The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK
Abstract
Macroautophagy (herein referred to as autophagy) is an evolutionarily conserved self-digestive process cells adapt to starvation and other stress responses. Upon starvation, autophagy is induced, providing cells with needed nutrient supplies. We report here that Unc-51-like kinase 1 (Ulk1), a key initiator for mammalian autophagy, undergoes dramatic dephosphorylation upon starvation, particularly at serine 638 and serine 758. Phosphorylations of Ulk1 are mediated by mammalian target-of-rapamycin (mTOR) kinase and adenosine monophosphate activated protein kinase (AMPK). AMPK interacts with Ulk1 in a nutrient-dependent manner. Proper phosphorylations on Ulk1 are crucial for Ulk1/AMPK association, as a single serine-to-alanine mutation (S758A) at Ulk1 impairs this interaction. Compared to the wild-type ULK1, this Ulk1-S758A mutant initiates starvation-induced autophagy faster at an early time point, but does not alter the maximum capacity of autophagy when starvation prolongs. This study therefore revealed previously unnoticed acute autophagy response to environmental changes.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
AMPK inhibits MTORC1 by phosphorylating and activating TSC2, as well as by phosphorylating the MTOR binding partner RPTOR.
“AMPK inhibits MTORC1 by phosphorylating and activating TSC2 [687], as well as by phosphorylating the MTOR binding partner RPTOR [688].”
From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [688]
Citations
Cites
Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
Regulation mechanisms and signaling pathways of autophagy
He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609
Nutrient-dependent mTORC1 Association with the ULK1–Atg13–FIP200 Complex Required for Autophagy
Hosokawa, N., Hara, T., Kaizuka, T., Kishi, C., Takamura, A., Miura, Y., Iemura, S.-I., Natsume, T., Takehana, K., Yamada, N., et al. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1248 · Cited by 2,076
Autophagy in mammalian development and differentiation
Mizushima, N., & Levine, B. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-823 · Cited by 1,555
The role of the Atg1/ULK1 complex in autophagy regulation
Mizushima, N. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.12.004 · Cited by 1,062
The Association of AMPK with ULK1 Regulates Autophagy
Lee, J. W., Park, S., Takahashi, Y., & Wang, H.-G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015394 · Cited by 482
Flagged first, then by citations
Research works printed but not linked: 13
- 10.1038/nrm2708 · DOI
- 10.1242/dev.016105 · DOI
- 10.1101/gad.1599207 · DOI
- 10.1083/jcb.150.6.1507 · DOI · Paper page
- 10.1128/MCB.01344-09 · DOI
- 10.1128/MCB.01082-08 · DOI · Paper page
- 10.1091/mbc.e08-12-1250 · DOI
- 10.1074/jbc.M900573200 · DOI · Paper page
- 10.4161/auto.5.7.9296 · DOI
- 10.1091/mbc.e08-12-1249 · DOI · Paper page
- 10.4161/auto.5.5.8249 · DOI
- 10.1038/nature09204 · DOI · Paper page
- 10.1002/jcp.1041190120 · DOI
Cited by
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
Self-citationGuidelines for the use and interpretation of assays for monitoring autophagy
Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996
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
The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
Mihaylova, M. M., & Shaw, R. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2329 · Cited by 2,923
Guidelines 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-citationAn Overview of Autophagy: Morphology, Mechanism, and Regulation
Parzych, K. R., & Klionsky, D. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5371 · Cited by 2,521
Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks
Alers, S., Löffler, A. S., Wesselborg, S., & Stork, B. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06159-11 · Cited by 1,483
Laker, R. C., Drake, J. C., Wilson, R. J., Lira, V. A., Lewellen, B. M., Ryall, K. A., Fisher, C. C., Zhang, M., Saucerman, J. J., Goodyear, L. J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00520-9 · Cited by 529
Huntingtin functions as a scaffold for selective macroautophagy
Rui, Y.-N., Xu, Z., Patel, B., Chen, Z., Chen, D., Tito, A., David, G., Sun, Y., Stimming, E. F., Bellen, H. J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3101 · Cited by 423
Autophagy in bone homeostasis and the onset of osteoporosis
Yin, X., Zhou, C., Li, J., Liu, R., Shi, B., Yuan, Q., & Zou, S. (2019) · Bone Research · doi:10.1038/s41413-019-0058-7 · Cited by 235
Regulation of autophagy by coordinated action of mTORC1 and protein phosphatase 2A
Wong, P.-M., Feng, Y., Wang, J., Shi, R., & Jiang, X. (2015) · Nature Communications · doi:10.1038/ncomms9048 · Cited by 239
A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy
Yang, M., Liang, C., Swaminathan, K., Herrlinger, S., Lai, F., Shiekhattar, R., & Chen, J.-F. (2016) · Science Advances · doi:10.1126/sciadv.1601167 · Cited by 238
Allosteric post-translational modification codes
Nussinov, R., Tsai, C.-J., Xin, F., & Radivojac, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.07.001 · Cited by 211
Fregno, I., Fasana, E., Bergmann, T. J., Raimondi, A., Loi, M., Soldà, T., Galli, C., D'Antuono, R., Morone, D., Danieli, A., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201899259 · Cited by 207
Yeo, E.-J. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0233-3 · Cited by 175
Podocytes maintain high basal levels of autophagy independent of mtor signaling
Bork, T., Liang, W., Yamahara, K., Lee, P., Tian, Z., Liu, S., Schell, C., Thedieck, K., Hartleben, B., Patel, K., et al. (2020) · Autophagy · doi:10.1080/15548627.2019.1705007 · Cited by 100
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
Salomäki, H., Vähätalo, L. H., Laurila, K., Jäppinen, N. T., Penttinen, A.-M., Ailanen, L., Ilyasizadeh, J., Pesonen, U., & Koulu, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056594 · Cited by 92
Autophagy in Pulmonary Diseases
Nakahira, K., Pabon Porras, M. A., & Choi, A. M. K. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201512-2468so · Cited by 78
HIF1α-dependent mitophagy facilitates cardiomyoblast differentiation
Zhao, J.-F., Rodger, C. E., Allen, G. F. G., Weidlich, S., & Ganley, I. G. (2020) · Cell Stress · doi:10.15698/cst2020.05.220 · Cited by 61
Shah, S. Z. A., Zhao, D., Hussain, T., & Yang, L. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.09.004 · Cited by 55
The contribution of altered neuronal autophagy to neurodegeneration
Filippone, A., Esposito, E., Mannino, D., Lyssenko, N., & Praticò, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108178 · Cited by 55
Castets, P., Frank, S., Sinnreich, M., & Rüegg, M. A. (2016) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-160153 · Cited by 49
Metadata
- Authors
- Shang, L., Chen, S., Du, F., Li, S., Zhao, L., & Wang, X.
- Affiliations
- Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390; and
- National Institute of Biological Sciences, Zhongguancun Life Science Park, Beijing 102206, China
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2011-03-07
- Volume
- 108
- Issue
- 12
- Pages
- 4788-4793
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 517
- References
- 6
- 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
