A lysosome-centered view of nutrient homeostasis

References

• Sleat DE, Della Valle MC, Zheng H, Moore DF, Lobel P. The mannose 6-phosphate glycoprotein proteome. J Proteome Res 2008; 7:3010-21; PMID:18507433; http://dx.doi.org/10.1021/pr800135v
   PubMed Web of Science ®Google Scholar
• Eskelinen EL, Tanaka Y, Saftig P. At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol 2003; 13:137-45; PMID:12628346; http://dx.doi.org/10.1016/S0962-8924(03)00005-9
   PubMed Web of Science ®Google Scholar
• Bainton DF. The Discovery of Lysosomes. J Cell Biol 1981; 91:S66-S76; http://dx.doi.org/10.1083/jcb.91.3.66s
   PubMed Web of Science ®Google Scholar
• Okamoto K. Organellophagy: eliminating cellular building blocks via selective autophagy. J Cell Biol 2014; 205:435-45; PMID:24862571; http://dx.doi.org/10.1083/jcb.201402054
   PubMed Web of Science ®Google Scholar
• Zoncu R, Efeyan A, Sabatini DM. mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol 2011; 12:21-35; PMID:21157483; http://dx.doi.org/10.1038/nrm3025
   PubMed Web of Science ®Google Scholar
• Sancak Y, Bar-Peled L, Zoncu R, Markhard AL, Nada S, Sabatini DM. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 2010; 141:290-303; PMID:20381137; http://dx.doi.org/10.1016/j.cell.2010.02.024
   PubMed Web of Science ®Google Scholar
• Efeyan A, Sabatini DM. Nutrients and growth factors in mTORC1 activation. Biochem Society Transactions 2013; 41:902-5; http://dx.doi.org/10.1042/BST20130063
   PubMed Web of Science ®Google Scholar
• Settembre C, Fraldi A, Medina DL, Ballabio A. Signals from the lysosome: a control centre for cellular clearance and energy metabolism. Nat Rev Mol Cell Biol 2013; 14:283-96; PMID:23609508; http://dx.doi.org/10.1038/nrm3565
   PubMed Web of Science ®Google Scholar
• Bar-Peled L, Schweitzer LD, Zoncu R, Sabatini DM. Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell 2012; 150:1196-208; PMID:22980980; http://dx.doi.org/10.1016/j.cell.2012.07.032
   PubMed Web of Science ®Google Scholar
• Kim E, Goraksha-Hicks P, Li L, Neufeld TP, Guan KL. Regulation of TORC1 by Rag GTPases in nutrient response. Nat Cell Biol 2008; 10:935-45; PMID:18604198; http://dx.doi.org/10.1038/ncb1753
   PubMed Web of Science ®Google Scholar
• Jewell JL, Kim YC, Russell RC, Yu FX, Park HW, Plouffe SW, Tagliabracci VS, Guan KL. Metabolism. Differential regulation of mTORC1 by leucine and glutamine. Science 2015; 347:194-8; PMID:25567907; http://dx.doi.org/10.1126/science.1259472
   PubMed Web of Science ®Google Scholar
• Rebsamen M, Pochini L, Stasyk T, de Araujo ME, Galluccio M, Kandasamy RK, Snijder B, Fauster A, Rudashevskaya EL, Bruckner M, et al. SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1. Nature 2015; 519:477-81; PMID:25561175; http://dx.doi.org/10.1038/nature14107
   PubMed Web of Science ®Google Scholar
• Wang S, Tsun ZY, Wolfson RL, Shen K, Wyant GA, Plovanich ME, Yuan ED, Jones TD, Chantranupong L, Comb W, et al. Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1. Science 2015; 347:188-94; PMID:25567906; http://dx.doi.org/10.1126/science.1257132
   PubMed Web of Science ®Google Scholar
• Schweitzer LD, Comb WC, Bar-Peled L, Sabatini DM. Disruption of the Rag-Ragulator Complex by c17orf59 Inhibits mTORC1. Cell Reports 2015; 12:1445-55; PMID:26299971; http://dx.doi.org/10.1016/j.celrep.2015.07.052
   PubMed Web of Science ®Google Scholar
• Pu J, Schindler C, Jia R, Jarnik M, Backlund P, Bonifacino JS. BORC, a Multisubunit Complex that Regulates Lysosome Positioning. Developmental Cell 2015; 33:176-88; PMID:25898167; http://dx.doi.org/10.1016/j.devcel.2015.02.011
   PubMed Web of Science ®Google Scholar
• Duran A, Amanchy R, Linares JF, Joshi J, Abu-Baker S, Porollo A, Hansen M, Moscat J, Diaz-Meco MT. p62 Is a Key Regulator of Nutrient Sensing in the mTORC1 Pathway. Mol Cell 2011; 44:134-46; PMID:21981924; http://dx.doi.org/10.1016/j.molcel.2011.06.038
   PubMed Web of Science ®Google Scholar
• Linares JF, Duran A, Yajima T, Pasparakis M, Moscat J, Diaz-Meco MT. K63 Polyubiquitination and Activation of mTOR by the p62-TRAF6 complex in nutrient-activated cells. Mol Cell 2013; 51:283-96; PMID:23911927; http://dx.doi.org/10.1016/j.molcel.2013.06.020
   PubMed Web of Science ®Google Scholar
• Bar-Peled L, Chantranupong L, Cherniack AD, Chen WW, Ottina KA, Grabiner BC, Spear ED, Carter SL, Meyerson M, Sabatini DM. A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1. Science 2013; 340:1100-6; PMID:23723238; http://dx.doi.org/10.1126/science.1232044
   PubMed Web of Science ®Google Scholar
• Panchaud N, Peli-Gulli MP, De Virgilio C. Amino acid deprivation inhibits TORC1 through a GTPase-activating protein complex for the Rag family GTPase Gtr1. Sci Signal 2013; 6:ra42; PMID:23716719; http://dx.doi.org/10.1126/scisignal.2004112
   PubMed Web of Science ®Google Scholar
• Chantranupong L, Wolfson RL, Orozco JM, Saxton RA, Scaria SM, Bar-Peled L, Spooner E, Isasa M, Gygi SP, Sabatini DM. The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1. Cell Reports 2014; 9:1-8; PMID:25263562; http://dx.doi.org/10.1016/j.celrep.2014.09.014
   PubMed Web of Science ®Google Scholar
• Parmigiani A, Nourbakhsh A, Ding B, Wang W, Kim YC, Akopiants K, Guan KL, Karin M, Budanov AV. Sestrins inhibit mTORC1 kinase activation through the GATOR complex. Cell Reports 2014; 9:1281-91; PMID:25457612; http://dx.doi.org/10.1016/j.celrep.2014.10.019
   PubMed Web of Science ®Google Scholar
• Peng M, Yin N, Li MO. Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling. Cell 2014; 159:122-33; PMID:25259925; http://dx.doi.org/10.1016/j.cell.2014.08.038
   PubMed Web of Science ®Google Scholar
• Zoncu R, Bar-Peled L, Efeyan A, Wang S, Sancak Y, Sabatini DM. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 2011; 334:678-83; PMID:22053050; http://dx.doi.org/10.1126/science.1207056
   PubMed Web of Science ®Google Scholar
• Stransky LA, Forgac M. Amino Acid Availability Modulates Vacuolar H+-ATPase assembly. J Biol Chem 2015; 290:27360-9; PMID:26378229; http://dx.doi.org/10.1074/jbc.M115.659128
   PubMed Web of Science ®Google Scholar
• Sancak Y, Peterson TR, Shaul YD, Lindquist RA, Thoreen CC, Bar-Peled L, Sabatini DM. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 2008; 320:1496-501; PMID:18497260; http://dx.doi.org/10.1126/science.1157535
   PubMed Web of Science ®Google Scholar
• Oshiro N, Rapley J, Avruch J. Amino Acids Activate Mammalian Target of Rapamycin (mTOR) Complex 1 without Changing Rag GTPase guanyl nucleotide charging. J Biol Chem 2014; 289:2658-74; PMID:24337580; http://dx.doi.org/10.1074/jbc.M113.528505
   PubMed Web of Science ®Google Scholar
• Demetriades C, Doumpas N, Teleman AA. Regulation of TORC1 in response to amino acid starvation via lysosomal recruitment of TSC2. Cell 2014; 156:786-99; PMID:24529380; http://dx.doi.org/10.1016/j.cell.2014.01.024
   PubMed Web of Science ®Google Scholar
• Tee AR, Manning BD, Roux PP, Cantley LC, Blenis J. Tuberous sclerosis complex gene products, Tuberin and Hamartin, control mTOR signaling by acting as a GTPase-activating protein complex toward Rheb. Curr Biol 2003; 13:1259-68; PMID:12906785; http://dx.doi.org/10.1016/S0960-9822(03)00506-2
   PubMed Web of Science ®Google Scholar
• Inoki K, Li Y, Xu T, Guan KL. Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling. Genes Dev 2003; 17:1829-34; PMID:12869586; http://dx.doi.org/10.1101/gad.1110003
   PubMed Web of Science ®Google Scholar
• Long X, Lin Y, Ortiz-Vega S, Yonezawa K, Avruch J. Rheb binds and regulates the mTOR kinase. Curr Biol 2005; 15:702-13; PMID:15854902; http://dx.doi.org/10.1016/j.cub.2005.02.053
   PubMed Web of Science ®Google Scholar
• Manning BD, Tee AR, Logsdon MN, Blenis J, Cantley LC. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol Cell 2002; 10:151-62; PMID:12150915; http://dx.doi.org/10.1016/S1097-2765(02)00568-3
   PubMed Web of Science ®Google Scholar
• Inoki K, Li Y, Zhu TQ, Wu J, Guan KL. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat Cell Biol 2002; 4:648-57; PMID:12172553; http://dx.doi.org/10.1038/ncb839
   PubMed Web of Science ®Google Scholar
• Potter CJ, Pedraza LG, Xu T. Akt regulates growth by directly phosphorylating Tsc2. Nat Cell Biol 2002; 4:658-65; PMID:12172554; http://dx.doi.org/10.1038/ncb840
   PubMed Web of Science ®Google Scholar
• Menon S, Dibble CC, Talbott G, Hoxhaj G, Valvezan AJ, Takahashi H, Cantley LC, Manning BD. Spatial control of the TSC complex integrates insulin and nutrient regulation of mTORC1 at the lysosome. Cell 2014; 156:771-85; PMID:24529379; http://dx.doi.org/10.1016/j.cell.2013.11.049
   PubMed Web of Science ®Google Scholar
• Lee MN, Ha SH, Kim J, Koh A, Lee CS, Kim JH, Jeon H, Kim DH, Suh PG, Ryu SH. Glycolytic flux signals to mTOR through glyceraldehyde-3-phosphate dehydrogenase-mediated regulation of Rheb. Mol Cell Biol 2009; 29:3991-4001; PMID:19451232; http://dx.doi.org/10.1128/MCB.00165-09
   PubMed Web of Science ®Google Scholar
• Inoki K, Zhu T, Guan KL. TSC2 mediates cellular energy response to control cell growth and survival. Cell 2003; 115:577-90; PMID:14651849; http://dx.doi.org/10.1016/S0092-8674(03)00929-2
   PubMed Web of Science ®Google Scholar
• Kim J, Kundu M, Viollet B, Guan KL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 2011; 13:132-41; PMID:21258367; http://dx.doi.org/10.1038/ncb2152
   PubMed Web of Science ®Google Scholar
• Yasuda M, Tanaka Y, Kume S, Morita Y, Chin-Kanasaki M, Araki H, Isshiki K, Araki S, Koya D, Haneda M, et al. Fatty acids are novel nutrient factors to regulate mTORC1 lysosomal localization and apoptosis in podocytes. Biochimica Et Biophysica Acta 2014; 1842:1097-108; PMID:24726883; http://dx.doi.org/10.1016/j.bbadis.2014.04.001
   PubMed Web of Science ®Google Scholar
• Kwon B, Querfurth HW. Palmitate activates mTOR/p70S6K through AMPK inhibition and hypophosphorylation of raptor in skeletal muscle cells: Reversal by oleate is similar to metformin. Biochimie 2015; 118:141-50; PMID:26344902; http://dx.doi.org/10.1016/j.biochi.2015.09.006
   PubMed Web of Science ®Google Scholar
• Gwinn DM, Shackelford DB, Egan DF, Mihaylova MM, Mery A, Vasquez DS, Turk BE, Shaw RJ. AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol Cell 2008; 30:214-26; PMID:18439900; http://dx.doi.org/10.1016/j.molcel.2008.03.003
   PubMed Web of Science ®Google Scholar
• Inoki K, Ouyang H, Zhu T, Lindvall C, Wang Y, Zhang X, Yang Q, Bennett C, Harada Y, Stankunas K, et al. TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth. Cell 2006; 126:955-68; PMID:16959574; http://dx.doi.org/10.1016/j.cell.2006.06.055
   PubMed Web of Science ®Google Scholar
• Zhang CS, Jiang B, Li M, Zhu M, Peng Y, Zhang YL, Wu YQ, Li TY, Liang Y, Lu Z, et al. The lysosomal v-ATPase-Ragulator complex is a common activator for AMPK and mTORC1, acting as a switch between catabolism and anabolism. Cell Metab 2014; 20:526-40; PMID:25002183; http://dx.doi.org/10.1016/j.cmet.2014.06.014
   PubMed Web of Science ®Google Scholar
• Korolchuk VI, Saiki S, Lichtenberg M, Siddiqi FH, Roberts EA, Imarisio S, Jahreiss L, Sarkar S, Futter M, Menzies FM, et al. Lysosomal positioning coordinates cellular nutrient responses. Nat Cell Biol 2011; 13:453-60; PMID:21394080; http://dx.doi.org/10.1038/ncb2204
   PubMed Web of Science ®Google Scholar
• Sardiello M, Palmieri M, di Ronza A, Medina DL, Valenza M, Gennarino VA, Di Malta C, Donaudy F, Embrione V, Polishchuk RS, et al. A gene network regulating lysosomal biogenesis and function. Science 2009; 325:473-7; PMID:19556463
   PubMed Web of Science ®Google Scholar
• Hemesath TJ, Steingrimsson E, McGill G, Hansen MJ, Vaught J, Hodgkinson CA, Arnheiter H, Copeland NG, Jenkins NA, Fisher DE. microphthalmia, a critical factor in melanocyte development, defines a discrete transcription factor family. Genes Dev 1994; 8:2770-80; PMID:7958932; http://dx.doi.org/10.1101/gad.8.22.2770
   PubMed Web of Science ®Google Scholar
• Martina JA, Diab HI, Lishu L, Jeong AL, Patange S, Raben N, Puertollano R. The nutrient-responsive transcription factor TFE3 promotes autophagy, lysosomal biogenesis, and clearance of cellular debris. Sci Signal 2014; 7:ra9; PMID:24448649; http://dx.doi.org/10.1126/scisignal.2004754
   PubMed Web of Science ®Google Scholar
• Martina JA, Puertollano R. Rag GTPases mediate amino acid-dependent recruitment of TFEB and MITF to lysosomes. J Cell Biol 2013; 200:475-91; PMID:23401004; http://dx.doi.org/10.1083/jcb.201209135
   PubMed Web of Science ®Google Scholar
• Roczniak-Ferguson A, Petit CS, Froehlich F, Qian S, Ky J, Angarola B, Walther TC, Ferguson SM. The transcription factor TFEB links mTORC1 signaling to transcriptional control of lysosome homeostasis. Sci Signal 2012; 5:ra42; PMID:22692423; http://dx.doi.org/10.1126/scisignal.2002790
   PubMed Web of Science ®Google Scholar
• Bronisz A, Sharma SM, Hu R, Godlewski J, Tzivion G, Mansky KC, Ostrowski MC. Microphthalmia-associated transcription factor interactions with 14-3-3 modulate differentiation of committed myeloid precursors. Mol Biol Cell 2006; 17:3897-906; PMID:16822840; http://dx.doi.org/10.1091/mbc.E06-05-0470
   PubMed Web of Science ®Google Scholar
• Martina JA, Chen Y, Gucek M, Puertollano R. MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy 2012; 8:903-14; PMID:22576015; http://dx.doi.org/10.4161/auto.19653
   PubMed Web of Science ®Google Scholar
• Settembre C, Zoncu R, Medina DL, Vetrini F, Erdin S, Huynh T, Ferron M, Karsenty G, Vellard MC, Facchinetti V, et al. A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB. EMBO J 2012; 31:1095-108; PMID:22343943; http://dx.doi.org/10.1038/emboj.2012.32
   PubMed Web of Science ®Google Scholar
• Munson MJ, Allen GFG, Toth R, Campbell DG, Lucocq JM, Ganley IG. mTOR activates the VPS34-UVRAG complex to regulate autolysosomal tubulation and cell survival. Embo J 2015; 34:2272-90; PMID:26139536; http://dx.doi.org/10.15252/embj.201590992
   PubMed Web of Science ®Google Scholar
• Cang C, Zhou Y, Navarro B, Seo YJ, Aranda K, Shi L, Battaglia-Hsu S, Nissim I, Clapham DE, Ren D. mTOR regulates lysosomal ATP-sensitive two-pore Na(+) channels to adapt to metabolic state. Cell 2013; 152:778-90; PMID:23394946; http://dx.doi.org/10.1016/j.cell.2013.01.023
   PubMed Web of Science ®Google Scholar
• Wang W, Gao Q, Yang M, Zhang X, Yu L, Lawas M, Li X, Bryant-Genevier M, Southall NT, Marugan J, et al. Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation. Proc Natl Acad Sci U S A 2015; 112:E1373-81; PMID:25733853; http://dx.doi.org/10.1073/pnas.1419669112
   PubMed Web of Science ®Google Scholar
• Wang X, Zhang XL, Dong XP, Samie M, Li XR, Cheng XP, Goschka A, Shen DB, Zhou YD, Harlow J, et al. TPC Proteins Are Phosphoinositide-Activated Sodium-Selective Ion Channels in Endosomes and Lysosomes. Cell 2012; 151:372-83; PMID:23063126; http://dx.doi.org/10.1016/j.cell.2012.08.036
   PubMed Web of Science ®Google Scholar
• Dong XP, Shen DBA, Wang X, Dawson T, Li XR, Zhang Q, Cheng XP, Zhang YL, Weisman LS, Delling M, et al. PI(3,5)P-2 controls membrane trafficking by direct activation of mucolipin Ca2+ release channels in the endolysosome. Nat Commun 2010; 1:38; http://dx.doi.org/10.1038/ncomms1037
   PubMed Web of Science ®Google Scholar
• Boustany RMN. Lysosomal storage diseases-the horizon expands. Nat Rev Neurol 2013; 9:583-98; PMID:23938739; http://dx.doi.org/10.1038/nrneurol.2013.163
   PubMed Web of Science ®Google Scholar
• Filocamo M, Morrone A. Lysosomal storage disorders: molecular basis and laboratory testing. Human Genomics 2011; 5:156-69; PMID:21504867; http://dx.doi.org/10.1186/1479-7364-5-3-156
   PubMedGoogle Scholar
• van der Ploeg AT, Reuser AJ. Pompe's disease. Lancet 2008; 372:1342-53; PMID:18929906; http://dx.doi.org/10.1016/S0140-6736(08)61555-X
   PubMed Web of Science ®Google Scholar
• Anderson RA, Rao N, Byrum RS, Rothschild CB, Bowden DW, Hayworth R, Pettenati M. In situ localization of the genetic locus encoding the lysosomal acid lipase/cholesteryl esterase (LIPA) deficient in Wolman disease to chromosome 10q23.2-q23.3. Genomics 1993; 15:245-7; PMID:8432549; http://dx.doi.org/10.1006/geno.1993.1052
   PubMed Web of Science ®Google Scholar
• Hesselink RP, Wagenmakers AJ, Drost MR, Van der Vusse GJ. Lysosomal dysfunction in muscle with special reference to glycogen storage disease type II. Biochimica Et Biophysica Acta 2003; 1637:164-70; PMID:12633905; http://dx.doi.org/10.1016/S0925-4439(02)00229-6
   PubMed Web of Science ®Google Scholar
• Manganelli F, Ruggiero L. Clinical features of Pompe disease. Acta Myol 2013; 32:82-4; PMID:24399863
   PubMedGoogle Scholar
• Verheijen FW, Verbeek E, Aula N, Beerens CE, Havelaar AC, Joosse M, Peltonen L, Aula P, Galjaard H, van der Spek PJ, et al. A new gene, encoding an anion transporter, is mutated in sialic acid storage diseases. Nat Genetics 1999; 23:462-5; PMID:10581036; http://dx.doi.org/10.1038/70585
   PubMed Web of Science ®Google Scholar
• Mancini GMS, Beerens CEMT, Verheijen FW. Glucose-Transport in Lysosomal Membrane-Vesicles - Kinetic Demonstration of a Carrier for Neutral Hexoses. J Biol Chem 1990; 265:12380-7; PMID:2373697
   PubMed Web of Science ®Google Scholar
• Maguire GA, Docherty K, Hales CN. Sugar-Transport in Rat-Liver Lysosomes - Direct Demonstration by Using Labeled Sugars. Biochem J 1983; 212:211-8; PMID:6409099; http://dx.doi.org/10.1042/bj2120211
   PubMed Web of Science ®Google Scholar
• Augustin R, Riley J, Moley KH. GLUT8 contains a [DE]XXXL[LI] sorting motif and localizes to a late endosomal/lysosomal compartment. Traffic 2005; 6:1196-212; PMID:16262729; http://dx.doi.org/10.1111/j.1600-0854.2005.00354.x
   PubMed Web of Science ®Google Scholar
• Goldstein JL, Brown MS, Anderson RG, Russell DW, Schneider WJ. Receptor-mediated endocytosis: concepts emerging from the LDL receptor system. Annual Rev Cell Biol 1985; 1:1-39; http://dx.doi.org/10.1146/annurev.cb.01.110185.000245
   PubMedGoogle Scholar
• Brown MS, Goldstein JL. A receptor-mediated pathway for cholesterol homeostasis. Science 1986; 232:34-47; PMID:3513311; http://dx.doi.org/10.1126/science.3513311
   PubMed Web of Science ®Google Scholar
• Goldstein JL, Dana SE, Faust JR, Beaudet AL, Brown MS. Role of lysosomal acid lipase in the metabolism of plasma low density lipoprotein. Observations in cultured fibroblasts from a patient with cholesteryl ester storage disease. J Biol Chem 1975; 250:8487-95; PMID:172501
   PubMed Web of Science ®Google Scholar
• Bona G, Bracco G, Gallina MR, Iavarone A, Artesani L, Perona A, Zaffaroni M. A case of acid lipase deficiency: Wolman's disease. Panminerva Medica 1989; 31:49-53; PMID:2726290
   PubMed Web of Science ®Google Scholar
• Sokol J, Blanchette-Mackie J, Kruth HS, Dwyer NK, Amende LM, Butler JD, Robinson E, Patel S, Brady RO, Comly ME, et al. Type C Niemann-Pick disease. Lysosomal accumulation and defective intracellular mobilization of low density lipoprotein cholesterol. J Biol Chem 1988; 263:3411-7; PMID:3277970
   PubMed Web of Science ®Google Scholar
• Carstea ED, Morris JA, Coleman KG, Loftus SK, Zhang D, Cummings C, Gu J, Rosenfeld MA, Pavan WJ, Krizman DB, et al. Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis. Science 1997; 277:228-31; PMID:9211849; http://dx.doi.org/10.1126/science.277.5323.228
   PubMed Web of Science ®Google Scholar
• Singh R, Kaushik S, Wang Y, Xiang Y, Novak I, Komatsu M, Tanaka K, Cuervo AM, Czaja MJ. Autophagy regulates lipid metabolism. Nature 2009; 458:1131-5; PMID:19339967; http://dx.doi.org/10.1038/nature07976
   PubMed Web of Science ®Google Scholar
• Schroeder B, Schulze RJ, Weller SG, Sletten AC, Casey CA, McNiven MA. The small GTPase Rab7 as a central regulator of hepatocellular lipophagy. Hepatol 2015; 61:1896-907; http://dx.doi.org/10.1002/hep.27667
   PubMed Web of Science ®Google Scholar
• Czaja MJ, Cuervo AM. Lipases in lysosomes, what for? Autophagy 2009; 5:866-7; PMID:19502773; http://dx.doi.org/10.4161/auto.9040
   PubMed Web of Science ®Google Scholar
• Kovsan J, Bashan N, Greenberg AS, Rudich A. Potential role of autophagy in modulation of lipid metabolism. Am J Physiol Endocrinol Metab 2010; 298:E1-7; PMID:19887596; http://dx.doi.org/10.1152/ajpendo.00562.2009
   PubMed Web of Science ®Google Scholar
• O'Rourke EJ, Ruvkun G. MXL-3 and HLH-30 transcriptionally link lipolysis and autophagy to nutrient availability. Nat Cell Biol 2013; 15:668-76; PMID:23604316; http://dx.doi.org/10.1038/ncb2741
   PubMed Web of Science ®Google Scholar
• Grove CA, De Masi F, Barrasa MI, Newburger DE, Alkema MJ, Bulyk ML, Walhout AJ. A multiparameter network reveals extensive divergence between C. elegans bHLH transcription factors. Cell 2009; 138:314-27; PMID:19632181; http://dx.doi.org/10.1016/j.cell.2009.04.058
   PubMed Web of Science ®Google Scholar
• Jandrositz A, Petschnigg J, Zimmermann R, Natter K, Scholze H, Hermetter A, Kohlwein SD, Leber R. The lipid droplet enzyme Tgl1p hydrolyzes both steryl esters and triglycerides in the yeast, Saccharomyces cerevisiae. Biochim Et Biophysica Acta 2005; 1735:50-8; http://dx.doi.org/10.1016/j.bbalip.2005.04.005
   PubMed Web of Science ®Google Scholar
• Folick A, Oakley HD, Yu Y, Armstrong EH, Kumari M, Sanor L, Moore DD, Ortlund EA, Zechner R, Wang MC. Aging. Lysosomal signaling molecules regulate longevity in Caenorhabditis elegans. Science 2015; 347:83-6; PMID:25554789; http://dx.doi.org/10.1126/science.1258857
   PubMed Web of Science ®Google Scholar
• Du H, Heur M, Duanmu M, Grabowski GA, Hui DY, Witte DP, Mishra JY. Lysosomal acid lipase-deficient mice: depletion of white and brown fat, severe hepatosplenomegaly, and shortened life span. J Lipid Res 2001; 42:489-500; PMID:11290820
   PubMed Web of Science ®Google Scholar
• Schneider JL, Suh Y, Cuervo AM. Deficient chaperone-mediated autophagy in liver leads to metabolic dysregulation. Cell Metab 2014; 20:417-32; PMID:25043815; http://dx.doi.org/10.1016/j.cmet.2014.06.009
   PubMed Web of Science ®Google Scholar
• Cuervo AM, Knecht E, Terlecky SR, Dice JF. Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am J Physiol 1995; 269:C1200-8; PMID:7491910
   PubMed Web of Science ®Google Scholar
• Kaushik S, Cuervo AM. Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis. Nat Cell Biol 2015; 17:759-70; PMID:25961502; http://dx.doi.org/10.1038/ncb3166
   PubMed Web of Science ®Google Scholar
• Rambold AS, Cohen S, Lippincott-Schwartz J. Fatty Acid Trafficking in Starved Cells: Regulation by Lipid Droplet Lipolysis, Autophagy, and Mitochondrial Fusion Dynamics. Dev Cell 2015; 32:678-92; PMID:25752962; http://dx.doi.org/10.1016/j.devcel.2015.01.029
   PubMed Web of Science ®Google Scholar
• Dunn WA, Jr. Studies on the mechanisms of autophagy: formation of the autophagic vacuole. J Cell Biol 1990; 110:1923-33; PMID:2351689; http://dx.doi.org/10.1083/jcb.110.6.1923
   PubMed Web of Science ®Google Scholar
• Yang Z, Huang J, Geng J, Nair U, Klionsky DJ. Atg22 recycles amino acids to link the degradative and recycling functions of autophagy. Mol Biol Cell 2006; 17:5094-104; PMID:17021250; http://dx.doi.org/10.1091/mbc.E06-06-0479
   PubMed Web of Science ®Google Scholar
• Kominami E, Tsukahara T, Bando Y, Katunuma N. Distribution of cathepsins B and H in rat tissues and peripheral blood cells. J Biochem 1985; 98:87-93; PMID:3900059
   PubMed Web of Science ®Google Scholar
• Ii K, Hizawa K, Kominami E, Bando Y, Katunuma N. Different immunolocalizations of cathepsins B, H, and L in the liver. J Histochem Cytochem 1985; 33:1173-5; PMID:4056381; http://dx.doi.org/10.1177/33.11.4056381
   PubMed Web of Science ®Google Scholar
• Baricos WH, Zhou YW, Fuerst RS, Barrett AJ, Shah SV. The role of aspartic and cysteine proteinases in albumin degradation by rat kidney cortical lysosomes. Arch Biochem Biophy 1987; 256:687-91; http://dx.doi.org/10.1016/0003-9861(87)90625-4
   PubMed Web of Science ®Google Scholar
• Massey AC, Zhang C, Cuervo AM. Chaperone-mediated autophagy in aging and disease. Curr Topics Dev Biol 2006; 73:205-35; http://dx.doi.org/10.1016/S0070-2153(05)73007-6
   PubMed Web of Science ®Google Scholar
• Kaushik S, Massey AC, Cuervo AM. Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy. EMBO J 2006; 25:3921-33; PMID:16917501; http://dx.doi.org/10.1038/sj.emboj.7601283
   PubMed Web of Science ®Google Scholar
• Town M, Jean G, Cherqui S, Attard M, Forestier L, Whitmore SA, Callen DF, Gribouval O, Broyer M, Bates GP, et al. A novel gene encoding an integral membrane protein is mutated in nephropathic cystinosis. Nat Genetics 1998; 18:319-24; PMID:9537412; http://dx.doi.org/10.1038/ng0498-319
   PubMed Web of Science ®Google Scholar
• Liu B, Du H, Rutkowski R, Gartner A, Wang X. LAAT-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis. Science 2012; 337:351-4; PMID:22822152; http://dx.doi.org/10.1126/science.1220281
   PubMed Web of Science ®Google Scholar
• Blaby-Haas CE, Merchant SS. Lysosome-related organelles as mediators of metal homeostasis. J Biol Chem 2014; 289:28129-36; PMID:25160625; http://dx.doi.org/10.1074/jbc.R114.592618
   PubMed Web of Science ®Google Scholar
• Roh HC, Collier S, Guthrie J, Robertson JD, Kornfeld K. Lysosome-related organelles in intestinal cells are a zinc storage site in C. elegans. Cell Metab 2012; 15:88-99; PMID:22225878; http://dx.doi.org/10.1016/j.cmet.2011.12.003
   PubMed Web of Science ®Google Scholar
• Beguinot L, Lyall RM, Willingham MC, Pastan I. Down-regulation of the epidermal growth factor receptor in KB cells is due to receptor internalization and subsequent degradation in lysosomes. Proc Natl Acad Sci U S A 1984; 81:2384-8; PMID:6326124; http://dx.doi.org/10.1073/pnas.81.8.2384
   PubMed Web of Science ®Google Scholar
• Aroian RV, Koga M, Mendel JE, Ohshima Y, Sternberg PW. The let-23 gene necessary for Caenorhabditis elegans vulval induction encodes a tyrosine kinase of the EGF receptor subfamily. Nature 1990; 348:693-9; PMID:1979659; http://dx.doi.org/10.1038/348693a0
   PubMed Web of Science ®Google Scholar
• Lloyd TE, Atkinson R, Wu MN, Zhou Y, Pennetta G, Bellen HJ. Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila. Cell 2002; 108:261-9; PMID:11832215; http://dx.doi.org/10.1016/S0092-8674(02)00611-6
   PubMed Web of Science ®Google Scholar
• Huang HS, Nagane M, Klingbeil CK, Lin H, Nishikawa R, Ji XD, Huang CM, Gill GN, Wiley HS, Cavenee WK. The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling. J Biol Chem 1997; 272:2927-35; PMID:9006938; http://dx.doi.org/10.1074/jbc.272.5.2927
   PubMed Web of Science ®Google Scholar
• Hoboth P, Muller A, Ivanova A, Mziaut H, Dehghany J, Sonmez A, Lachnit M, Meyer-Hermann M, Kalaidzidis Y, Solimena M. Aged insulin granules display reduced microtubule-dependent mobility and are disposed within actin-positive multigranular bodies. Proc Natl Acad Sci U S A 2015; 112:E667-76; PMID:25646459; http://dx.doi.org/10.1073/pnas.1409542112
   PubMedGoogle Scholar
• Schuck S, Gallagher CM, Walter P. ER-phagy mediates selective degradation of endoplasmic reticulum independently of the core autophagy machinery. J Cell Sci 2014; 127:4078-88; PMID:25052096; http://dx.doi.org/10.1242/jcs.154716
   PubMed Web of Science ®Google Scholar
• Kim I, Rodriguez-Enriquez S, Lemasters JJ. Selective degradation of mitochondria by mitophagy. Arch Biochem Biophys 2007; 462:245-53; PMID:17475204; http://dx.doi.org/10.1016/j.abb.2007.03.034
   PubMed Web of Science ®Google Scholar
• Kraft C, Deplazes A, Sohrmann M, Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat Cell Biol 2008; 10:602-10; PMID:18391941; http://dx.doi.org/10.1038/ncb1723
   PubMed Web of Science ®Google Scholar
• Tuttle DL, Lewin AS, Dunn WA, Jr. Selective autophagy of peroxisomes in methylotrophic yeasts. Eur J Cell Biol 1993; 60:283-90; PMID:8330626
   PubMed Web of Science ®Google Scholar
• Hung YH, Chen LM, Yang JY, Yang WY. Spatiotemporally controlled induction of autophagy-mediated lysosome turnover. Nat Commun 2013; 4:2111; PMID:23817530; http://dx.doi.org/10.1038/ncomms3111
   PubMed Web of Science ®Google Scholar
• Kim JB, Spiegelman BM. ADD1/SREBP1 promotes adipocyte differentiation and gene expression linked to fatty acid metabolism. Genes Dev 1996; 10:1096-107; PMID:8654925; http://dx.doi.org/10.1101/gad.10.9.1096
   PubMed Web of Science ®Google Scholar
• Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R, Goldstein JL, Brown MS. Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 2002; 110:489-500; PMID:12202038; http://dx.doi.org/10.1016/S0092-8674(02)00872-3
   PubMed Web of Science ®Google Scholar
• Brown MS, Goldstein JL. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 1997; 89:331-40; PMID:9150132; http://dx.doi.org/10.1016/S0092-8674(00)80213-5
   PubMed Web of Science ®Google Scholar
• Brown MS, Goldstein JL. A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood. Proc Natl Acad Sci U S A 1999; 96:11041-8; PMID:10500120; http://dx.doi.org/10.1073/pnas.96.20.11041
   PubMed Web of Science ®Google Scholar
• Venkateswaran A, Laffitte BA, Joseph SB, Mak PA, Wilpitz DC, Edwards PA, Tontonoz P. Control of cellular cholesterol efflux by the nuclear oxysterol receptor LXR α. Proc Natl Acad Sci U S A 2000; 97:12097-102; PMID:11035776; http://dx.doi.org/10.1073/pnas.200367697
   PubMed Web of Science ®Google Scholar
• O'Rourke EJ, Kuballa P, Xavier R, Ruvkun G. omega-6 Polyunsaturated fatty acids extend life span through the activation of autophagy. Genes Dev 2013; 27:429-40; PMID:23392608; http://dx.doi.org/10.1101/gad.205294.112
   PubMed Web of Science ®Google Scholar
• Lapierre LR, Gelino S, Melendez A, Hansen M. Autophagy and lipid metabolism coordinately modulate life span in germline-less C. elegans. Curr Biol 2011; 21:1507-14; PMID:21906946; http://dx.doi.org/10.1016/j.cub.2011.07.042
   PubMed Web of Science ®Google Scholar
• Rovito D, Giordano C, Vizza D, Plastina P, Barone I, Casaburi I, Lanzino M, De Amicis F, Sisci D, Mauro L, et al. Omega-3 PUFA ethanolamides DHEA and EPEA induce autophagy through PPARgamma activation in MCF-7 breast cancer cells. J Cell Physiol 2013; 228:1314-22; PMID:23168911; http://dx.doi.org/10.1002/jcp.24288
   PubMed Web of Science ®Google Scholar
• Rizzuto R, Pozzan T. Microdomains of intracellular Ca2+: molecular determinants and functional consequences. Physiol Rev 2006; 86:369-408; PMID:16371601; http://dx.doi.org/10.1152/physrev.00004.2005
   PubMed Web of Science ®Google Scholar
• Medina DL, Di Paola S, Peluso I, Armani A, De Stefani D, Venditti R, Montefusco S, Scotto-Rosato A, Prezioso C, Forrester A, et al. Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB. Nat Cell Biol 2015; 17:288-99; PMID:25720963; http://dx.doi.org/10.1038/ncb3114
   PubMed Web of Science ®Google Scholar
• Cuervo AM, Wong E. Chaperone-mediated autophagy: roles in disease and aging. Cell Res 2014; 24:92-104; PMID:24281265; http://dx.doi.org/10.1038/cr.2013.153
   PubMed Web of Science ®Google Scholar
• Cuervo AM, Hu W, Lim B, Dice JF. IkappaB is a substrate for a selective pathway of lysosomal proteolysis. Mol Biol Cell 1998; 9:1995-2010; PMID:9693362; http://dx.doi.org/10.1091/mbc.9.8.1995
   PubMed Web of Science ®Google Scholar
• Teste MA, Enjalbert B, Parrou JL, Francois JM. The Saccharomyces cerevisiae YPR184w gene encodes the glycogen debranching enzyme. FEMS Microbiol Lett 2000; 193:105-10; PMID:11094287; http://dx.doi.org/10.1111/j.1574-6968.2000.tb09410.x
   PubMed Web of Science ®Google Scholar
• Sikora J, Urinovska J, Majer F, Poupetova H, Hlavata J, Kostrouchova M, Ledvinova J, Hrebicek M. Bioinformatic and biochemical studies point to AAGR-1 as the ortholog of human acid α-glucosidase in Caenorhabditis elegans. Mol Cell Biochem 2010; 341:51-63; PMID:20349118; http://dx.doi.org/10.1007/s11010-010-0436-3
   PubMed Web of Science ®Google Scholar
• Khanna R, Flanagan JJ, Feng J, Soska R, Frascella M, Pellegrino LJ, Lun Y, Guillen D, Lockhart DJ, Valenzano KJ. The pharmacological chaperone AT2220 increases recombinant human acid α-glucosidase uptake and glycogen reduction in a mouse model of Pompe disease. PloS One 2012; 7:e40776; PMID:22815812; http://dx.doi.org/10.1371/journal.pone.0040776
   PubMed Web of Science ®Google Scholar
• van der Beek NA, van Capelle CI, van der Velden-van Etten KI, Hop WC, van den Berg B, Reuser AJ, van Doorn PA, van der Ploeg AT, Stam H. Rate of progression and predictive factors for pulmonary outcome in children and adults with Pompe disease. Mol Genetics Metab 2011; 104:129-36; http://dx.doi.org/10.1016/j.ymgme.2011.06.012
   PubMed Web of Science ®Google Scholar
• Seifert BL, Snyder MS, Klein AA, O'Loughlin JE, Magid MS, Engle MA. Development of obstruction to ventricular outflow and impairment of inflow in glycogen storage disease of the heart: serial echocardiographic studies from birth to death at 6 months. Am Heart J 1992; 123:239-42; PMID:1729839; http://dx.doi.org/10.1016/0002-8703(92)90779-U
   PubMed Web of Science ®Google Scholar
• Kostera-Pruszczyk A, Opuchlik A, Lugowska A, Nadaj A, Bojakowski J, Tylki-Szymanska A, Kaminska A. Juvenile onset acid maltase deficiency presenting as a rigid spine syndrome. Neuromuscular Disorders 2006; 16:282-5; PMID:16531044; http://dx.doi.org/10.1016/j.nmd.2006.02.001
   PubMed Web of Science ®Google Scholar
• Du H, Heur M, Duanmu M, Grabowski GA, Hui DY, Witte DP, Mishra J. Lysosomal acid lipase-deficient mice: depletion of white and brown fat, severe hepatosplenomegaly, and shortened life span. J Lipid Res 2001; 42:489-500; PMID:11290820
   PubMed Web of Science ®Google Scholar
• Hoffman EP, Barr ML, Giovanni MA, Murray MF. Lysosomal Acid Lipase Deficiency. In: Pagon RA, Adam MP, Ardinger HH, Wallace SE, Amemiya A, Bean LJH, Bird TD, Fong CT, Smith RJH, Stephens K, eds. GeneReviews(R) Seattle (WA), 1993
   Google Scholar