The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Control of autophagy initiation by phosphoinositide 3‐phosphatase jumpy
Open accessAbstract
The majority of studies on autophagy, a cytoplasmic homeostasis pathway of broad biological and medical significance, have been hitherto focused on the phosphatidylinositol 3-kinases as the regulators of autophagy. Here, we addressed the reverse process driven by phosphoinositide phosphatases and uncovered a key negative regulatory role in autophagy of a phosphatidylinositol 3-phosphate (PI3P) phosphatase Jumpy (MTMR14). Jumpy associated with autophagic isolation membranes and early autophagosomes, defined by the key factor Atg16 necessary for proper localization and development of autophagic organelles. Jumpy orchestrated orderly succession of Atg factors by controlling recruitment to autophagic membranes of the sole mammalian Atg factor that interacts with PI3P, WIPI-1 (Atg18), and by affecting the distribution of Atg9 and LC3, the two Atg factors controlling organization and growth of autophagic membranes. A catalytically inactive Jumpy mutant, R336Q, found in congenital disease centronuclear myopathy, lost the ability to negatively regulate autophagy. This work reports for the first time that initiation of autophagy is controlled not only by the forward reaction of generating PI3P through a lipid kinase but that its levels are controlled by a specific PI3P phosphatase, which when defective can lead to human 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?
In the citing paper
“Furthermore, mounting evidence shows that autophagy is regulated by distinct mechanisms in different cell types [11–26], and these cell type-specific mechanisms underlie the differential vulnerability of separate tissues to autophagy mutations, resulting in heterogenous manifestations of disease.”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [20]
In the citing paper
“For instance, centronuclear myopathy is caused by mutations in the genes encoding MTM1 (myotubularin1) or MTMR14/Jumpy (myotubularin related protein 14) [17,20].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [20]
In the citing paper
“These loss-of-function mutations prevent these enzymes from metabolizing phosphoinositides required for autophagy, thereby disinhibiting autophagy flux and muscle atrophy [17,20].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [20]
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 in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
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
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
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
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
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276
How to Interpret LC3 Immunoblotting
Mizushima, N., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4600 · Cited by 2,595 · cited 1×
“To discern whether LC3-II increase following Jumpy or MTMR6 knock-downs was due to autophagy stimulation or inhibition of LC3-II degradation, Bafilomycin A1 (BafA1) and lysosomal protease inhibitors were added during the 30-min treatment (Mizushima and Yoshimori, 2007).”
Kimura, S., Noda, T., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4451 · Cited by 2,278
Autophagosome formation: core machinery and adaptations
Xie, Z., & Klionsky, D. J. (2007) · Nature Cell Biology · doi:10.1038/ncb1007-1102 · Cited by 2,237
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
Cited by
Sorted by citations
Items 201–270 of 270
PI3P-dependent regulation of cell size and autophagy by phosphatidylinositol 5-phosphate 4-kinase
Ghosh, A., Venugopal, A., Shinde, D. D., Sharma, S., Krishnan, M., Mathre, S., Krishnan, H., Saha, S., & Raghu, P. (2023) · Life Science Alliance · doi:10.26508/lsa.202301920 · Cited by 12
Myotubularins and associated neuromuscular diseases
Tronchère, H., Bolino, A., Laporte, J., & Payrastre, B. (2012) · Clinical Lipidology · doi:10.2217/clp.12.7 · Cited by 13
Self-citationPhosphoinositides: Functions in autophagy-related stress responses
Claude‐Taupin, A., & Morel, É. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.158903 · Cited by 12
Recent advances of myotubularin-related (MTMR) protein family in cardiovascular diseases
Wang, J., Guo, W., Wang, Q., Yang, Y., & Sun, X. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2024.1364604 · Cited by 10
Yu, X., Ma, J., Lin, F. W., Zhao, W., Fu, X., & Zhao, Z. J. (2012) · BMC Cell Biology · doi:10.1186/1471-2121-13-28 · Cited by 10
Crosstalk between lipid droplets and autophagy in cancer: A nexus for therapeutic targeting
Li, X., Zhang, J., Luo, S., Yu, X., & Song, C. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.108023 · Cited by 9
MTMR4 Is Required for the Stability of the Salmonella-Containing Vacuole
Teo, W. X., Kerr, M. C., & Teasdale, R. D. (2016) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2016.00091 · Cited by 10
MTMR14 Alleviates Chronic Obstructive Pulmonary Disease as a Regulator in Inflammation and Emphysema
Gu, Y., Chen, J., Huang, Q., Zhan, Y., Wang, T., Wu, J., Zhao, J., Zeng, Z., Lv, Y., Xiao, C., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/9300269 · Cited by 9
In Vitro Characterization of VPS34 Lipid Kinase Inhibition by Small Molecules
Fassy, F., Dureuil, C., Lamberton, A., Mathieu, M., Michot, N., Ronan, B., & Pasquier, B. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.070 · Cited by 9
Targeting STAT3-mediated autophagy with small molecules in cancer treatment – A comprehensive review
Azad, S. M. A. K., Meem, J. N., Shaikat, A. H., Ali, M. L., Arif, M. S. R., Sabrin, S., Mostaq, M. S., Haque, M. R. U., Amin, M. N., & Mahmud, M. A. (2024) · Clinical Traditional Medicine and Pharmacology · doi:10.1016/j.ctmp.2024.200174 · Cited by 8
Molecular Mechanisms Controlling Skeletal Muscle Mass
Sakuma, K., & Yamaguchi, A. (2015) · InTech eBooks · doi:10.5772/60876 · Cited by 8
The autophagosome: current understanding of formation and maturation
Lane, J. D., & Mannack, L. (2015) · Research and Reports in Biochemistry · doi:10.2147/rrbc.s57405 · Cited by 8
Xiao, C., Qiu, S., Li, X., Luo, D., & Liu, G. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.053 · Cited by 8
NeuroHeal Reduces Muscle Atrophy and Modulates Associated Autophagy
Marmolejo-Martínez-Artesero, S., Romeo-Guitart, D., Mañas‐García, L., Barreiro, E., & Casas, C. (2020) · Cells · doi:10.3390/cells9071575 · Cited by 6
McLeod, I. X., Saxena, R., Carico, Z. M., & He, Y.-W. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.709398 · Cited by 6
Mass Assays to Quantify Bioactive PtdIns3P and PtdIns5P During Autophagic Responses
Viaud, J., Chicanne, G., Solinhac, R., Hnia, K., Gaits‐Iacovoni, F., & Payrastre, B. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.061 · Cited by 6
Autophagy selectively clears ER in TNF-α-induced muscle atrophy
Dueren, U. K., Wei, A. A. J., Gressler, A. E., Rapp, S., Popp, O., Kerridge, R., Buonomo, V., Grumati, P., Mertins, P., Selbach, M., et al. (2026) · Autophagy Reports · doi:10.1080/27694127.2026.2649064 · Cited by 5
Human myotubularin-related protein 9 regulates ER-to-Golgi trafficking and modulates WNT3A secretion
Doubravská, L., Dostál, V., Knop, F. K., Libusová, L., & Macůrková, M. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.111709 · Cited by 5
Li, G., Kawashima, H., Ogose, A., Ariizumi, T., Hotta, T., Kuwano, R., Urata, Y., Fujiwara, T., & Endo, N. (2013) · Cancer Science · doi:10.1111/cas.12208 · Cited by 5
Xiao, C., Qiu, S., Robertson, R. M., & Seroude, L. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.12.009 · Cited by 5
Khatami, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-66475-0_2 · Cited by 5
Autophagy in different flavors: Dysregulated protein degradation in neurological diseases
Chu, C. T. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.03.020 · Cited by 6
Nagpal, A., Ndamukong, I., Hassan, A., AVRAMOVA, Z. V., & Baluška, F. (2016) · Journal of Plant Physiology · doi:10.1016/j.jplph.2016.06.001 · Cited by 4
Interplay between myotubularins and Ca2+ homeostasis
Dai, N., Groenendyk, J., & Michalak, M. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119739 · Cited by 4
Li, X., Zheng, J., Su, J., Wang, L., Luan, L., Wang, T., Bai, F., Zhong, Q., & Gong, Q. (2024) · Autophagy · doi:10.1080/15548627.2024.2394302 · Cited by 4
Phosphoinositides in membrane remodeling during infections and cellular stresses
Alemany, C., & Morel, É. (2025) · FEBS Letters · doi:10.1002/1873-3468.70213 · Cited by 2
Role of endoplasmic reticulum domains in determining secretion routes
Seedorf, M. (2010) · F1000 Biology Reports · doi:10.3410/b2-77 · Cited by 2
Congenital Myopathies and Related Disorders
(2013) · Elsevier eBooks · doi:10.1016/b978-0-7020-4340-6.00015-x · Cited by 2
Autophagy: Identification of MTMR5 as a neuron-enriched suppressor
Vogel, M. C., & Maday, S. (2022) · Current Biology · doi:10.1016/j.cub.2022.04.075 · Cited by 2
Overexpression of MTMR14 induced learning and memory impairments in 2-month-old C57 mice
Feng, Q., Li, X., Liu, R., Liu, G., He, Y., & Li, T. (2024) · Neuroscience Letters · doi:10.1016/j.neulet.2024.137700 · Cited by 2
Lipid Codes and Lipid‐Binding Proteins as Central Regulators of Autophagy
Kumar, A., & Ghosh, D. K. (2026) · BioFactors · doi:10.1002/biof.70124 · Cited by 1
Mitochondrial Fission-Fusion and Parkinson’s Disease: A Dynamic Question of Compensatory Networks
Chu, C. T., & Berman, S. (2011) · Springer eBooks · doi:10.1007/978-94-007-1291-1_7 · Cited by 1
강윤석, Kim, J.-C., 박대령, 김정하, & 유성경 (2011) · Exercise Science · doi:10.15857/ksep.2011.20.4.379 · Cited by 1
MAINTAINING AUTOPHAGIC BALANCE: A ROLE FOR BRAKES
Cherra, S. J., & Chu, C. T. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0005 · Cited by 1
The Autophagy-Dependent Signaling in Skeletal Muscle
Sakuma, K., Aizawa, M., Wakabayashi, H., & Yamaguchi, A. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_4 · Cited by 1
Pierre-Jerome, C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-13328-2.00008-8 · Cited by 1
Roy, R., Floyd, B. E., & Bassham, D. C. (2014) · Springer eBooks · doi:10.1007/978-1-4614-7881-2_2-1 · Cited by 1
Human WIPIs as Phosphoinositide Effectors at the Nascent Autophagosome
Takács, Z., & Proikas‐Cezanne, T. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801043-3.00004-2 · Cited by 1
Self-citationSynaptojanin1 is involved in endolysosomal trafficking in cone photoreceptors
George, A. A. (2015) · ResearchWorks at the University of Washington (University of Washington) · Cited by 1
Role of Human WIPIs in Macroautophagy
Proikas‐Cezanne, T., & Bakul, D. (2013) · InTech eBooks · doi:10.5772/54601
Self-citationAtg9 cycling: The molecular mechanisms of anterograde and retrograde Atg9 trafficking
van der Burgh, A. W. (2011) · Utrecht University Repository (Utrecht University)
Effect of prolonged mechanical ventilation on sepsis-induced diaphragm dysfunction
Stamiris, A. (2014) · eScholarship@McGill (McGill) · doi:10.82308/25517
1 Developmental and Molecular Pathways, Novartis Institutes for BioMedical Research,
Fetalvero, K. M., Yu, Y., Goetschkes, M., Liang, G., Reginald, A., Gould, T. A., Triantafellow, E., Bergling, S., Loureiro, J., , J., et al. (2012)
Reactive oxygen species mediated regulation of autophagy in skeletal muscles
Rahman, M. (2014) · eScholarship@McGill (McGill) · doi:10.82308/18633
The role of autophagy in clearance of protein aggregates
Isakson, P. (2011) · NORA - Norwegian Open Research Archives
Schneider, J. L., & Cuervo, A. M. (2012) · Oxidative stress and disease · doi:10.1201/b12308-19
Examining the Role of Autophagy in Skeletal Muscle Cell Death and Differentiation
McMillan, M. E. (2015) · UWSpace (University of Waterloo)
The role of phosphatidylinositol 3-kinases in autophagy regulation
Devereaux, K. A. (2014) · doi:10.7916/d8qz2842
Xiao, C., Qiu, S., Robertson, R. M., & Seroude, L. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/130559
Autophagy in Immunity and Cell-Autonomous Defense Against
Microbes, I., & Deretic, V. P. (2015)
Self-citationUnselective Disposal of Cellular Aggregates
Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00004-3
(2010) · Current Opinion in Rheumatology · doi:10.1097/bor.0b013e3283404094
Congenital Myopathies and Related Disorders
(2020) · Elsevier eBooks · doi:10.1016/b978-0-7020-7471-4.00015-x
A novel autophagy inhibitor, bTBT, disturbs autophagosome formation
Chiba, M., Yanagawa, M., Oyama, Y., Harada, S., Nemoto, T., Matsuura, A., & Itakura, E. (2023) · Autophagy Reports · doi:10.1080/27694127.2023.2194620
Interplay between Phospholipid signaling and autophagy
Maan, M., & Dutta, M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95582-9.00021-8
Stressz-indukált autofágia szabályozási mechanizmusai Drosophila melanogasterben
Manzéger, A. (2023) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2022.245
Az autofág kapacitás életkor-függő szabályozása Drosophila melanogasterben
Szinyákovics, J. (2024) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2023.204
The Source of Membrane During Autophagy and the Early Steps in Autophagosome Formation
Ktistakis, N. T. (2025) · Learning materials in biosciences · doi:10.1007/978-3-031-88121-3_5
ER Stress As Modulator of Autophagy Pathways
Salazar‐Roa, M., Hernández‐Tiedra, S., Lorente, M., & Velasco, G. (2012) · Springer eBooks · doi:10.1007/978-94-007-4351-9_7
The role of myotubularin-related lipid phosphatases in cancer pathogenesis
Doubravská, L., & Macůrková, M. (2026) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2026.105022
Burján, T., Horvath, H., Illés, E., Schlett, K., Bencsik, N., & Kovács, T. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.23.707351
ZIEGLER, M. L., Guenter, C., Alecu, J. E., Xue, X., Kim, H. M., Saffari, A., Davies, A. K., Şahin, M., & Ebrahimi‐Fakhari, D. (2026) · JCI Insight · doi:10.1172/jci.insight.202204
Yuan, W.-B., Tan, L., Du, Y.-Y., Xu, T.-T., Du, Z.-C., Wu, L.-P., Cui, D.-X., & Zhao, Q.-R. (2026) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-026-05704-w
EDTP Loss of Function Impairs Longevity and ReproductionPreprint
Lu, X., Barwell, T., Edelman, S., & Seroude, L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.31.748413
Metadata
- Authors
- Vergne, I., Roberts, E., Elmaoued, R. A., Tosch, V., Delgado, M. A., Proikas‐Cezanne, T., Laporte, J., & Deretic, V.
- Affiliations
- University of New Mexico (US)
- Centre National de la Recherche Scientifique (FR)
- University of Tübingen (DE)
- Corresponding author
- Vergne, Isabelle
- Deretic, Vojo
- Venue
- The EMBO Journal
- Published
- 2009-07-09
- Volume
- 28
- Issue
- 15
- Pages
- 2244-2258
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2726690
- OpenAlex
- W2103545941
- Cited by
- 270
- References
- 55
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 8 · 2023: 7 · 2022: 5 · 2021: 12 · 2020: 6 · 2019: 12 · 2018: 11 · 2017: 13 · 2016: 23 · 2015: 22 · 2014: 25 · 2013: 22 · 2012: 29
- FWCI
- 20.69
- Type
- journal article
- Language
- en
- Update notices
- erratum (2009-09-10)
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (SFB 773)
- Agence Nationale de la Recherche
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- National Institutes of Health
- School of Medicine, University of New Mexico
- National Institute of Allergy and Infectious Diseases (R01AI042999, AI 45148, R01AI045148, R37AI042999)
- 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 initiation, Atg16, Atg9, LC3, autophagosome formation, centronuclear myopathy, phosphatidylinositol 3-phosphate
- MeSH terms
- Animals, Autophagy, Cell Line, Humans, Molecular Sequence Data, Phosphoric Monoester Hydrolases, Sequence Analysis, DNA, Amino Acid Substitution, Mutation, Missense, Myopathies, Structural, Congenital, Mice
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
