{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T02:36:13Z","timestamp":1780454173019,"version":"3.54.1"},"reference-count":104,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2024,2,1]],"date-time":"2024-02-01T00:00:00Z","timestamp":1706745600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,2,1]],"date-time":"2024-02-01T00:00:00Z","timestamp":1706745600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,1,5]],"date-time":"2024-01-05T00:00:00Z","timestamp":1704412800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009633","name":"Eunice Kennedy Shriver National Institute of Child Health and Human Development","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009633","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2024,2]]},"DOI":"10.1016\/j.jbc.2024.105641","type":"journal-article","created":{"date-parts":[[2024,1,9]],"date-time":"2024-01-09T11:25:20Z","timestamp":1704799520000},"page":"105641","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Disruption of lysosomal nutrient sensing scaffold contributes to pathogenesis of a fatal neurodegenerative lysosomal storage disease"],"prefix":"10.1016","volume":"300","author":[{"given":"Maria B.","family":"Bagh","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abhilash P.","family":"Appu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tamal","family":"Sadhukhan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Avisek","family":"Mondal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nisha","family":"Plavelil","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mahadevan","family":"Raghavankutty","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ajayan M.","family":"Supran","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sriparna","family":"Sadhukhan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aiyi","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anil B.","family":"Mukherjee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2024.105641_bib1","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.cell.2012.03.017","article-title":"mTOR signaling in growth control and disease","volume":"149","author":"Laplante","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib2","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/nrd.2017.214","article-title":"Emptying the stores: lysosomal diseases and therapeutic strategies","volume":"17","author":"Platt","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.jbc.2024.105641_bib3","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1146\/annurev-neuro-070815-014031","article-title":"Brain disorders due to lysosomal dysfunction","volume":"39","author":"Fraldi","year":"2016","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.jbc.2024.105641_bib4","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1042\/EBC20170055","article-title":"Dysregulation of autophagy as a common mechanism in lysosomal storage diseases","volume":"61","author":"Seranova","year":"2017","journal-title":"Essays Biochem."},{"key":"10.1016\/j.jbc.2024.105641_bib5","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1038\/ncb0905-847","article-title":"The lysosome turns fifty","volume":"7","author":"de Duve","year":"2005","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib6","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/s41580-019-0185-4","article-title":"Lysosomes as dynamic regulators of cell and organismal homeostasis","volume":"21","author":"Ballabio","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib7","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1016\/j.bbadis.2012.11.014","article-title":"Human pathology in NCL","volume":"1832","author":"Anderson","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2024.105641_bib8","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.1016\/j.bbadis.2012.08.012","article-title":"The neuronal ceroid lipofuscinoses: a historical introduction","volume":"1832","author":"Haltia","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2024.105641_bib9","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/S1474-4422(18)30368-5","article-title":"Clinical challenges and future therapeutic approaches for neuronal ceroid lipofuscinosis","volume":"18","author":"Mole","year":"2019","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.jbc.2024.105641_bib10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13024-018-0300-6","article-title":"Emerging new roles of the lysosome and neuronal ceroid lipofuscinoses","volume":"14","author":"Mukherjee","year":"2019","journal-title":"Mol. Neurodegener"},{"key":"10.1016\/j.jbc.2024.105641_bib11","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s40265-020-01440-7","article-title":"Neuronal ceroid lipofuscinosis: potential for targeted therapy","volume":"81","author":"Specchio","year":"2021","journal-title":"Drugs"},{"key":"10.1016\/j.jbc.2024.105641_bib12","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1002\/ajmg.1320310606","article-title":"Batten disease: past, present, and future","volume":"5","author":"Rider","year":"1988","journal-title":"Am. J. Med. Genet. Suppl."},{"key":"10.1016\/j.jbc.2024.105641_bib13","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1002\/humu.21624","article-title":"Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses","volume":"33","author":"Kousi","year":"2012","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.jbc.2024.105641_bib14","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1111\/j.1469-8749.1974.tb04183.x","article-title":"Infantile type of so-called neuronal ceroid-lipofuscinosis","volume":"16","author":"Santavuori","year":"1974","journal-title":"Dev. Med. Child Neurol."},{"key":"10.1016\/j.jbc.2024.105641_bib15","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/376584a0","article-title":"Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis","volume":"376","author":"Vesa","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105641_bib16","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/S1474-4422(14)70142-5","article-title":"Oral cysteamine bitartrate and N-acetylcysteine for patients with infantile neuronal ceroid lipofuscinosis: a pilot study","volume":"13","author":"Levin","year":"2014","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.jbc.2024.105641_bib17","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/S1474-4422(14)70151-6","article-title":"Development of new treatments for Batten disease","volume":"13","author":"Mole","year":"2014","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.jbc.2024.105641_bib18","doi-asserted-by":"crossref","first-page":"22566","DOI":"10.1016\/S0021-9258(18)41567-0","article-title":"Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras","volume":"268","author":"Camp","year":"1993","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.105641_bib19","doi-asserted-by":"crossref","first-page":"5240","DOI":"10.1002\/j.1460-2075.1996.tb00909.x","article-title":"Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis","volume":"15","author":"Hellsten","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2024.105641_bib20","doi-asserted-by":"crossref","first-page":"15831","DOI":"10.1074\/jbc.271.26.15831","article-title":"Lysosomal targeting of palmitoyl-protein thioesterase","volume":"271","author":"Verkruyse","year":"1996","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.105641_bib21","doi-asserted-by":"crossref","first-page":"92","DOI":"10.3389\/fncel.2019.00092","article-title":"The interactome of palmitoyl-protein thioesterase 1 (PPT1) affects neuronal morphology and function","volume":"13","author":"Sapir","year":"2019","journal-title":"Front. Cell Neurosci."},{"key":"10.1016\/j.jbc.2024.105641_bib22","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/nrm2084","article-title":"Palmitoylation: policing protein stability and traffic","volume":"8","author":"Linder","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib23","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/0304-4157(89)90013-0","article-title":"Fatty acylation of proteins","volume":"988","author":"Schmidt","year":"1989","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2024.105641_bib24","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1038\/nrn2788","article-title":"Protein palmitoylation in neuronal development and synaptic plasticity","volume":"11","author":"Fukata","year":"2010","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.jbc.2024.105641_bib25","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1042\/BST20160236","article-title":"Protein S-palmitoylation in cellular differentiation","volume":"45","author":"Zhang","year":"2017","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jbc.2024.105641_bib26","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1083\/jcb.201008160","article-title":"The intracellular dynamic of protein palmitoylation","volume":"191","author":"Salaun","year":"2010","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib27","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3001590","article-title":"Identification of substrates of palmitoyl protein thioesterase 1 highlights roles of depalmitoylation in disulfide bond formation and synaptic function","volume":"20","author":"Gorenberg","year":"2022","journal-title":"PLoS Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib28","doi-asserted-by":"crossref","DOI":"10.1016\/j.cell.2017.02.004","article-title":"mTOR signaling in growth, metabolism, and disease","author":"Saxton","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib29","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/nrm3565","article-title":"Signals from the lysosome: a control centre for cellular clearance and energy metabolism","volume":"14","author":"Settembre","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib30","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/s41556-018-0244-7","article-title":"The lysosome as a cellular centre for signalling, metabolism and quality control","volume":"21","author":"Lawrence","year":"2019","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib31","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/s41580-019-0199-y","article-title":"mTOR at the nexus of nutrition, growth, ageing and disease","volume":"21","author":"Liu","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib32","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.tcb.2003.12.002","article-title":"Autophagy: in sickness and in health","volume":"14","author":"Cuervo","year":"2004","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib33","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.devcel.2020.06.010","article-title":"The lysosome at the intersection of cellular growth and destruction","volume":"54","author":"Shin","year":"2020","journal-title":"Dev. Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib34","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1038\/s41556-018-0148-6","article-title":"A\u00a0nutrient-induced affinity switch controls mTORC1 activation by its Rag GTPase-Ragulator lysosomal scaffold","volume":"20","author":"Lawrence","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib35","doi-asserted-by":"crossref","first-page":"903","DOI":"10.4161\/auto.19653","article-title":"MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB","volume":"8","author":"Martina","year":"2012","journal-title":"Autophagy"},{"key":"10.1016\/j.jbc.2024.105641_bib36","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1038\/nature04723","article-title":"Loss of autophagy in the central nervous system causes neurodegeneration in mice","volume":"441","author":"Komatsu","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105641_bib37","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.cell.2007.12.018","article-title":"Autophagy in the pathogenesis of disease","volume":"132","author":"Levine","year":"2008","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib38","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1038\/s41593-022-01084-8","article-title":"Faulty autolysosome acidification in Alzheimer's disease mouse models induces autophagic build-up of A\u03b2 in neurons, yielding senile plaques","volume":"25","author":"Lee","year":"2022","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.jbc.2024.105641_bib39","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1038\/nm.3232","article-title":"The role of autophagy in neurodegenerative disease","volume":"19","author":"Nixon","year":"2013","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2024.105641_bib40","doi-asserted-by":"crossref","first-page":"13566","DOI":"10.1073\/pnas.251485198","article-title":"Disruption of PPT1 or PPT2 causes neuronal ceroid lipofuscinosis in knockout mice","volume":"98","author":"Gupta","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.105641_bib41","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.nbd.2004.02.010","article-title":"Regional and cellular neuropathology in the palmitoyl protein thioesterase-1 null mutant mouse model of infantile neuronal ceroid lipofuscinosis","volume":"16","author":"Bible","year":"2004","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.jbc.2024.105641_bib42","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1038\/369756a0","article-title":"A\u00a0mammalian protein targeted by G1-arresting rapamycin-receptor complex","volume":"369","author":"Brown","year":"1994","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105641_bib43","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/0092-8674(94)90570-3","article-title":"RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs","volume":"78","author":"Sabatini","year":"1994","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib44","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1074\/jbc.270.2.815","article-title":"Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells","volume":"270","author":"Sabers","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.105641_bib45","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1038\/ncb2763","article-title":"Signal integration by mTORC1 coordinates nutrient input with biosynthetic output","volume":"15","author":"Dibble","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib46","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.655731","article-title":"The mTOR-autophagy Axis and the control of metabolism","volume":"9","author":"Deleyto-Seldas","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib47","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.neuron.2014.09.034","article-title":"The neurology of mTOR","volume":"84","author":"Lipton","year":"2014","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2024.105641_bib48","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1016\/j.neuron.2017.01.022","article-title":"Autophagy and neurodegeneration: pathogenic mechanisms and therapeutic opportunities","volume":"93","author":"Menzies","year":"2017","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2024.105641_bib49","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/j.neuron.2022.01.017","article-title":"The different autophagy degradation pathways and neurodegeneration","volume":"110","author":"Fleming","year":"2022","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2024.105641_bib50","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1038\/nrg2339","article-title":"Detecting genetic responses to environmental change","volume":"9","author":"Hoffmann","year":"2008","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.jbc.2024.105641_bib51","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1038\/nature03029","article-title":"The role of autophagy during the early neonatal starvation period","volume":"432","author":"Kuma","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105641_bib52","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/nature11745","article-title":"Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival","volume":"493","author":"Efeyan","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105641_bib53","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1126\/science.1232044","article-title":"A\u00a0Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1","volume":"340","author":"Bar-Peled","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.jbc.2024.105641_bib54","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/nature14190","article-title":"Nutrient-sensing mechanisms and pathways","volume":"517","author":"Efeyan","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105641_bib55","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1038\/ncb1753","article-title":"Regulation of TORC1 by Rag GTPases in nutrient response","volume":"10","author":"Kim","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib56","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1126\/science.1157535","article-title":"The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1","volume":"320","author":"Sancak","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.jbc.2024.105641_bib57","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/S0378-1119(99)00050-5","article-title":"Palmitoyl-protein thioesterase gene expression in the developing mouse brain and retina: implications for early loss of vision in infantile neuronal ceroid lipofuscinosis","volume":"231","author":"Zhang","year":"1999","journal-title":"Gene"},{"key":"10.1016\/j.jbc.2024.105641_bib58","doi-asserted-by":"crossref","DOI":"10.15252\/emmm.202012836","article-title":"The rapidly evolving view of lysosomal storage diseases","volume":"13","author":"Parenti","year":"2021","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.jbc.2024.105641_bib59","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1080\/15548627.2017.1378838","article-title":"Autophagy pathway: cellular and molecular mechanisms","volume":"14","author":"Yu","year":"2018","journal-title":"Autophagy"},{"key":"10.1016\/j.jbc.2024.105641_bib60","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1146\/annurev-cellbio-111315-125125","article-title":"The lysosome as a regulatory hub","volume":"32","author":"Perera","year":"2016","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib61","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1172\/JCI73939","article-title":"mTOR: a pharmacologic target for autophagy regulation","volume":"125","author":"Kim","year":"2015","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2024.105641_bib62","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1146\/annurev-physiol-012110-142317","article-title":"Lysosomal acidification mechanisms","volume":"74","author":"Mindell","year":"2012","journal-title":"Annu. Rev. Physiol."},{"key":"10.1016\/j.jbc.2024.105641_bib63","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1038\/nrm2272","article-title":"Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology","volume":"8","author":"Forgac","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1016\/j.jbc.2024.105641_bib64","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1126\/science.aan6298","article-title":"Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes","volume":"358","author":"Abu-Remaileh","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.jbc.2024.105641_bib65","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.1016\/j.celrep.2015.07.052","article-title":"Disruption of the rag-ragulator complex by c17orf59 inhibits mTORC1","volume":"12","author":"Schweitzer","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2024.105641_bib66","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms14612","article-title":"Misrouting of v-ATPase subunit V0a1 dysregulates lysosomal acidification in a neurodegenerative lysosomal storage disease model","volume":"8","author":"Bagh","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.105641_bib67","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1038\/nature14107","article-title":"SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1","volume":"519","author":"Rebsamen","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105641_bib68","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1126\/science.1257132","article-title":"Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1","volume":"347","author":"Wang","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.jbc.2024.105641_bib69","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/nmeth.1293","article-title":"Large-scale profiling of protein palmitoylation in mammalian cells","volume":"6","author":"Martin","year":"2009","journal-title":"Nat. Methods"},{"key":"10.1016\/j.jbc.2024.105641_bib70","doi-asserted-by":"crossref","first-page":"115","DOI":"10.3389\/fncel.2019.00115","article-title":"mTORC1 signaling is palmitoylation-dependent in hippocampal neurons and non-neuronal cells and involves dynamic palmitoylation of LAMTOR1 and mTOR","volume":"13","author":"Sanders","year":"2019","journal-title":"Front. Cell Neurosci."},{"key":"10.1016\/j.jbc.2024.105641_bib71","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1038\/s41467-017-01762-3","article-title":"Structural basis for the assembly of the Ragulator-Rag GTPase complex","volume":"8","author":"Yonehara","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.105641_bib72","article-title":"Detection of protein palmitoylation in cultured hippocampal neurons by immunoprecipitation and acyl-biotin exchange (ABE)","volume":"72","author":"Brigidi","year":"2013","journal-title":"J.\u00a0Vis. Exp."},{"key":"10.1016\/j.jbc.2024.105641_bib73","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1093\/protein\/gzn039","article-title":"CSS-Palm 2.0: an updated software for palmitoylation sites prediction","volume":"21","author":"Ren","year":"2008","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jbc.2024.105641_bib74","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1194\/jlr.D011106","article-title":"Site-specific analysis of protein S-acylation by resin-assisted capture","volume":"52","author":"Forrester","year":"2011","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jbc.2024.105641_bib75","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/j.tcb.2015.06.002","article-title":"Regulation of mTORC1 by PI3K signaling","volume":"25","author":"Dibble","year":"2015","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib76","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/j.cell.2013.11.049","article-title":"Spatial control of the TSC complex integrates insulin and nutrient regulation of mTORC1 at the lysosome","volume":"156","author":"Menon","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib77","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.cell.2017.04.001","article-title":"AKT\/PKB signaling: navigating the network","volume":"169","author":"Manning","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib78","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1111\/j.1749-6632.2009.05117.x","article-title":"The tuberous sclerosis complex","volume":"1184","author":"Orlova","year":"2010","journal-title":"Ann. N. Y Acad. Sci."},{"key":"10.1016\/j.jbc.2024.105641_bib79","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1016\/j.molmed.2011.07.008","article-title":"mTOR: a pathogenic signaling pathway in developmental brain malformations","volume":"17","author":"Crino","year":"2011","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.jbc.2024.105641_bib80","doi-asserted-by":"crossref","first-page":"7273","DOI":"10.3390\/ijms22147273","article-title":"Effects of mutations in TSC genes on neurodevelopment and synaptic transmission","volume":"22","author":"Bassetti","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2024.105641_bib81","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1172\/JCI96342","article-title":"Tuberous sclerosis complex-associated CNS abnormalities depend on hyperactivation of mTORC1 and Akt","volume":"128","author":"Zordan","year":"2018","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2024.105641_bib82","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2022.111278","article-title":"DEPDC5-dependent mTORC1 signaling mechanisms are critical for the anti-seizure effects of acute fasting","volume":"40","author":"Yuskaitis","year":"2022","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2024.105641_bib83","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1042\/BST0370217","article-title":"A\u00a0complex interplay between Akt, TSC2 and the two mTOR complexes","volume":"37","author":"Huang","year":"2009","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jbc.2024.105641_bib84","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1038\/nature25023","article-title":"Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40","volume":"552","author":"Yang","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2024.105641_bib85","doi-asserted-by":"crossref","first-page":"15619","DOI":"10.1074\/jbc.M800723200","article-title":"Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation","volume":"283","author":"Wang","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.105641_bib86","doi-asserted-by":"crossref","first-page":"6541","DOI":"10.1002\/j.1460-2075.1996.tb01045.x","article-title":"Mechanism of activation of protein kinase B by insulin and IGF-1","volume":"15","author":"Alessi","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2024.105641_bib87","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202004010","article-title":"mTORC1 activity is supported by spatial association with focal adhesions","volume":"220","author":"Rabanal-Ruiz","year":"2021","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib88","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.19960","article-title":"Dynamics of mTORC1 activation in response to amino acids","volume":"5","author":"Manifava","year":"2016","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2024.105641_bib89","doi-asserted-by":"crossref","first-page":"883","DOI":"10.2174\/1568026620666200224101808","article-title":"Akt pathway inhibitors","volume":"20","author":"Uko","year":"2020","journal-title":"Curr. Top Med. Chem."},{"key":"10.1016\/j.jbc.2024.105641_bib90","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1146\/annurev-med-050715-104343","article-title":"Innate immunity and neurodegeneration","volume":"69","author":"Labzin","year":"2018","journal-title":"Annu. Rev. Med."},{"key":"10.1016\/j.jbc.2024.105641_bib91","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1172\/JCI58644","article-title":"Innate immunity in the central nervous system","volume":"122","author":"Ransohoff","year":"2012","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.jbc.2024.105641_bib92","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1002\/jimd.12379","article-title":"In a mouse model of INCL reduced S-palmitoylation of cytosolic thioesterase APT1 contributes to microglia proliferation and neuroinflammation","volume":"44","author":"Sadhukhan","year":"2021","journal-title":"J.\u00a0Inherit. Metab. Dis."},{"key":"10.1016\/j.jbc.2024.105641_bib93","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1042\/BST20140188","article-title":"Astrocytosis in infantile neuronal\u00a0ceroid lipofuscinosis: friend or foe?","volume":"42","author":"Shyng","year":"2014","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jbc.2024.105641_bib94","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1089\/neu.1994.11.187","article-title":"The rotarod test: an evaluation of its effectiveness in assessing motor deficits following traumatic brain injury","volume":"11","author":"Hamm","year":"1994","journal-title":"J.\u00a0Neurotrauma"},{"key":"10.1016\/j.jbc.2024.105641_bib95","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1016\/j.cell.2012.07.032","article-title":"Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1","volume":"150","author":"Bar-Peled","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib96","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.cell.2010.02.024","article-title":"Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids","volume":"141","author":"Sancak","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2024.105641_bib97","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1146\/annurev-med-122313-085916","article-title":"Lysosomal storage diseases: from pathophysiology to therapy","volume":"66","author":"Parenti","year":"2015","journal-title":"Annu. Rev. Med."},{"key":"10.1016\/j.jbc.2024.105641_bib98","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.neuron.2021.12.029","article-title":"Brain-derived autophagosome profiling reveals the engulfment of nucleoid-enriched mitochondrial fragments by basal autophagy in neurons","volume":"110","author":"Goldsmith","year":"2022","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2024.105641_bib99","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.neuroscience.2016.11.017","article-title":"Molecular neurobiology of mTOR","volume":"341","author":"Switon","year":"2016","journal-title":"Neuroscience"},{"key":"10.1016\/j.jbc.2024.105641_bib100","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1126\/science.1207056","article-title":"mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase","volume":"334","author":"Zoncu","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.jbc.2024.105641_bib101","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1007\/978-94-007-3012-0_4","article-title":"Phosphoinositide 3-kinase- a historical perspective","volume":"58","author":"Toker","year":"2012","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.jbc.2024.105641_bib102","doi-asserted-by":"crossref","first-page":"137","DOI":"10.3390\/biom10010137","article-title":"Microglia mediated neuroinflammation: focus on PI3K modulation","volume":"10","author":"Cianciulli","year":"2020","journal-title":"Biomolecules"},{"key":"10.1016\/j.jbc.2024.105641_bib103","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.626404","article-title":"Akt is S-palmitoylated: a new layer of regulation for Akt","volume":"9","author":"Blaustein","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2024.105641_bib104","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1111\/j.1365-2818.2006.01706.x","article-title":"A\u00a0guided tour into subcellular colocalization analysis in light microscopy","volume":"224","author":"Bolte","year":"2006","journal-title":"J.\u00a0Microsc."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824000176?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824000176?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T00:52:20Z","timestamp":1758243140000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925824000176"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,2]]},"references-count":104,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2024,2]]}},"alternative-id":["S0021925824000176"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2024.105641","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2024,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Disruption of lysosomal nutrient sensing scaffold contributes to pathogenesis of a fatal neurodegenerative lysosomal storage disease","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2024.105641","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"105641"}}