 · DOI
- Ponpuak, 2015, Secretory autophagy, Curr. Opin. Cell Biol., 35, 106, 10.1016/j.ceb.2015.04.016 · DOI
- Gardella, 2002, The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway, EMBO Rep., 3, 995, 10.1093/embo-reports/kvf198 · DOI
- Wang, Z., Zhou, H., Zheng, H., Zhou, X., Shen, G., Teng, X., Liu, X., Zhang, J., Wei, X., and Hu, Z. (2020). Autophagy-based unconventional secretion of HMGB1 by keratinocytes plays a pivotal role in psoriatic skin inflammation. Autophagy, 1–24. · DOI
- Ghatak, 2018, TGFB1 is secreted through an unconventional pathway dependent on the autophagic machinery and cytoskeletal regulators, Autophagy, 14, 465, 10.1080/15548627.2017.1422850 · DOI
- Noh, 2018, Specific autophagy and ESCRT components participate in the unconventional secretion of CFTR, Autophagy, 14, 1761, 10.1080/15548627.2018.1489479 · DOI
- Wong, 2017, Lysosomal Degradation Is Required for Sustained Phagocytosis of Bacteria by Macrophages, Cell Host Microbe, 21, 719, 10.1016/j.chom.2017.05.002 · DOI · Paper page
- Romao, 2014, LC3-associated phagocytosis, Autophagy, 10, 526, 10.4161/auto.27606 · DOI
- Fletcher, 2018, The WD40 domain of ATG16L1 is required for its non-canonical role in lipidation of LC3 at single membranes, EMBO J., 37, e97840, 10.15252/embj.201797840 · DOI
- Wong, 2018, Rubicon: LC3-associated phagocytosis and beyond, FEBS J., 285, 1379, 10.1111/febs.14354 · DOI · Paper page
- Florey, 2019, Macropinocytosis and autophagy crosstalk in nutrient scavenging, Philos. Trans. R. Soc. B, 374, 20180154, 10.1098/rstb.2018.0154 · DOI
- Gerstenmaier, 2015, The autophagic machinery ensures nonlytic transmission of mycobacteria, Proc. Natl. Acad. Sci. USA, 112, E687, 10.1073/pnas.1423318112 · DOI
- Starr, 2012, Selective subversion of autophagy complexes facilitates completion of the Brucella intracellular cycle, Cell Host Microbe, 11, 33, 10.1016/j.chom.2011.12.002 · DOI
- Takenouchi, 2009, The Activation of P2X7 Receptor Impairs Lysosomal Functions and Stimulates the Release of Autophagolysosomes in Microglial Cells, J. Immunol., 182, 2051, 10.4049/jimmunol.0802577 · DOI
- Chen, 2015, Phosphatidylserine vesicles enable efficient en bloc transmission of enteroviruses, Cell, 160, 619, 10.1016/j.cell.2015.01.032 · DOI
- Mutsafi, Y., and Altan-Bonnet, N. (2018). Enterovirus Transmission by Secretory Autophagy. Viruses, 10. · DOI
- Bird, 2014, Nonlytic viral spread enhanced by autophagy components, Proc. Natl. Acad. Sci. USA, 111, 13081, 10.1073/pnas.1401437111 · DOI
- Zhang, 2017, The Role of Secretory Autophagy in Zika Virus Transfer through the Placental Barrier, Front. Cell Infect. Microbiol., 6, 206, 10.3389/fcimb.2016.00206 · DOI
- Urbanelli, L., Buratta, S., Tancini, B., Sagini, K., Delo, F., Porcellati, S., and Emiliani, C. (2019). The Role of Extracellular Vesicles in Viral Infection and Transmission. Vaccines, 7. · DOI
- Nolte, 2016, Extracellular vesicles and viruses: Are they close relatives?, Proc. Natl. Acad. Sci. USA, 113, 9155, 10.1073/pnas.1605146113 · DOI
- Clevers, 2013, Paneth cells: Maestros of the small intestinal crypts, Ann. Rev. Physiol., 75, 289, 10.1146/annurev-physiol-030212-183744 · DOI
- Klionsky, 2018, Secretory autophagy holds the key to lysozyme secretion during bacterial infection of the intestine, Autophagy, 14, 365, 10.1080/15548627.2017.1401425 · DOI
- Kong, 2014, Parkinson’s disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes, Hum. Mol. Genet., 23, 2816, 10.1093/hmg/ddu099 · DOI
- Poehler, 2014, Autophagy modulates SNCA/α-synuclein release, thereby generating a hostile microenvironment, Autophagy, 10, 2171, 10.4161/auto.36436 · DOI · Paper page
- Ejlerskov, 2013, Tubulin polymerization-promoting protein (TPPP/p25alpha) promotes unconventional secretion of alpha-synuclein through exophagy by impairing autophagosomelysosome fusion, J. Biol. Chem., 288, 17313, 10.1074/jbc.M112.401174 · DOI
- Lee, 2013, Autophagic failure promotes the exocytosis and intercellular transfer of α-synuclein, Exp. Mol. Med., 45, e22, 10.1038/emm.2013.45 · DOI
- Yuyama, 2017, Exosomes as Carriers of Alzheimer’s Amyloid-ß, Front. Neurosci., 11, 229, 10.3389/fnins.2017.00229 · DOI
- Tian, 2011, A small-molecule enhancer of autophagy decreases levels of Aβ and APP-CTF via Atg5-dependent autophagy pathway, FASEB J., 25, 1934, 10.1096/fj.10-175158 · DOI
- Kang, 2019, Autophagy-Mediated Secretory Pathway is Responsible for Both Normal and Pathological Tau in Neurons, J. Alzheimers Dis., 70, 667, 10.3233/JAD-190180 · DOI
- Son, 2016, Insulin-degrading enzyme secretion from astrocytes is mediated by an autophagy-based unconventional secretory pathway in Alzheimer disease, Autophagy, 12, 784, 10.1080/15548627.2016.1159375 · DOI
- Duran, 2010, Unconventional secretion of Acb1 is mediated by autophagosomes, J. Cell Biol., 188, 527, 10.1083/jcb.200911154 · DOI · Paper page
- Manjithaya, 2010, Role of autophagy in unconventional protein secretion, Autophagy, 6, 650, 10.4161/auto.6.5.12066 · DOI
- Kinseth, 2007, The Golgi-associated protein GRASP is required for unconventional protein secretion during development, Cell, 130, 524, 10.1016/j.cell.2007.06.029 · DOI
- Deretic, 2012, Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation, Trends Cell Biol., 22, 397, 10.1016/j.tcb.2012.04.008 · DOI
- Pilli, 2012, TBK-1 promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation, Immunity, 37, 223, 10.1016/j.immuni.2012.04.015 · DOI · Paper page
- Kimura, 2017, Dedicated SNAREs and specialized TRIM cargo receptors mediate secretory autophagy, EMBO J., 36, 42, 10.15252/embj.201695081 · DOI
- Shibutani, 2014, A current perspective of autophagosome biogenesis, Cell Res., 24, 58, 10.1038/cr.2013.159 · DOI
- Fader, 2009, TI-VAMP/VAMP7 and VAMP3/cellubrevin: Two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways, Biochim. Biophys. Acta, 1793, 1901, 10.1016/j.bbamcr.2009.09.011 · DOI
- Bader, 2015, Atg9 is required for intraluminal vesicles in amphisomes and autolysosomes, Biol. Open, 4, 1345, 10.1242/bio.013979 · DOI
- Chen, 2017, Exophagy of annexin A2 via RAB11, RAB8A and RAB27A in IFN-γ-stimulated lung epithelial cells, Sci. Rep., 7, 5676, 10.1038/s41598-017-06076-4 · DOI
- Griffiths, 2012, Maturing reticulocytes internalize plasma membrane in glycophorin A-containing vesicles that fuse with autophagosomes before exocytosis, Blood, 119, 6296, 10.1182/blood-2011-09-376475 · DOI
- Patel, 2013, Autophagy proteins control goblet cell function by potentiating reactive oxygen species production, EMBO J., 32, 3130, 10.1038/emboj.2013.233 · DOI
- Guo, 2017, Atg5 Disassociates the V1V0-ATPase to Promote Exosome Production and Tumor Metastasis Independent of Canonical Macroautophagy, Dev. Cell, 43, 716, 10.1016/j.devcel.2017.11.018 · DOI
- Murrow, 2015, ATG12-ATG3 interacts with Alix to promote basal autophagic flux and late endosome function, Nat. Cell Biol., 17, 300, 10.1038/ncb3112 · DOI
- Papandreou, 2017, Autophagy and the endo/exosomal pathways in health and disease, Biotechnol. J., 12, 1600175, 10.1002/biot.201600175 · DOI
Cited by
Sorted by citations
Autophagy and the hallmarks of aging
Kaushik, S., Tasset, I., Arias, E., Pampliega, O., Wong, E., Martinez-Vicente, M., & Cuervo, A. M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101468 · Cited by 285
The needs of a synapse—How local organelles serve synaptic proteostasis
Grochowska, K. M., Andres‐Alonso, M., Karpova, A., & Kreutz, M. R. (2022) · The EMBO Journal · doi:10.15252/embj.2021110057 · Cited by 38
Lysosomal Functions in Glia Associated with Neurodegeneration
Kreher, C., Favret, J., Maulik, M., & Shin, D. (2021) · Biomolecules · doi:10.3390/biom11030400 · Cited by 38
Krause, G. J., Diaz, A., Jafari, M., Khawaja, R. R., Agullo‐Pascual, E., Santiago‐Fernández, O., Richards, A. L., Chen, K., Dmitriev, P., Sun, Y., et al. (2022) · Aging Cell · doi:10.1111/acel.13713 · Cited by 35
The Alzheimer's Disease Gene SORL1 Regulates Lysosome Function in Human Microglia
Mishra, S., Morshed, N., Sidhu, S. B., Kinoshita, C., Stevens, B., Jayadev, S., & Young, J. E. (2025) · Glia · doi:10.1002/glia.70009 · Cited by 31
Yu, X., Elfimova, N., Müller, M., Bachurski, D., Koitzsch, U., Drebber, U., Mahabir, E., Hansen, H. P., Friedman, S. L., Klein, S., et al. (2022) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2022.02.013 · Cited by 27
Hu, Z., Chen, G., Yan, C., Li, Z., Wu, T., Li, L., & Zhang, S. (2023) · Environmental Toxicology · doi:10.1002/tox.23795 · Cited by 18
VPS34 in Autophagy, Cancer and Cancer Therapy
Bartolini, E., Janji, B., & Gao, R. (2026) · doi:10.20944/preprints202603.0323.v1 · Cited by 1
Metadata
- Authors
- Buratta, S., Tancini, B., Sagini, K., Delo, F., Chiaradia, E., Urbanelli, L., & Emiliani, C.
- Affiliations
- Department of Chemistry, Biology and Biotechnology, University of Perugia, Via del Giochetto, 06123 Perugia, Italy
- Department of Veterinary Medicine, University of Perugia, Via S. Costanzo 4, 06126 Perugia, Italy
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2020-04-08
- Volume
- 21
- Issue
- 7
- Pages
- 2576
- ISSN
- 1422-0067
- PMC
- PMC7178086
- Cited by
- 446
- References
- 19
- Language
- en
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