Defects of Vps15 in skeletal muscles lead to autophagic vacuolar myopathy and lysosomal disease
Open accessAbstract
The complex of Vacuolar Protein Sorting 34 and 15 (Vps34 and Vps15) has Class III phosphatidylinositol 3‐kinase activity and putative roles in nutrient sensing, mammalian Target Of Rapamycin (mTOR) activation by amino acids, cell growth, vesicular trafficking and autophagy. Contrary to expectations, here we show that Vps15 ‐deficient mouse tissues are competent for LC3‐positive autophagosome formation and maintain mTOR activation. However, an impaired lysosomal function in mutant cells is traced by accumulation of adaptor protein p62, LC3 and Lamp2 positive vesicles, which can be reverted to normal levels after ectopic overexpression of Vps15. Mice lacking Vps15 in skeletal muscles, develop a severe myopathy. Distinct from the autophagy deficient Atg7 −/− mutants, pathognomonic morphological hallmarks of autophagic vacuolar myopathy (AVM) are observed in Vps15 −/− mutants, including elevated creatine kinase plasma levels, accumulation of autophagosomes, glycogen and sarcolemmal features within the fibres. Importantly, Vps34/Vps15 overexpression in myoblasts of Danon AVM disease patients alleviates the glycogen accumulation. Thus, the activity of the Vps34/Vps15 complex is critical in disease conditions such as AVMs, and possibly a variety of other lysosomal storage diseases.
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
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?
Over-expression of the VPS34-VPS15 complex in Danon disease patient myoblasts results in a partial amelioration of glycogen overload.
“Also, over-expression of the VPS34–VPS15 complex in Danon disease patients in myoblasts results in a partial amelioration of glycogen overload [242].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [242]
Muscle-specific VPS15 knockout mice develop a severe myopathy with hallmarks of Danon disease myopathy, including alterations in mitochondrial morphology and accumulation of autophagosomes and glycogen due to a defect in fusion of autophagosomes with lysosomes.
“Muscle-specific VPS15 knockout mice develop a severe myopathy with hallmarks of DD myopathy, including alterations in mitochondrial morphology, and accumulation of autophagosomes and glycogen due to a defect in the fusion of autophagosomes with lysosomes.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [242]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
(1975) · Journal of AOAC INTERNATIONAL · doi:10.1093/jaoac/58.5.1085 · Cited by 20,078 · see citing works
(1974) · Elsevier eBooks · doi:10.1016/b978-0-12-091304-6.x5001-0 · Cited by 6,786 · see citing works
The 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 · see citing works
Impairment of starvation-induced and constitutive autophagy in <i>Atg7</i> -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331 · see citing works
Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,323 · see citing works
Kimura, S., Noda, T., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4451 · Cited by 2,278 · see citing works
Jung, C. H., Ro, S.-H., Cao, J., Otto, N. M., & Kim, D.-H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.017 · Cited by 2,090 · see citing works
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
Self-citationAutophagy: from phenomenology to molecular understanding in less than a decade
Klionsky, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2245 · Cited by 1,933 · see citing works
The emerging mechanisms of isoform-specific PI3K signalling
Vanhaesebroeck, B., Guillermet-Guibert, J., Graupera, M., & Bilanges, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2882 · Cited by 1,767 · see citing works
Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673 · see citing works
Schwenk, F., Baron, U., & Rajewsky, K. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.24.5080 · Cited by 1,289 · see citing works
Autophagy is required to maintain muscle mass.
Masiero, E., Agatea, L., Mammucari, C., Blaauw, B., Loro, E., Komatsu, M., Metzger, D., Reggiani, C., Schiaffino, S., & Sandri, M. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.10.008 · Cited by 1,282 · see citing works
Self-citationMatsunaga, K., Saitoh, T., Tabata, K., Omori, H., Satoh, T., Kurotori, N., Maejima, I., Shirahama-Noda, K., Ichimura, T., Isobe, T., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1846 · Cited by 1,235 · see citing works
Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z. (2009) · Nature Cell Biology · doi:10.1038/ncb1854 · Cited by 1,005 · see citing works
Kihara, A., Noda, T., Ishihara, N., & Ohsumi, Y. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.3.519 · Cited by 1,004 · see citing works
Robinson, J. S., Klionsky, D. J., Banta, L. M., & Emr, S. D. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.11.4936 · Cited by 967 · see citing works
Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)
Nishino, I., Fu, J., Tanji, K., Yamada, T., Shimojo, S., Koori, T., Mora, M., Riggs, J. E., Oh, S. J., Koga, Y., et al. (2000) · Nature · doi:10.1038/35022604 · Cited by 959 · see citing works
Self-citationAccumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice
Tanaka, Y., Guhde, G., Suter, A., Eskelinen, E.-L., Hartmann, D., Lüllmann-Rauch, R., Janssen, P. M. L., Blanz, J., von Figura, K., & Saftig, P. (2000) · Nature · doi:10.1038/35022595 · Cited by 925 · see citing works
Phosphatidylinositol 3-Kinase Encoded by Yeast VPS 34 Gene Essential for Protein Sorting
Schu, P. V., Takegawa, K., Fry, M., Stack, J. H., Waterfield, M. D., & Emr, S. D. (1993) · Science · doi:10.1126/science.8385367 · Cited by 920 · see citing works
Nobukuni, T., Joaquin, M., Roccio, M., Dann, S. G., Kim, S. Y., Gulati, P., Byfield, M. P., Backer, J., Natt, F., Bos, J. L., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506925102 · Cited by 753 · see citing works
Autophagy: A lysosomal degradation pathway with a central role in health and disease
Eskelinen, E., & Säftig, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.07.014 · Cited by 699 · see citing works
Hariharan, N., Maejima, Y., Nakae, J., Paik, J., DePinho, R. A., & Sadoshima, J. (2010) · Circulation Research · doi:10.1161/circresaha.110.227371 · Cited by 688 · see citing works
Disruption of the p70s6k/p85s6k gene reveals a small mouse phenotype and a new functional S6 kinase
Shima, H., Pende, M., Chen, Y., Fumagalli, S., THOMAS, G. V., & Kozma, S. C. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6649 · Cited by 636 · see citing works
Self-citationCanonical and non-canonical autophagy: variations on a common theme of self-eating?
Codogno, P., Mehrpour, M., & Proikas‐Cezanne, T. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3249 · Cited by 545 · see citing works
Self-citationGrumati, P., Coletto, L., Sabatelli, P., Cescon, M., Angelin, A., Bertaggia, E., Blaauw, B., Urciuolo, A., Tiepolo, T., Merlini, L., et al. (2010) · Nature Medicine · doi:10.1038/nm.2247 · Cited by 540 · see citing works
Self-citationhVps34 Is a Nutrient-regulated Lipid Kinase Required for Activation of p70 S6 Kinase
Byfield, M. P., Murray, J. T., & Backer, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507201200 · Cited by 526 · see citing works
p62 Is a Key Regulator of Nutrient Sensing in the mTORC1 Pathway
Durán, Á., Amanchy, R., Linares, J. F., Joshi, J. P., Abu‐Baker, S., Porollo, A., Hansen, M., Moscat, J., & Díaz-Meco, M. T. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.038 · Cited by 502 · see citing works
Coordination of membrane events during autophagy by multiple class III PI3-kinase complexes
Simonsen, A., & Tooze, S. A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200907014 · Cited by 500 · see citing works
ESCRT-III Dysfunction Causes Autophagosome Accumulation and Neurodegeneration
Lee, J., Beigneux, A. P., Ahmad, S. T., Young, S. G., & Gao, F. (2007) · Current Biology · doi:10.1016/j.cub.2007.07.029 · Cited by 490 · see citing works
Overview of macroautophagy regulation in mammalian cells
Mehrpour, M., Esclatine, A., Beau, I., & Codogno, P. (2010) · Cell Research · doi:10.1038/cr.2010.82 · Cited by 488 · see citing works
Regulation of TFEB and V‐ATPases by mTORC1
Peña‐Llopis, S., Vega-Rubín-de-Celis, S., Schwartz, J. C., Wolff, N. C., Tran, T. A. T., Zou, L., Xie, X., Corey, D. R., & Brugarolas, J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.257 · Cited by 456 · see citing works
Sandri, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.056 · Cited by 451 · see citing works
Self-citationFabry Disease: Perspectives from 5 Years of FOS
Mehta, A. B., Beck, M., & Sunder–Plassmann, G. (2006) · Cited by 445 · see citing works
Banta, L. M., Robinson, J. S., Klionsky, D. J., & Emr, S. D. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.4.1369 · Cited by 403 · see citing works
Class III PI3K Vps34 plays an essential role in autophagy and in heart and liver function
Jaber, N. L., Dou, Z., Chen, J., Catanzaro, J. M., Jiang, Y.-P., Ballou, L. M., Selinger, E. S., Ouyang, X., Lin, R. Z., Zhang, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112848109 · Cited by 386 · see citing works
Amino acid regulation of TOR complex 1
Avruch, J., Long, X., Ortiz-Vega, S., Rapley, J., Papageorgiou, A., & Dai, N. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90645.2008 · Cited by 382 · see citing works
Role of LAMP-2 in Lysosome Biogenesis and Autophagy
Eskelinen, E., Illert, A. L., Tanaka, Y., Schwarzmann, G. O. H., Blanz, J., FIGURA, K. V., & Säftig, P. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-02-0114 · Cited by 365 · see citing works
Proikas‐Cezanne, T., Waddell, S., Gaugel, A., Frickey, T., Lupas, A. N., & Nordheim, A. (2004) · Oncogene · doi:10.1038/sj.onc.1208331 · Cited by 356 · see citing works
Self-citationRaben, N., Hill, V., Shea, L., Takikita, S., Baum, R., Mizushima, N., Ralston, E., & Plotz, P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn292 · Cited by 352 · see citing works
Robinson, J. S., Klionsky, D. J., Banta, L. M., & Emr, S. D. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.11.4936-4948.1988 · Cited by 351 · see citing works
ESCRTs and Fab1 Regulate Distinct Steps of Autophagy
Rusten, T. E., Vaccari, T., Lindmo, K., Rodahl, L. M., Nezis, I. P., Sem-Jacobsen, C., Wendler, F., Vincent, J., Brech, A., Bilder, D. H., et al. (2007) · Current Biology · doi:10.1016/j.cub.2007.09.032 · Cited by 332 · see citing works
The class III PI(3)K Vps34 promotes autophagy and endocytosis but not TOR signaling in Drosophila
Juhász, G., Hill, J. H., Yan, Y., Sass, M., Baehrecke, E. H., Backer, J., & Neufeld, T. P. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200712051 · Cited by 311 · see citing works
p62, an autophagy hero or culprit?
Rusten, T. E., & Stenmark, H. (2010) · Nature Cell Biology · doi:10.1038/ncb0310-207 · Cited by 237 · see citing works
Gene targeting restricted to mouse striated muscle lineage
Miniou, P. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.19.e27 · Cited by 226 · see citing works
A Mammalian Autophagosome Maturation Mechanism Mediated by TECPR1 and the Atg12-Atg5 Conjugate
Chen, D., Fan, W., Lu, Y., Ding, X., Chen, S., & Zhong, Q. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.12.036 · Cited by 210 · see citing works
Modulation of Local PtdIns3P Levels by the PI Phosphatase MTMR3 Regulates Constitutive Autophagy
Taguchi‐Atarashi, N., Hamasaki, M., Matsunaga, K., Omori, H., Ktistakis, N. T., Yoshimori, T., & Noda, T. (2010) · Traffic · doi:10.1111/j.1600-0854.2010.01034.x · Cited by 199 · see citing works
FYVE-finger proteins – effectors of an inositol lipid
Stenmark, H., & Aasland, R. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.23.4175 · Cited by 198 · see citing works
Thoresen, S. B., Pedersen, N. M., Liestøl, K., & Stenmark, H. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.07.008 · Cited by 192 · see citing works
Willinger, T., & Flavell, R. A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205305109 · Cited by 183 · see citing works
Aguilar, V. M., Alliouachene, S., Sotiropoulos, A., Sobering, A. K., Athéa, Y., Djouadi, F., Miraux, S., Thiaudière, E., Foretz, M., Viollet, B., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.05.006 · Cited by 182 · see citing works
Self-citationRaben, N., Schreiner, C. N., Baum, R., Takikita, S., Xu, S., Xie, T., Myerowitz, R., Komatsu, M., van der Meulen, J. H., Nagaraju, K., et al. (2010) · Autophagy · doi:10.4161/auto.6.8.13378 · Cited by 167 · see citing works
Human WIPI‐1 puncta‐formation: A novel assay to assess mammalian autophagy
Proikas-Cezanne, T., Ruckerbauer, S., Stierhof, Y.-D., Berg, C., & Nordheim, A. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.06.040 · Cited by 165 · see citing works
Self-citationClass III PI-3-kinase activates phospholipase D in an amino acid–sensing mTORC1 pathway
Yoon, M., Du, G., Backer, J., Frohman, M. A., & Chen, J. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201107033 · Cited by 161 · see citing works
Lysosomal myopathies: An excessive build-up in autophagosomes is too much to handle
Malicdan, M. C. V., Noguchi, S., Nonaka, I., Säftig, P., & Nishino, I. (2008) · Neuromuscular Disorders · doi:10.1016/j.nmd.2008.04.010 · Cited by 151 · see citing works
Self-citationInteraction of the EEA1 FYVE Finger with Phosphatidylinositol 3-Phosphate and Early Endosomes
Gaullier, J., Rønning, E., Gillooly, D. J., & Stenmark, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m906554199 · Cited by 144 · see citing works
The role of PI3P phosphatases in the regulation of autophagy
Vergne, I., & Deretic, V. P. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.054 · Cited by 143 · see citing works
Abnormalities in structure and function of limb skeletal muscle fibres of dystrophic mdx mice
Head, S. I., Williams, D. A., & Stephenson, D. G. (1992) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1992.0058 · Cited by 140 · see citing works
Lee, J., & Gao, F. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0924-09.2009 · Cited by 124 · see citing works
Autophagic vacuolar myopathies
Nishino, I. (2003) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-003-0040-y · Cited by 123 · see citing works
Self-citationShaping development with ESCRTs
Rusten, T. E., Vaccari, T., & Stenmark, H. (2011) · Nature Cell Biology · doi:10.1038/ncb2381 · Cited by 122 · see citing works
MTM1 mutation associated with X-linked myotubular myopathy in Labrador Retrievers
Beggs, A. H., Böhm, J., Snead, E., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003677107 · Cited by 119 · see citing works
hVps15, but not Ca2+/CaM, is required for the activity and regulation of hVps34 in mammalian cells
Yan, Y., Flinn, R. J., Wu, H., Schnur, R. S., & Backer, J. (2008) · Biochemical Journal · doi:10.1042/bj20081865 · Cited by 113 · see citing works
Epidemiology of lysosomal storage diseases: an overview
Fuller, M., Meikle, P. J., & Hopwood, J. J. (2006) · Europe PMC (PubMed Central) · Cited by 101 · see citing works
The Mammalian Class 3 PI3K (PIK3C3) Is Required for Early Embryogenesis and Cell Proliferation
Zhou, X., Takatoh, J., & Wang, F. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016358 · Cited by 99 · see citing works
McLeod, I. X., Zhou, X., Li, Q.-J., Wang, F., & He, Y.-W. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100710 · Cited by 91 · see citing works
Chapter 16 Assessing Mammalian Autophagy by WIPI‐1/Atg18 Puncta Formation
Proikas‐Cezanne, T., & Pfisterer, S. G. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)03616-1 · Cited by 32 · see citing works
Self-citationChapter 7 The GST‐BHMT Assay and Related Assays for Autophagy
Dennis, P. B., & Mercer, C. A. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)03607-0 · Cited by 21 · see citing works
Mercer, C. A., Kaliappan, A., & Dennis, P. B. (2008) · Autophagy · doi:10.4161/auto.5275 · Cited by 19 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mechanisms of muscle atrophy and hypertrophy: implications in health and disease
Sartori, R., Romanello, V., & Sandri, M. (2021) · Nature Communications · doi:10.1038/s41467-020-20123-1 · Cited by 940 · see citing works
Self-citationProtein breakdown in muscle wasting: Role of autophagy-lysosome and ubiquitin-proteasome
Sandri, M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.023 · Cited by 689 · see citing works
Self-citationRomanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Self-citationMisregulation of autophagy and protein degradation systems in myopathies and muscular dystrophies.
Sandri, M., Coletto, L., Grumati, P., & Bonaldo, P. (2013) · Journal of Cell Science · doi:10.1242/jcs.114041 · Cited by 179 · see citing works
Self-citationSkeletal muscle autophagy: a new metabolic regulator
Neel, B. A., Lin, Y., & Pessin, J. E. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.004 · Cited by 178 · see citing works
Protein breakdown in cancer cachexia
Sandri, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.11.002 · Cited by 134 · see citing works
Self-citationIershov, A., Nemazanyy, I., Alkhoury, C., Girard, M., Barth, E., Cagnard, N., Montagner, A., Chretien, D., Rugarli, E. I., Guillou, H., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09598-9 · Cited by 109 · see citing works
Self-citationVainshtein, A., Grumati, P., Sandri, M., & Bonaldo, P. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1096-z · Cited by 88 · see citing works
Self-citationTriolo, M., Oliveira, A. N., Kumari, R., & Hood, D. A. (2022) · Skeletal Muscle · doi:10.1186/s13395-022-00296-7 · Cited by 75 · see citing works
“Inhibition of autophagy promotes atrophy, neuromuscular junction decay, sarcomere disarrangement, and ultimately weakness [12–16].”
BackgroundCastets, P., Frank, S., Sinnreich, M., & Rüegg, M. A. (2016) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-160153 · Cited by 49 · see citing works
Exercise prevents impaired autophagy and proteostasis in a model of neurogenic myopathy
Campos, J. C., Baehr, L. M., Gomes, K. M. S., Bechara, L. R. G., Voltarelli, V. A., Bozi, L. H. M., Ribeiro, M. A. C., Ferreira, N. D., Moreira, J. B. N., Brum, P. C., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-30365-1 · Cited by 32 · see citing works
Picca, A., Triolo, M., Wohlgemuth, S. E., Martenson, M. S., Mankowski, R. T., Anton, S. D., Marzetti, E., Leeuwenburgh, C., & Hood, D. A. (2023) · Cells · doi:10.3390/cells12010183 · Cited by 23 · see citing works
- Authors
- Nemazanyy, I., Blaauw, B., Paolini, C., Caillaud, C., Protasi, F., Mueller, A., Proikas‐Cezanne, T., Russell, R. C., Guan, K., Nishino, I., Sandri, M., Pende, M., & Panasyuk, G.
- Affiliations
- Inserm (FR)
- Veneto Institute of Molecular Medicine (IT)
- University of Chieti-Pescara (IT)
- University of Tübingen (DE)
- University of California San Diego (US)
- National Center of Neurology and Psychiatry (JP)
- Corresponding author
- Pende, Mario
- ORCID
- Venue
- EMBO Molecular Medicine
- Published
- 2013-04-30
- Volume
- 5
- Issue
- 6
- Pages
- 870-890
- ISSN
- 1757-4676 (ISSN-L)
- 1757-4684
- PMC
- PMC3779449
- OpenAlex
- W2164029978
- Cited by
- 126
- References
- 69
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 10 · 2023: 11 · 2022: 11 · 2021: 16 · 2020: 8 · 2019: 5 · 2018: 8 · 2017: 10 · 2016: 8 · 2015: 11 · 2014: 10 · 2013: 8
- FWCI
- 8.99
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- EMBO Molecular Medicine (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM051586)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- VPS15, Vps34, class III phosphatidylinositol 3-kinase, autophagic vacuolar myopathy, lysosomal storage disease, skeletal muscle, autophagy, mTOR activation, p62, LC3, LAMP2, glycogen accumulation, Danon disease, creatine kinase, myoblasts, lysosomal function
- MeSH terms
- Autophagy-Related Protein 7, Animals, Autophagy, Cell Line, Humans, Microtubule-Associated Proteins, Muscular Diseases, Transcription Factors, Lysosomal Storage Diseases, Mice, Knockout, Muscle, Skeletal, Mice, Transcription Factor TFIIH, Lysosomal-Associated Membrane Protein 2, Class III Phosphatidylinositol 3-Kinases, TOR Serine-Threonine Kinases, Vacuolar Sorting Protein VPS15
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
