The lysosome as a cellular centre for signalling, metabolism and quality control

mTOR Signaling in Growth, Metabolism, and Disease

Saxton, R. A., & Sabatini, D. M. (2017) · Cell · doi:10.1016/j.cell.2017.02.004 · Cited by 7,555 · see citing works

TFEB Links Autophagy to Lysosomal Biogenesis

Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365 · see citing works

Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino Acids

Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464 · see citing works

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

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Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy

Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C. (2014) · Nature · doi:10.1038/nature13148 · Cited by 2,084 · see citing works

Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy

Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · see citing works

Macropinocytosis of protein is an amino acid supply route in Ras-transformed cells

Commisso, C., Davidson, S. M., Soydaner-Azeloglu, R. G., Parker, S. J., Kamphorst, J. J., Hackett, S., Grabocka, E., Nofal, M., Drebin, J. A., Thompson, C. B., et al. (2013) · Nature · doi:10.1038/nature12138 · Cited by 1,683 · see citing works

mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H ⁺ -ATPase

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

The role for autophagy in cancer

White, E. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73941 · Cited by 1,332 · see citing works

The translational landscape of mTOR signalling steers cancer initiation and metastasis

Hsieh, A. C., Liu, Y., Edlind, M. P., Ingolia, N. T., Janes, M. R., Sher, A., Shi, E. Y., Stumpf, C. R., Christensen, C., Bonham, M. J., et al. (2012) · Nature · doi:10.1038/nature10912 · Cited by 1,313 · see citing works

Sestrin2 is a leucine sensor for the mTORC1 pathway

Wolfson, R. L., Chantranupong, L., Saxton, R. A., Shen, K., Scaria, S. M., Cantor, J. R., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aab2674 · Cited by 1,306 · see citing works

A Tumor Suppressor Complex with GAP Activity for the Rag GTPases That Signal Amino Acid Sufficiency to mTORC1

Bar-Peled, L., Chantranupong, L., Cherniack, A. D., Chen, W. W., Ottina, K. A., Grabiner, B. C., Spear, E. D., Carter, S. L., Meyerson, M., & Sabatini, D. M. (2013) · Science · doi:10.1126/science.1232044 · Cited by 1,080 · see citing works

Ragulator Is a GEF for the Rag GTPases that Signal Amino Acid Levels to mTORC1

Bar-Peled, L., Schweitzer, L. D., Zoncu, R., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.07.032 · Cited by 918 · see citing works

Autophagy maintains the metabolism and function of young and old stem cells

Ho, T. T., Warr, M. R., Adelman, E. R., Lansinger, O. M., Flach, J., Verovskaya, E. V., Figueroa, M. E., & Passegué, E. (2017) · Nature · doi:10.1038/nature21388 · Cited by 896 · see citing works

The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway

Chantranupong, L., Scaria, S. M., Saxton, R. A., Gygi, M. P., Shen, K., Wyant, G. A., Wang, T., Harper, J. W., Gygi, S. P., & Sabatini, D. M. (2016) · Cell · doi:10.1016/j.cell.2016.02.035 · Cited by 843 · see citing works

α-Synuclein impairs macroautophagy: implications for Parkinson’s disease

Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · see citing works

Transcriptional control of autophagy-lysosome function drives pancreatic cancer metabolism

Perera, R. M., Stoykova, S., Nicolay, B. N., Ross, K. N., Fitamant, J., Boukhali, M., Lengrand, J., Deshpande, V., Selig, M. K., Ferrone, C. R., et al. (2015) · Nature · doi:10.1038/nature14587 · Cited by 799 · see citing works

Differential regulation of mTORC1 by leucine and glutamine

Jewell, J. L., Kim, Y. C., Russell, R. C., Yu, F.-X., Park, H. W., Plouffe, S. W., Tagliabracci, V. S., & Guan, K.-L. (2015) · Science · doi:10.1126/science.1259472 · Cited by 757 · see citing works

SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1

Rebsamen, M., Pochini, L., Stasyk, T., de Araújo, M. E. G., Galluccio, M., Kandasamy, R. K., Snijder, B., Fauster, A., Rudashevskaya, E. L., Bruckner, M., et al. (2015) · Nature · doi:10.1038/nature14107 · Cited by 673 · see citing works

Lysosomal cholesterol activates mTORC1 via an SLC38A9–Niemann-Pick C1 signaling complex

Castellano, B. M., Thelen, A. M., Moldavski, O., Feltes, M., van der Welle, R. E. N., Mydock-McGrane, L., Jiang, X., van Eijkeren, R. J., Davis, O. B., Louie, S. M., et al. (2017) · Science · doi:10.1126/science.aag1417 · Cited by 562 · see citing works

Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40

Yang, H., Jiang, X., Li, B., Yang, H. J., Miller, M., Yang, A., Dhar, A., & Pavletich, N. P. (2017) · Nature · doi:10.1038/nature25023 · Cited by 548 · see citing works

The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy

Webster, C. P., Smith, E. F., Bauer, C. S., Moller, A., Hautbergue, G. M., Ferraiuolo, L., Myszczynska, M. A., Higginbottom, A., Walsh, M. J., Whitworth, A. J., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694401 · Cited by 404 · see citing works

Amyloid precursor protein and endosomal-lysosomal dysfunction in Alzheimer's disease: inseparable partners in a multifactorial disease

Nixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400 · see citing works

A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation

Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., & Xu, H. (2016) · Nature Cell Biology · doi:10.1038/ncb3324 · Cited by 387 · see citing works

NUFIP1 is a ribosome receptor for starvation-induced ribophagy

Wyant, G. A., Abu-Remaileh, M., Frenkel, E. M., Laqtom, N. N., Dharamdasani, V., Lewis, C. A., Chan, S. H., Heinze, I., Ori, A., & Sabatini, D. M. (2018) · Science · doi:10.1126/science.aar2663 · Cited by 363 · see citing works

Rapamycin activation of 4E-BP prevents parkinsonian dopaminergic neuron loss

Tain, L. S., Mortiboys, H., Tao, R. N., Ziviani, E., Bandmann, O., & Whitworth, A. J. (2009) · Nature Neuroscience · doi:10.1038/nn.2372 · Cited by 323 · see citing works

Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation

Rong, Y., McPhee, C. K., Deng, S., Huang, L., Chen, L., Liu, M., Tracy, K., Baehrecke, E. H., Yu, L., & Lenardo, M. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013800108 · Cited by 273 · see citing works

<i>App</i>Gene Dosage Modulates Endosomal Abnormalities of Alzheimer's Disease in a Segmental Trisomy 16 Mouse Model of Down Syndrome

Cataldo, A. M., Petanceska, S., Peterhoff, C. M., Terio, N. B., Epstein, C. J., Villar, A., Carlson, E. J., Staufenbiel, M., & Nixon, R. A. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-17-06788.2003 · Cited by 241 · see citing works

Coordinate regulation of ribosome biogenesis and function by the ribosomal protein S6 kinase, a key mediator of mTOR function

Jastrzebski, K., Hannan, K. M., Tchoubrieva, E. B., Hannan, R. D., & Pearson, R. B. (2007) · Growth Factors · doi:10.1080/08977190701779101 · Cited by 240 · see citing works

Crystal structure of the human lysosomal mTORC1 scaffold complex and its impact on signaling

de Araujo, M. E. G., Naschberger, A., Fürnrohr, B. G., Stasyk, T., Dunzendorfer-Matt, T., Lechner, S., Welti, S., Kremser, L., Shivalingaiah, G., Offterdinger, M., et al. (2017) · Science · doi:10.1126/science.aao1583 · Cited by 134 · see citing works

Feedback Inhibition of the Rag GTPase GAP Complex Lst4-Lst7 Safeguards TORC1 from Hyperactivation by Amino Acid Signals

Péli-Gulli, M.-P., Raucci, S., Hu, Z., Dengjel, J., & De Virgilio, C. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.058 · Cited by 28 · see citing works

Lysosomes as dynamic regulators of cell and organismal homeostasis

Ballabio, A., & Bonifacino, J. S. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0185-4 · Cited by 1,469 · see citing works

The many functions of ESCRTs

Vietri, M., Radulovic, M., & Stenmark, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0177-4 · Cited by 962 · see citing works

Maintaining Iron Homeostasis Is the Key Role of Lysosomal Acidity for Cell Proliferation

Weber, R. A., Yen, F. S., Nicholson, S. P. V., Alwaseem, H., Bayraktar, E. C., Alam, M., Timson, R. C., La, K., Abu-Remaileh, M., Molina, H., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.01.003 · Cited by 236 · see citing works

Targeting lysosomes in human disease: from basic research to clinical applications

Cao, M., Luo, X., Wu, K., & He, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00778-y · Cited by 225 · see citing works

Autophagy in animal development

Allen, E. A., & Baehrecke, E. H. (2020) · Cell Death &amp; Differentiation · doi:10.1038/s41418-020-0497-0 · Cited by 127 · see citing works

Defective lysosomal acidification: a new prognostic marker and therapeutic target for neurodegenerative diseases

Lo, C. H., & Zeng, J. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00362-0 · Cited by 117 · see citing works

Metabolomic profiling of single enlarged lysosomes

Zhu, H., Li, Q., Liao, T., Yin, X., Chen, Q., Wang, Z., Dai, M., Yi, L., Ge, S., Miao, C., et al. (2021) · Nature Methods · doi:10.1038/s41592-021-01182-8 · Cited by 103 · see citing works

Macrophages recycle phagocytosed bacteria to fuel immunometabolic responses

Lesbats, J., Brillac, A., Reisz, J. A., Mukherjee, P., Lhuissier, C., Fernández-Monreal, M., Dupuy, J.-W., Sequeira, A., Tioli, G., De La Calle Arregui, C., et al. (2025) · Nature · doi:10.1038/s41586-025-08629-4 · Cited by 74 · see citing works

Moving towards a new era of genomics in the neuronal ceroid lipofuscinoses

Butz, E. S., Chandrachud, U., Mole, S. E., & Cotman, S. L. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.165571 · Cited by 62 · see citing works

TFEB Transcriptional Responses Reveal Negative Feedback by BHLHE40 and BHLHE41

Carey, K. L., Paulus, G. L. C., Wang, L., Balce, D. R., Luo, J. W., Bergman, P., Ferder, I. C., Kong, L., Renaud, N., Singh, S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108371 · Cited by 55 · see citing works

Multi cell line analysis of lysosomal proteomes reveals unique features and novel lysosomal proteins

Akter, F., Ponnaiyan, S., Kögler-Mohrbacher, B., Bleibaum, F., Damme, M., Renard, B. Y., & Winter, D. (2020) · doi:10.1101/2020.12.21.423747 · Cited by 55 · see citing works

The needs of a synapse—How local organelles serve synaptic proteostasis

Grochowska, K. M., Andres‐Alonso, M., Karpova, A., & Kreutz, M. R. (2022) · The EMBO Journal · doi:10.15252/embj.2021110057 · Cited by 38 · see citing works

When friendship turns sour: Effective communication between mitochondria and intracellular organelles in parkinson’s disease

Lin, T.-K., Lin, K.-J., Lin, K.-L., Liou, C.-W., Chen, S.-D., Chuang, Y.-C., Wang, P.-W., Chuang, J.-H., & Wang, T.-J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607392 · Cited by 19 · see citing works

The radioenhancer NBTXR3: bridging physics and biology to improve radiotherapy outcomes and prime anti-tumor immunity

Bienassis, C., Vivar, O. I., Hu, Y., Da silva, J., Darmon, A., Marill, J., Anesary, N. M., Schmitt, P., Levy, L., Welsh, J., et al. (2025) · Journal of Experimental &amp; Clinical Cancer Research · doi:10.1186/s13046-025-03579-1 · Cited by 9 · see citing works

The lysosome and proteostatic stress at the intersection of pediatric neurological disorders and adult neurodegenerative diseases

Lane-Donovan, C., Paredes, M., & Kao, A. W. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102854 · Cited by 3 · see citing works