The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets
Open accessAbstract
Macroautophagy is an intracellular degradation system by which cytoplasmic materials are enclosed by the autophagosome and delivered to the lysosome. Autophagosome formation is considered to take place on the endoplasmic reticulum and involves functions of autophagy-related (Atg) proteins. Here, we report the identification and characterization of mammalian Atg2 homologues Atg2A and Atg2B. Simultaneous silencing of Atg2A and Atg2B causes a block in autophagic flux and accumulation of unclosed autophagic structures containing most Atg proteins. Atg2A localizes on the autophagic membrane, as well as on the surface of lipid droplets. The Atg2A region containing amino acids 1723–1829, which shows relatively high conservation among species, is required for localization to both the autophagic membrane and lipid droplet and is also essential for autophagy. Depletion of both Atg2A and Atg2B causes clustering of enlarged lipid droplets in an autophagy-independent manner. These data suggest that mammalian Atg2 proteins function both in autophagosome formation and regulation of lipid droplet morphology and dispersion.
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.
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
Autophagy regulates lipid metabolism
Singh, R., Kaushik, S., Wang, Y., Xiang, Y., Novak, I., Komatsu, M., Tanaka, K., Cuervo, A. M., & Czaja, M. J. (2009) · Nature · doi:10.1038/nature07976 · Cited by 3,975
Autophagy in immunity and inflammation
Levine, B., Mizushima, N., & Virgin, H. W. (2011) · Nature · doi:10.1038/nature09782 · Cited by 3,289
Self-citationThe Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978
Self-citationThe role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Self-citationAutophagy in mammalian development and differentiation
Mizushima, N., & Levine, B. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-823 · Cited by 1,555
Self-citationNetwork organization of the human autophagy system
Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554
Beclin 1 Forms Two Distinct Phosphatidylinositol 3-Kinase Complexes with Mammalian Atg14 and UVRAG
Itakura, E., Kishi, C., Inoue, K., & Mizushima, N. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-01-0080 · Cited by 1,176
Self-citationMizushima, N., Kuma, A., Kobayashi, Y., Yamamoto, A., Matsubae, M., Takao, T., Natsume, T., Ohsumi, Y., & Yoshimori, T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00381 · Cited by 791
Self-citationAutophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L
Matsunaga, K., Morita, E., Saitoh, T., Akira, S., Ktistakis, N. T., Izumi, T., Noda, T., & Yoshimori, T. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911141 · Cited by 456
Itakura, E., Kishi-Itakura, C., Koyama-Honda, I., & Mizushima, N. (2012) · Journal of Cell Science · doi:10.1242/jcs.094110 · Cited by 286
Self-citation
Cited by
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
Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
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 2,897
Self-citationAutophagy in healthy aging and disease
Aman, Y., Schmauck-Medina, T., Hansen, M., Morimoto, R. I., Simon, A. K., Bjedov, I., Palikaras, K., Simonsen, A., Johansen, T., Tavernarakis, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00098-4 · Cited by 1,313
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134
Nguyen, T. N., Padman, B. S., Usher, J., Oorschot, V., Ramm, G., & Lazarou, M. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201607039 · Cited by 668
Saitsu, H., Nishimura, T., Muramatsu, K., Kodera, H., Kumada, S., Sugai, K., Kasai-Yoshida, E., Sawaura, N., Nishida, H., Hoshino, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2562 · Cited by 474
Self-citationGalectin-3 Coordinates a Cellular System for Lysosomal Repair and Removal
Jia, J., Claude-Taupin, A., Gu, Y., Choi, S. W., Peters, R., Bissa, B., Mudd, M. H., Allers, L., Pallikkuth, S., Lidke, K. A., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2019.10.025 · Cited by 434
An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
Takahashi, Y., He, H., Tang, Z., Hattori, T., Liu, Y., Young, M. M., Serfass, J. M., Chen, L., Gebru, M., Chen, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05254-w · Cited by 381
Miao, G., Zhao, H., Li, Y., Ji, M., Chen, Y., Shi, Y., Bi, Y., Wang, P., & Zhang, H. (2021) · Developmental Cell · doi:10.1016/j.devcel.2020.12.010 · Cited by 354
“A1 treatment, RFP-LC3 puncta remained largely fluorescent upon treatment with PK in control and ORF3a-expressing cells (Figures 1Q, 1R, and 1T), while the signal disappeared in Atg2A/B KD cells, in which isolation membranes cannotproceed toautophagosomes (Velikkakath et al., 2012) (Figure 1S).”
BackgroundStavoe, A. K. H., & Holzbaur, E. L. F. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125242 · Cited by 328
Redundancy of human ATG4 protease isoforms in autophagy and LC3/GABARAP processing revealed in cells
Agrotis, A., Pengo, N., Burden, J. J., & Ketteler, R. (2019) · Autophagy · doi:10.1080/15548627.2019.1569925 · Cited by 255
Regulation of mammalian autophagy by class II and III PI 3-kinases through PI3P synthesis
Devereaux, K., Dall’Armi, C., Alcazar-Roman, A., Ogasawara, Y., Zhou, X., Wang, F., Yamamoto, A., De Camilli, P., & Di Paolo, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076405 · Cited by 182
Lipid droplets and steroidogenic cells
Shen, W.-J., Azhar, S., & Kraemer, F. B. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.11.024 · Cited by 175
How and why to study autophagy in Drosophila: It’s more than just a garbage chute
Nagy, P., Varga, Á., Kovács, A. L., Takáts, S., & Juhász, G. (2015) · Methods · doi:10.1016/j.ymeth.2014.11.016 · Cited by 115
Crosstalk between apoptosis and autophagy signaling pathways
(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2020.01.003 · Cited by 92
VMP1 Establishes ER-Microdomains that Regulate Membrane Contact Sites and Autophagy
Tábara, L.-C., & Escalante, R. (2016) · PLOS ONE · doi:10.1371/journal.pone.0166499 · Cited by 89
Lipids and membrane-associated proteins in autophagy
Li, L., Tong, M., Fu, Y., Chen, F., Zhang, S., Chen, H., Ma, X., Li, D., Liu, X., & Zhong, Q. (2021) · Protein & Cell · doi:10.1007/s13238-020-00793-9 · Cited by 88
Expression of WIPI2B counteracts age-related decline in autophagosome biogenesis in neurons
Stavoe, A. K., Gopal, P. P., Gubas, A., Tooze, S. A., & Holzbaur, E. L. (2019) · eLife · doi:10.7554/elife.44219 · Cited by 82
Role of VPS13, a protein with similarity to ATG2, in physiology and disease
Ugur, B., Hancock-Cerutti, W., Leonzino, M., & De Camilli, P. (2020) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2020.05.027 · Cited by 73
Autophagy in metabolism and quality control: opposing, complementary or interlinked functions?
Deretic, V., & Kroemer, G. (2022) · Autophagy · doi:10.1080/15548627.2021.1933742 · Cited by 71
Excess sphingomyelin disturbs ATG9A trafficking and autophagosome closure
Corcelle-Termeau, E., Vindeløv, S. D., Hämälistö, S., Mograbi, B., Keldsbo, A., Bräsen, J. H., Favaro, E., Adam, D., Szyniarowski, P., Hofman, P., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1159378 · Cited by 64
Castro, I. G., Shortill, S. P., Dziurdzik, S. K., Cadou, A., Ganesan, S., Valenti, R., David, Y., Davey, M., Mattes, C., Thomas, F. B., et al. (2022) · eLife · doi:10.7554/elife.74602 · Cited by 60
The Implications of Autophagy in Alzheimer’s Disease
Hamano, T., Hayashi, K., Shirafuji, N., & Nakamoto, Y. (2018) · Current Alzheimer Research · doi:10.2174/1567205015666181004143432 · Cited by 57
Lipid droplets as signaling platforms linking metabolic and cellular functions
Arrese, E. L., Saudale, F. Z., & Soulages, J. L. (2014) · Lipid Insights · doi:10.4137/lpi.s11128 · Cited by 54
A mutation in the major autophagy gene, WIPI2, associated with global developmental abnormalities
Jelani, M., Dooley, H. C., Gubas, A., Mohamoud, H. S. A., Khan, M. T. M., Ali, Z., Kang, C., Rahim, F., Jan, A., Vadgama, N., et al. (2019) · Brain · doi:10.1093/brain/awz075 · Cited by 48
Neuronal Autophagy: Regulations and Implications in Health and Disease
Liénard, C., Pintart, A., & Bomont, P. (2024) · Cells · doi:10.3390/cells13010103 · Cited by 44
Defective proteostasis in induced pluripotent stem cell models of frontotemporal lobar degeneration
Mahali, S., Martinez, R., King, M., Verbeck, A., Harari, O., Benitez, B. A., Horie, K., Sato, C., Temple, S., & Karch, C. M. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02274-5 · Cited by 33
Emerging roles of ATG9/ATG9A in autophagy: implications for cell and neurobiology
Choi, J., Jang, H., Xuan, Z., & Park, D. (2024) · Autophagy · doi:10.1080/15548627.2024.2384349 · Cited by 28
Spartin-mediated lipid transfer facilitates lipid droplet turnover
Wan, N., Hong, Z., Parson, M. A. H., Korfhage, J. L., Burke, J. E., Melia, T. J., & Reinisch, K. M. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314093121 · Cited by 22
Luhr, M., Szalai, P., & Engedal, N. (2018) · Journal of Visualized Experiments · doi:10.3791/57971 · Cited by 7
Metadata
- Authors
- Velikkakath, A. K. G., Nishimura, T., Oita, E., Ishihara, N., & Mizushima, N.
- Venue
- Molecular Biology of the Cell
- Published
- 2012-03
- Volume
- 23
- Issue
- 5
- Pages
- 896-909
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2150723052
- Cited by
- 430
- References
- 11
- FWCI
- 15.94
- Type
- journal article
- Language
- en
- Open access
- green
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.