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Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1–phosphatidylinositol-3-kinase complex
Open accessAbstract
Beclin 1, a mammalian autophagy protein that has been implicated in development, tumour suppression, neurodegeneration and cell death, exists in a complex with Vps34, the class III phosphatidylinositol-3-kinase (PI(3)K) that mediates multiple vesicle-trafficking processes including endocytosis and autophagy. However, the precise role of the Beclin 1-Vps34 complex in autophagy regulation remains to be elucidated. Combining mouse genetics and biochemistry, we have identified a large in vivo Beclin 1 complex containing the known proteins Vps34, p150/Vps15 and UVRAG, as well as two newly identified proteins, Atg14L (yeast Atg14-like) and Rubicon (RUN domain and cysteine-rich domain containing, Beclin 1-interacting protein). Characterization of the new proteins revealed that Atg14L enhances Vps34 lipid kinase activity and upregulates autophagy, whereas Rubicon reduces Vps34 activity and downregulates autophagy. We show that Beclin 1 and Atg14L synergistically promote the formation of double-membraned organelles that are associated with Atg5 and Atg12, whereas forced expression of Rubicon results in aberrant late endosomal/lysosomal structures and impaired autophagosome maturation. We hypothesize that by forming distinct protein complexes, Beclin 1 and its binding proteins orchestrate the precise function of the class III PI(3)K in regulating autophagy at multiple steps.
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In the citing paper
“Yeast Atg14 is the autophagy-specific subunit of the Vps34 complex I, 404 and a human homolog, named ATG14 (ATG14L/BARKOR), has been identified.[405][406][407][408]”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [406]
Experimental — accuracy not yet measuredIn the citing paper
“the class III phosphoinositide 3-kinase (PI3K) complex regulates vesicle nucleation and phagophore formation”
From Autophagy in kidney homeostasis and disease (2020) · cites this paper as [10]
In the citing paper
“Defects in induction, maturation, or lysosomal clearance impair protein degradation (Zhong et al. 2009), (Pickford et al. 2008), (Ravikumar et al. 2005), (Webb et al. 2004), (Iwata et al. 2005), (Kimura et al. 2008), (Wong and Cuervo 2010), (Lee et al. 2010), and is assessable via LC3-II turnover or p62 degradation (Mizushima et al. 2010), (Ju et al. 2010), (Klionsky et al. 2008b), (Tanida et al.”
From TMEM55B downregulation promotes neurodegeneration in Alzheimer’s disease models (2026) · cites this paper as Zhong et al. 2009
In the citing paper
“Detection of endogenous phospho-ATG16L1 [823] has been demonstrated as a novel method to monitor autophagy induction.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [823]
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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347
Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene
Qu, X., Yu, J., Bhagat, G., Furuya, N., Hibshoosh, H., Troxel, A., Rosen, J., Eskelinen, E.-L., Mizushima, N., Ohsumi, Y., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci20039 · Cited by 2,311
A ubiquitin-like system mediates protein lipidation
Ichimura, Y., Kirisako, T., Takao, T., Satomi, Y., Shimonishi, Y., Ishihara, N., Mizushima, N., Tanida, I., Kominami, E., Ohsumi, M., et al. (2000) · Nature · doi:10.1038/35044114 · Cited by 2,139
Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice.
Komatsu, M., Waguri, S., Koike, M., Sou, Y.-S., Ueno, T., Hara, T., Mizushima, N., Iwata, J.-I., Ezaki, J., Murata, S., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.035 · Cited by 2,124
Self-citationYue, Z., Jin, S., Yang, C., Levine, A. J., & Heintz, N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436255100 · Cited by 2,116
Self-citationLC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
Kabeya, Y., Mizushima, N., Yamamoto, A., Oshitani-Okamoto, S., Ohsumi, Y., & Yoshimori, T. (2004) · Journal of Cell Science · doi:10.1242/jcs.01131 · Cited by 1,394
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Li, Y., Guo, T., Zhang, Z., Yao, Y., Chang, S., Nor, J. E., Clarkson, B. H., Ni, L., & Liu, J. (2016) · Journal of Dental Research · doi:10.1177/0022034516636852 · Cited by 23
Peptide inhibition of p22phox and Rubicon interaction as a therapeutic strategy for septic shock
Kim, Y.-R., Koh, H.-J., Kim, J., Yun, J.-S., Jang, K., Lee, J., Jung, J. U., & Yang, C. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.05.046 · Cited by 23
Shiozaki, Y., Miyazaki‐Anzai, S., Okamura, K., Keenan, A. L., Masuda, M., & Miyazaki, M. (2020) · iScience · doi:10.1016/j.isci.2020.101105 · Cited by 25
Pathogenic Single Nucleotide Polymorphisms on Autophagy-Related Genes
Tamargo‐Gómez, I., Fernández, Á. F., & Mariño, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218196 · Cited by 24
Regulation of innate immunity by the molecular machinery of macroautophagy
Münz, C. (2014) · Cellular Microbiology · doi:10.1111/cmi.12358 · Cited by 23
Autophagy and Mechanisms of Effective Immunity
Mintern, J. D., & Villadangos, J. A. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00060 · Cited by 25
Kim, C., & Bergelson, J. M. (2013) · Journal of Virology · doi:10.1128/jvi.02706-13 · Cited by 23
Ktistakis, N. T., Manifava, M., Schoenfelder, P., & Rotondo, S. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110684 · Cited by 23
Adipose tissue autophagy and homeostasis in alcohol-induced liver injury
Li, Y., & Ding, W. (2017) · Liver Research · doi:10.1016/j.livres.2017.03.004 · Cited by 23
Novel Role of vBcl2 in the Virion Assembly of Kaposi's Sarcoma-Associated Herpesvirus
Liang, Q., Wei, D., Chung, B., Brulois, K., Guo, C.-R., Dong, S., Gao, S., Feng, P., Liang, C., & Jung, J. U. (2017) · Journal of Virology · doi:10.1128/jvi.00914-17 · Cited by 25
Ming, K., Yuan, W., Chen, Y., Du, H., He, M., Hu, Y., Wang, D., Wu, Y., & Liu, J. (2018) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2018.12.035 · Cited by 23
Zhang, H., Xie, S., & Deng, W. (2024) · Biomolecules · doi:10.3390/biom14121614 · Cited by 22
Guo, L., Xu, J., & Mo, X. (2012) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3533 · Cited by 22
ER-mitochondrial contact protein Miga regulates autophagy through Atg14 and Uvrag
Xu, L., Qiu, Y., Wang, X., Shang, W., Bai, J., Shi, K., Liu, H., Liu, J., Wang, L., & Tong, C. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111583 · Cited by 22
Acetylation modification in the regulation of macroautophagy
Huang, L., & Guo, H. (2024) · Advanced Biotechnology · doi:10.1007/s44307-024-00027-7 · Cited by 24
Liu, Z., & Huang, S. (2015) · Cancer Cell International · doi:10.1186/s12935-015-0165-5 · Cited by 23
Yang, M., Ramanathan, A., Glover, K., Stanley, C. B., Sanishvili, R., Chakravarthy, S., Yang, Z., Colbert, C. L., & Sinha, S. C. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01264 · Cited by 21
Autophagy – molecular mechanism, apoptosis and cancer
Polewska, J. (2012) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/17322693.1021109 · Cited by 22
Batool, S., Joseph, T. P., Hussain, M., Vuai, M. S., Khinsar, K. H., Din, S. R. U., Padhiar, A. A., Zhong, M., Ning, A., Zhang, W., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102986 · Cited by 22
Diao, C., Wang, L., Liu, H., Du, Y., & Xiuheng, L. (2019) · Clinical Interventions in Aging · doi:10.2147/cia.s197444 · Cited by 22
Autophagy in endothelial cells regulates their haematopoiesis-supporting ability
Lyu, Z., Cao, X.-N., Wen, Q., Mo, X., Zhao, H., Chen, Y., Wang, Y., Chang, Y., Xu, L., Zhang, X., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.102677 · Cited by 22
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Kaur, N., Raja, R., Ruiz‐Velasco, A., & Liu, W. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.585309 · Cited by 24
Antonell, A., Lladó, A., Sánchez‐Valle, R., Sanfeliu, C., Casserras, T., Rami, L., Muñoz‐García, C., Dangla-Valls, A., Balasa, M., Boya, P., et al. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9483-9 · Cited by 22
Rajendran, P., Renu, K., Ali, E. M., Genena, M. A. M., Veeraraghavan, V., Sekar, R., Sekar, A. K., Tejavat, S., Barik, P., & Abdallah, B. M. (2024) · Immunity Inflammation and Disease · doi:10.1002/iid3.70041 · Cited by 29
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Zhang, J., Jinan, Z., & Chen, Y. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-024-06063-0 · Cited by 24
Membrane receptors cluster phosphatidylserine to activate LC3-associated phagocytosis
Boada-Romero, E., Guy, C. S., Palacios, G., Mari, L., Poudel, S., Li, Z., Sharma, P., & Green, D. R. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01749-z · Cited by 28
SIRT2-PFKP interaction dysregulates phagocytosis in macrophages with acute ethanol-exposure
Anugraha, G., Roychowdhury, S., Kibler, C. D., Cross, E., Abraham, S., Bellar, A., Nagy, L. E., Scheraga, R. G., & Vachharajani, V. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1079962 · Cited by 23
Liu, T., Yang, P., Chen, H., Huang, Y., Liu, Y., Waqas, Y., Ahmed, N., Chu, X., & Chen, Q. (2016) · Scientific Reports · doi:10.1038/srep33296 · Cited by 22
Santarelli, R., Granato, M., Faggioni, A., & Cirone, M. (2015) · Journal of Immunology Research · doi:10.1155/2015/546063 · Cited by 21
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Campisi, D., Hawkins, N., Bonjour, K., & Wollert, T. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169138 · Cited by 22
Mitochondrial damage triggers the concerted degradation of negative regulators of neuronal autophagy
Basak, B., & Holzbaur, E. L. F. (2025) · Nature Communications · doi:10.1038/s41467-025-62379-5 · Cited by 22
Critical Role for Phosphatidylinositol-3 Kinase Vps34/PIK3C3 in ON-Bipolar Cells
He, F., Nichols, R. M., Kailasam, L., Wensel, T. G., & Agosto, M. A. (2019) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.19-26586 · Cited by 20
Genome-wide CRISPR screening reveals nucleotide synthesis negatively regulates autophagy
Mimura, K., Sakamaki, J.-I., Morishita, H., Kawazu, M., Mano, H., & Mizushima, N. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100780 · Cited by 20
Yang, Q., Qiu, X., Zhang, X., Yu, Y., Li, N., Wei, X., Feng, G., Li, Y., Zhao, Y., & Wang, R. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00870 · Cited by 21
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Zhang, R., Lin, H., You, Q., Zhang, Z., Bai, L., Chen, F., Zhu, X., Zhang, Z., & Li, Y. (2022) · Journal of Virology · doi:10.1128/jvi.01375-22 · Cited by 22
Tran, S. H., Juliani, J., Fairlie, W. D., & Lee, E. F. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221300 · Cited by 21
UVRAG cooperates with cargo receptors to assemble the ER‐phagy site
Qian, X., He, L., Yang, J., Sun, J., Peng, X., Zhang, Y., Mao, Y., Zhang, Y., & Cui, Y. (2023) · The EMBO Journal · doi:10.15252/embj.2023113625 · Cited by 19
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He, L., Eslamfam, S., Ma, X., & Li, D. (2016) · Frontiers of Agricultural Science and Engineering · doi:10.15302/j-fase-2016106 · Cited by 20
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Martinez, J., & Cook, D. N. (2021) · Trends in Immunology · doi:10.1016/j.it.2021.08.004 · Cited by 19
Lin, C., Li, L., Xu, Q., Xu, S., & Tang, C. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03344-5 · Cited by 19
Autophagy as a dual-faced host response to viral infections
Zhai, H., Wang, T., Liu, D., Pan, L., Sun, Y., & Qiu, H. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1289170 · Cited by 21
Martyniszyn, L., Szulc‐Dąbrowska, L., Boratyńska-Jasińska, A., Struzik, J., Winnicka, A., & Niemiałtowski, M. (2013) · Viral Immunology · doi:10.1089/vim.2013.0003 · Cited by 19
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Nakajima, S., Aikawa, C., Nozawa, T., Minowa‐Nozawa, A., Toh, H., & Nakagawa, I. (2017) · PLoS ONE · doi:10.1371/journal.pone.0170138 · Cited by 20
Yu, Y., Yang, L., Han, S., Wu, Y., Liu, L., Chang, Y., Wang, X., & Chai, J. (2018) · Shock · doi:10.1097/shk.0000000000001284 · Cited by 19
Beclin1 inhibition enhances paclitaxel‑mediated cytotoxicity in breast cancer in�vitro and in�vivo
Wu, C., Liu, J., Liu, Y., Wang, Y., Fu, K., Yu, X., Pu, Q., Chen, X., & Zhou, L. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4089 · Cited by 19
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Luo, S., Yang, M., Lv, D., Jing, L., Li, Y., Liu, Z., & Diao, A. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.05.004 · Cited by 18
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Nam, R. K., Benatar, T., Amemiya, Y., Sherman, C., & Seth, A. K. (2020) · Anticancer Research · doi:10.21873/anticanres.14689 · Cited by 18
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Münz, C. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.100987 · Cited by 18
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Münz, C. (2011) · Frontiers in Immunology · doi:10.3389/fimmu.2011.00042 · Cited by 19
Bostancıklıoğlu, M., Demiryürek, Ş., Cengiz, B., Demi̇r, T., Öztuzcu, S., Aras, M. H., Özsevik, A. S., Usumez, A., Ergün, S., Özbal, H. K., et al. (2015) · Lasers in Medical Science · doi:10.1007/s10103-015-1727-4 · Cited by 18
Yamada, K., Ito, M., Nunomura, H., Nishigori, T., Furuta, A., Yoshida, M., Yamaki, A., Shozu, K., Yasuda, I., Tsuda, S., et al. (2025) · Antioxidants · doi:10.3390/antiox14080919 · Cited by 17
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Gordon, R. A., Giannouli, C. C., Raparia, C., Bastacky, S., Marinov, A. D., Hawse, W. F., Cattley, R. T., Tilstra, J. S., Campbell, A. M., Nickerson, K. M., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.155537 · Cited by 15
Zhou, C., Dong, X., Wang, M., Qian, X., Hu, M., Liang, K., Liang, Y., Zhang, R., Huang, Y., Lyu, H., et al. (2022) · Cell Insight · doi:10.1016/j.cellin.2022.100045 · Cited by 15
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Shizukuishi, S., Ogawa, M., Matsunaga, S., Tomokiyo, M., Ikebe, T., Fushinobu, S., Ryo, A., & Ohnishi, M. (2020) · EMBO Reports · doi:10.15252/embr.201949232 · Cited by 17
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Qu, Y., Wang, X., Zhu, Y., Wang, Y., Yang, X., Hu, G., Liu, C., Li, J., Ren, S., Xiao, Z., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.12.380709 · Cited by 16
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Ben‐Hur, S., Afar, S., Politi, Y., Gal, L., Golani, O., Sivan, E., Haffner‐Krausz, R., Maizenberg, E., Peretz, S., Roth, Z., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50041-5 · Cited by 17
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Din, S. R. U., Nisar, M. A., Ramzan, M. N., Saleem, M. Z., Ghayas, H., Ahmad, B., Batool, S., Kifayat, K., Guo, X., Huang, M., et al. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174305 · Cited by 15
Liu, B., Lu, Y., Zhang, T., Yu, X., Wang, Q., Chi, Y., Jin, S., & Cheng, G. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00720-3 · Cited by 17
Self-citationGao, X., Lin, H., Ray, R., & Ray, P. (2013) · Neurochemical Research · doi:10.1007/s11064-013-0996-1 · Cited by 15
AMBRA1-regulated autophagy in vertebrate development
Antonioli, M., Albiero, F., Fimia, G. M., & Piacentini, M. (2015) · The International Journal of Developmental Biology · doi:10.1387/ijdb.150057mp · Cited by 16
Cheng, X., Zhong, F., He, K., Sun, S., Chen, H., & Zhou, J. (2016) · Oncology Letters · doi:10.3892/ol.2016.5178 · Cited by 15
The multiple roles of viral 3D pol protein in picornavirus infections
Nie, Z., Zhai, F., Zhang, H., Zheng, H., & Pei, J. (2024) · Virulence · doi:10.1080/21505594.2024.2333562 · Cited by 14
The Core Molecular Machinery of Autophagosome Formation
Jin, M., & Klionsky, D. J. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6561-4_2 · Cited by 15
Spagnuolo, R. D., Brich, S., Bozzi, F., Conca, E., Castelli, C., Tazzari, M., Maestro, R., Brenca, M., Gualeni, A. V., Gloghini, A., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7523 · Cited by 14
Human Diversity in a Cell Surface Receptor that Inhibits Autophagy
Chaudhary, A., Leite, M., Kulasekara, B. R., Altura, M. A., Ogahara, C., Weiss, E. J., Fu, W., Blanc, M.-P., O’Keeffe, M., Terhorst, C., et al. (2016) · Current Biology · doi:10.1016/j.cub.2016.05.003 · Cited by 14
Sun, W., Dong, S., Lu, H., Wang, N., Zhao, Y. X., An, J., Sun, L., & Lu, D. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110008 · Cited by 14
Hou, C., Lu, S., Su, Y., Ding, D., Tao, L., Wang, M., Wang, Y., & Liu, X. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112721 · Cited by 14
Autophagy, a Novel Pathway to Regulate Calcium Mobilization in T Lymphocytes
Jia, W., He, M., McLeod, I. X., & He, Y.-W. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00179 · Cited by 14
Autophagy as a pharmacological target in hematopoiesis and hematological disorders
Orsini, M., Morceau, F., Dicato, M. A., & Diederich, M. F. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.04.007 · Cited by 14
Moussa, C. E.-H. (2015) · Neurodegenerative Diseases · doi:10.1159/000430888 · Cited by 13
Vps21 Directs the PI3K-PI(3)P-Atg21-Atg16 Module to Phagophores via Vps8 for Autophagy
Zhao, L. Q., You, W., Sun, D., Xu, H., You, X., Xu, H., Wu, Z., Xie, Z., & Liang, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179550 · Cited by 13
Understanding the molecular regulatory mechanisms of autophagy in lung disease pathogenesis
Lin, L., Lin, Y., Han, Z., Wang, K., Zhou, S., Wang, Z., Wang, S., & Chen, H. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1460023 · Cited by 13
Yeganeh, B., Jäger, R., Gorman, A. M., Samali, A., & Ghavami, S. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801043-3.00005-4 · Cited by 17
The kinetics of autophagy in the lung following acute spinal cord injury in rats
Chu, R., Wang, J., Bi, Y., & Nan, G. (2018) · The Spine Journal · doi:10.1016/j.spinee.2018.01.001 · Cited by 13
miR-181b-5p suppresses starvation-induced cardiomyocyte autophagy by targeting Hspa5
Chang, L., Chai, X., Chen, P., Cao, J., Xie, H., & Zhu, J. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3988 · Cited by 12
Metadata
- Authors
- Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z.
- Affiliations
- Howard Hughes Medical Institute (US)
- Rockefeller University (US)
- Icahn School of Medicine at Mount Sinai (US)
- Albert Einstein College of Medicine (US)
- Corresponding author
- Yue, Zhenyu
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2009-03-08
- Volume
- 11
- Issue
- 4
- Pages
- 468-476
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC2664389
- OpenAlex
- W1983831622
- Cited by
- 1,005
- References
- 35
- Citations by year
- 2026: 29 · 2025: 43 · 2024: 38 · 2023: 48 · 2022: 63 · 2021: 62 · 2020: 69 · 2019: 51 · 2018: 57 · 2017: 58 · 2016: 72 · 2015: 56 · 2014: 64 · 2013: 77 · 2012: 64
- FWCI
- 49.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Public Health Service (RNS055683A)
- National Institute of Neurological Disorders and Stroke (R21NS055683, R01NS060123)
- National Center for Research Resources (RR00862, P41RR000862, RR 022220, U54RR022220)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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 › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- autophagy regulation, Beclin-1, ATG14L, Rubicon, Vps34, class III phosphatidylinositol 3-kinase, UVRAG, autophagosome maturation, late endosomes, lysosomes, ATG5, ATG12, lipid kinase activity
- MeSH terms
- Beclin-1, Amino Acid Sequence, Animals, Autophagy, Cell Membrane, HeLa Cells, Humans, Lysosomes, Molecular Sequence Data, Protein Binding, Proteins, Endosomes, Phosphatidylinositol Phosphates, Phosphatidylinositol 3-Kinases, NIH 3T3 Cells, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Apoptosis Regulatory Proteins, Mice
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