메뉴 건너뛰기




Volumn 112, Issue 11, 2015, Pages E1373-E1381

Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation

Author keywords

Lysosome; mTOR; Starvation; TFEB; TRPML1

Indexed keywords

CALCIUM ION; MAMMALIAN TARGET OF RAPAMYCIN; MUCOLIPIN 1; SODIUM; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR EB; TRANSIENT RECEPTOR POTENTIAL CHANNEL; UNCLASSIFIED DRUG; AMINO ACID; BASIC HELIX LOOP HELIX LEUCINE ZIPPER TRANSCRIPTION FACTOR; CALCIUM; CHOLESTEROL; MCOLN1 PROTEIN, HUMAN; PHOSPHATIDYLINOSITOL 3,5-DIPHOSPHATE; POLYPHOSPHOINOSITIDE; TARGET OF RAPAMYCIN KINASE;

EID: 84925324770     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1419669112     Document Type: Article
Times cited : (190)

References (49)
  • 1
    • 78649704325 scopus 로고    scopus 로고
    • Autophagy and metabolism
    • Rabinowitz JD, White E (2010) Autophagy and metabolism. Science 330(6009):1344-1348.
    • (2010) Science , vol.330 , Issue.6009 , pp. 1344-1348
    • Rabinowitz, J.D.1    White, E.2
  • 2
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • Mizushima N, Komatsu M (2011) Autophagy: Renovation of cells and tissues. Cell 147(4):728-741.
    • (2011) Cell , vol.147 , Issue.4 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 3
    • 84855645313 scopus 로고    scopus 로고
    • Mechanisms of autophagosome biogenesis
    • Rubinsztein DC, Shpilka T, Elazar Z (2012) Mechanisms of autophagosome biogenesis. Curr Biol 22(1):R29-R34.
    • (2012) Curr Biol , vol.22 , Issue.1 , pp. R29-R34
    • Rubinsztein, D.C.1    Shpilka, T.2    Elazar, Z.3
  • 4
    • 67749122634 scopus 로고    scopus 로고
    • A gene network regulating lysosomal biogenesis and function
    • Sardiello M, et al. (2009) A gene network regulating lysosomal biogenesis and function. Science 325(5939):473-477.
    • (2009) Science , vol.325 , Issue.5939 , pp. 473-477
    • Sardiello, M.1
  • 5
    • 80955177196 scopus 로고    scopus 로고
    • TFEB links autophagy to lysosomal biogenesis
    • Settembre C, et al. (2011) TFEB links autophagy to lysosomal biogenesis. Science 332(6036):1429-1433.
    • (2011) Science , vol.332 , Issue.6036 , pp. 1429-1433
    • Settembre, C.1
  • 6
    • 84876408458 scopus 로고    scopus 로고
    • Activation of lysosomal function in the course of autophagy via mTORC1 suppression and autophagosome-lysosome fusion
    • Zhou J, et al. (2013) Activation of lysosomal function in the course of autophagy via mTORC1 suppression and autophagosome-lysosome fusion. Cell Res 23(4):508-523.
    • (2013) Cell Res , vol.23 , Issue.4 , pp. 508-523
    • Zhou, J.1
  • 7
    • 84892875805 scopus 로고    scopus 로고
    • At the end of the autophagic road: An emerging understanding of lysosomal functions in autophagy
    • Shen HM, Mizushima N (2014) At the end of the autophagic road: An emerging understanding of lysosomal functions in autophagy. Trends Biochem Sci 39(2):61-71.
    • (2014) Trends Biochem Sci , vol.39 , Issue.2 , pp. 61-71
    • Shen, H.M.1    Mizushima, N.2
  • 8
    • 77953699711 scopus 로고    scopus 로고
    • Termination of autophagy and reformation of lysosomes regulated by mTOR
    • Yu L, et al. (2010) Termination of autophagy and reformation of lysosomes regulated by mTOR. Nature 465(7300):942-946.
    • (2010) Nature , vol.465 , Issue.7300 , pp. 942-946
    • Yu, L.1
  • 9
    • 78650510609 scopus 로고    scopus 로고
    • mTOR: From growth signal integration to cancer, diabetes and ageing
    • Zoncu R, Efeyan A, Sabatini DM (2011) mTOR: From growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol 12(1):21-35.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.1 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 10
    • 84903158167 scopus 로고    scopus 로고
    • Regulation of mTORC1 by amino acids
    • Bar-Peled L, Sabatini DM (2014) Regulation of mTORC1 by amino acids. Trends Cell Biol 24(7):400-406.
    • (2014) Trends Cell Biol , vol.24 , Issue.7 , pp. 400-406
    • Bar-Peled, L.1    Sabatini, D.M.2
  • 12
    • 84864874958 scopus 로고    scopus 로고
    • MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
    • Martina JA, Chen Y, Gucek M, Puertollano R (2012) MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy 8(6):903-914.
    • (2012) Autophagy , vol.8 , Issue.6 , pp. 903-914
    • Martina, J.A.1    Chen, Y.2    Gucek, M.3    Puertollano, R.4
  • 13
    • 84862539692 scopus 로고    scopus 로고
    • The transcription factor TFEB links mTORC1 signaling to transcriptional control of lysosome homeostasis
    • Roczniak-Ferguson A, et al. (2012) The transcription factor TFEB links mTORC1 signaling to transcriptional control of lysosome homeostasis. Sci Signal 5(228):ra42.
    • (2012) Sci Signal , vol.5 , Issue.228 , pp. ra42
    • Roczniak-Ferguson, A.1
  • 14
    • 84857997408 scopus 로고    scopus 로고
    • A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB
    • Settembre C, et al. (2012) A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB. EMBO J 31(5):1095-1108.
    • (2012) EMBO J , vol.31 , Issue.5 , pp. 1095-1108
    • Settembre, C.1
  • 15
    • 84901670787 scopus 로고    scopus 로고
    • Lysosomal exocytosis and lipid storage disorders
    • Samie MA, Xu H (2014) Lysosomal exocytosis and lipid storage disorders. J Lipid Res 55(6):995-1009.
    • (2014) J Lipid Res , vol.55 , Issue.6 , pp. 995-1009
    • Samie, M.A.1    Xu, H.2
  • 16
    • 84876812269 scopus 로고    scopus 로고
    • Signals from the lysosome: A control centre for cellular clearance and energy metabolism
    • Settembre C, Fraldi A, Medina DL, Ballabio A (2013) Signals from the lysosome: A control centre for cellular clearance and energy metabolism. Nat Rev Mol Cell Biol 14(5):283-296.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.5 , pp. 283-296
    • Settembre, C.1    Fraldi, A.2    Medina, D.L.3    Ballabio, A.4
  • 17
    • 84903729995 scopus 로고    scopus 로고
    • Lysosomal adaptation: How the lysosome responds to external cues
    • Settembre C, Ballabio A (2014) Lysosomal adaptation: How the lysosome responds to external cues. Cold Spring Harb Perspect Biol 6(6):a016907.
    • (2014) Cold Spring Harb Perspect Biol , vol.6 , Issue.6
    • Settembre, C.1    Ballabio, A.2
  • 18
    • 84884290253 scopus 로고    scopus 로고
    • Regulation of membrane trafficking by signalling on endosomal and lysosomal membranes
    • Li X, Garrity AG, Xu H (2013) Regulation of membrane trafficking by signalling on endosomal and lysosomal membranes. J Physiol 591(Pt 18):4389-4401.
    • (2013) J Physiol , vol.591 , pp. 4389-4401
    • Li, X.1    Garrity, A.G.2    Xu, H.3
  • 19
    • 84859175854 scopus 로고    scopus 로고
    • Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release
    • Shen D, et al. (2012) Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release. Nat Commun 3:731.
    • (2012) Nat Commun , vol.3 , pp. 731
    • Shen, D.1
  • 20
    • 77949696020 scopus 로고    scopus 로고
    • Mucolipins: Intracellular TRPML1-3 channels
    • Cheng X, Shen D, Samie M, Xu H (2010) Mucolipins: Intracellular TRPML1-3 channels. FEBS Lett 584(10):2013-2021.
    • (2010) FEBS Lett , vol.584 , Issue.10 , pp. 2013-2021
    • Cheng, X.1    Shen, D.2    Samie, M.3    Xu, H.4
  • 21
    • 18744363612 scopus 로고    scopus 로고
    • Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway
    • LaPlante JM, et al. (2002) Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway. FEBS Lett 532(1-2):183-187.
    • (2002) FEBS Lett , vol.532 , Issue.1-2 , pp. 183-187
    • LaPlante, J.M.1
  • 22
    • 80052729465 scopus 로고    scopus 로고
    • Transcriptional activation of lysosomal exocytosis promotes cellular clearance
    • Medina DL, et al. (2011) Transcriptional activation of lysosomal exocytosis promotes cellular clearance. Dev Cell 21(3):421-430.
    • (2011) Dev Cell , vol.21 , Issue.3 , pp. 421-430
    • Medina, D.L.1
  • 23
    • 84884154195 scopus 로고    scopus 로고
    • A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis
    • Samie M, et al. (2013) A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis. Dev Cell 26(5):511-524.
    • (2013) Dev Cell , vol.26 , Issue.5 , pp. 511-524
    • Samie, M.1
  • 24
    • 84867908738 scopus 로고    scopus 로고
    • In vivo, Pikfyve generates PI(3,5)P2, which serves as both a signaling lipid and the major precursor for PI5P
    • Zolov SN, et al. (2012) In vivo, Pikfyve generates PI(3,5)P2, which serves as both a signaling lipid and the major precursor for PI5P. Proc Natl Acad Sci USA 109(43):17472-17477.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.43 , pp. 17472-17477
    • Zolov, S.N.1
  • 25
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • Dong XP, et al. (2008) The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 455(7215):992-996.
    • (2008) Nature , vol.455 , Issue.7215 , pp. 992-996
    • Dong, X.P.1
  • 26
    • 80051473235 scopus 로고    scopus 로고
    • PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca(2+) release channels in the endolysosome
    • Dong XP, et al. (2010) PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca(2+) release channels in the endolysosome. Nat Commun 1:38.
    • (2010) Nat Commun , vol.1 , pp. 38
    • Dong, X.P.1
  • 27
    • 84867565289 scopus 로고    scopus 로고
    • TPC proteins are phosphoinositide- activated sodium-selective ion channels in endosomes and lysosomes
    • Wang X, et al. (2012) TPC proteins are phosphoinositide- activated sodium-selective ion channels in endosomes and lysosomes. Cell 151(2):372-383.
    • (2012) Cell , vol.151 , Issue.2 , pp. 372-383
    • Wang, X.1
  • 28
    • 67650228579 scopus 로고    scopus 로고
    • Rapamycin inhibits mTORC1, but not completely
    • Thoreen CC, Sabatini DM (2009) Rapamycin inhibits mTORC1, but not completely. Autophagy 5(5):725-726.
    • (2009) Autophagy , vol.5 , Issue.5 , pp. 725-726
    • Thoreen, C.C.1    Sabatini, D.M.2
  • 29
    • 65549145048 scopus 로고    scopus 로고
    • An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1
    • Thoreen CC, et al. (2009) An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1. J Biol Chem 284(12):8023-8032.
    • (2009) J Biol Chem , vol.284 , Issue.12 , pp. 8023-8032
    • Thoreen, C.C.1
  • 30
    • 79960348203 scopus 로고    scopus 로고
    • Relieving autophagy and 4EBP1 from rapamycin resistance
    • Nyfeler B, et al. (2011) Relieving autophagy and 4EBP1 from rapamycin resistance. Mol Cell Biol 31(14):2867-2876.
    • (2011) Mol Cell Biol , vol.31 , Issue.14 , pp. 2867-2876
    • Nyfeler, B.1
  • 31
    • 17444408542 scopus 로고    scopus 로고
    • Microelectrode array recordings of cultured hippocampal networks reveal a simple model for transcription and protein synthesis-dependent plasticity
    • Arnold FJ, et al. (2005) Microelectrode array recordings of cultured hippocampal networks reveal a simple model for transcription and protein synthesis-dependent plasticity. J Physiol 564(Pt 1):3-19.
    • (2005) J Physiol , vol.564 , pp. 3-19
    • Arnold, F.J.1
  • 32
    • 43949112650 scopus 로고    scopus 로고
    • DNA-dependent protein kinase catalytic subunit modulates the stability of c-Myc oncoprotein
    • An J, et al. (2008) DNA-dependent protein kinase catalytic subunit modulates the stability of c-Myc oncoprotein. Mol Cancer 7:32.
    • (2008) Mol Cancer , vol.7 , pp. 32
    • An, J.1
  • 33
    • 0016762233 scopus 로고
    • Turnover studies on proteins of rat liver lysosomes
    • Wang C-C, Touster O (1975) Turnover studies on proteins of rat liver lysosomes. J Biol Chem 250(13):4896-4902.
    • (1975) J Biol Chem , vol.250 , Issue.13 , pp. 4896-4902
    • Wang, C.-C.1    Touster, O.2
  • 34
    • 84874105202 scopus 로고    scopus 로고
    • mTOR regulates lysosomal ATP-sensitive two-pore Na(+) channels to adapt to metabolic state
    • Cang C, et al. (2013) mTOR regulates lysosomal ATP-sensitive two-pore Na(+) channels to adapt to metabolic state. Cell 152(4):778-790.
    • (2013) Cell , vol.152 , Issue.4 , pp. 778-790
    • Cang, C.1
  • 35
    • 84874352229 scopus 로고    scopus 로고
    • Rag GTPases mediate amino acid-dependent recruitment of TFEB and MITF to lysosomes
    • Martina JA, Puertollano R (2013) Rag GTPases mediate amino acid-dependent recruitment of TFEB and MITF to lysosomes. J Cell Biol 200(4):475-491.
    • (2013) J Cell Biol , vol.200 , Issue.4 , pp. 475-491
    • Martina, J.A.1    Puertollano, R.2
  • 36
    • 84891368628 scopus 로고    scopus 로고
    • Genetically encoded fluorescent probe to visualize intracellular phosphatidylinositol 3,5-bisphosphate localization and dynamics
    • Li X, et al. (2013) Genetically encoded fluorescent probe to visualize intracellular phosphatidylinositol 3,5-bisphosphate localization and dynamics. Proc Natl Acad Sci USA 110(52):21165-21170.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.52 , pp. 21165-21170
    • Li, X.1
  • 37
    • 84864751451 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate plays a role in the activation and subcellular localization of mechanistic target of rapamycin 1
    • Bridges D, et al. (2012) Phosphatidylinositol 3,5-bisphosphate plays a role in the activation and subcellular localization of mechanistic target of rapamycin 1. Mol Biol Cell 23(15):2955-2962.
    • (2012) Mol Biol Cell , vol.23 , Issue.15 , pp. 2955-2962
    • Bridges, D.1
  • 38
    • 38949207192 scopus 로고    scopus 로고
    • A selective PIKfyve inhibitor blocks PtdIns(3,5)P(2) production and disrupts endomembrane transport and retroviral budding
    • Jefferies HB, et al. (2008) A selective PIKfyve inhibitor blocks PtdIns(3,5)P(2) production and disrupts endomembrane transport and retroviral budding. EMBO Rep 9(2):164-170.
    • (2008) EMBO Rep , vol.9 , Issue.2 , pp. 164-170
    • Jefferies, H.B.1
  • 39
    • 84880888092 scopus 로고    scopus 로고
    • PIKfyve, a class III PI kinase, is the target of the small molecular IL-12/IL-23 inhibitor apilimod and a player in Toll-like receptor signaling
    • Cai X, et al. (2013) PIKfyve, a class III PI kinase, is the target of the small molecular IL-12/IL-23 inhibitor apilimod and a player in Toll-like receptor signaling. Chem Biol 20(7):912-921.
    • (2013) Chem Biol , vol.20 , Issue.7 , pp. 912-921
    • Cai, X.1
  • 40
    • 84890405966 scopus 로고    scopus 로고
    • Suppression of lysosome function induces autophagy via a feedback down-regulation of MTOR complex 1 (MTORC1) activity
    • Li M, et al. (2013) Suppression of lysosome function induces autophagy via a feedback down-regulation of MTOR complex 1 (MTORC1) activity. J Biol Chem 288(50):35769-35780.
    • (2013) J Biol Chem , vol.288 , Issue.50 , pp. 35769-35780
    • Li, M.1
  • 41
    • 84877332222 scopus 로고    scopus 로고
    • Inhibition of the autophagic flux by salinomycin in breast cancer stem-like/progenitor cells interferes with their maintenance
    • Yue W, et al. (2013) Inhibition of the autophagic flux by salinomycin in breast cancer stem-like/progenitor cells interferes with their maintenance. Autophagy 9(5):714-729.
    • (2013) Autophagy , vol.9 , Issue.5 , pp. 714-729
    • Yue, W.1
  • 42
    • 59249088570 scopus 로고    scopus 로고
    • Assays to assess autophagy induction and fusion of autophagic vacuoles with a degradative compartment, using monodansylcadaverine (MDC) and DQ-BSA
    • Vázquez CL, Colombo MI (2009) Assays to assess autophagy induction and fusion of autophagic vacuoles with a degradative compartment, using monodansylcadaverine (MDC) and DQ-BSA. Methods Enzymol 452:85-95.
    • (2009) Methods Enzymol , vol.452 , pp. 85-95
    • Vázquez, C.L.1    Colombo, M.I.2
  • 43
    • 84866163103 scopus 로고    scopus 로고
    • Drosophila TRPML is required for TORC1 activation
    • Wong CO, Li R, Montell C, Venkatachalam K (2012) Drosophila TRPML is required for TORC1 activation. Curr Biol 22(17):1616-1621.
    • (2012) Curr Biol , vol.22 , Issue.17 , pp. 1616-1621
    • Wong, C.O.1    Li, R.2    Montell, C.3    Venkatachalam, K.4
  • 45
    • 33748572921 scopus 로고    scopus 로고
    • Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic
    • Pryor PR, Reimann F, Gribble FM, Luzio JP (2006) Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic. Traffic 7(10):1388-1398.
    • (2006) Traffic , vol.7 , Issue.10 , pp. 1388-1398
    • Pryor, P.R.1    Reimann, F.2    Gribble, F.M.3    Luzio, J.P.4
  • 46
    • 1842428593 scopus 로고    scopus 로고
    • Caenorhabditis elegans functional orthologue of human protein h-mucolipin-1 is required for lysosome biogenesis
    • Treusch S, et al. (2004) Caenorhabditis elegans functional orthologue of human protein h-mucolipin-1 is required for lysosome biogenesis. Proc Natl Acad Sci USA 101(13):4483-4488.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.13 , pp. 4483-4488
    • Treusch, S.1
  • 47
    • 80051473235 scopus 로고    scopus 로고
    • PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca(2+) release channels in the endolysosome
    • Dong XP, et al. (2010) PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca(2+) release channels in the endolysosome. Nat Commun 1(4):38.
    • (2010) Nat Commun , vol.1 , Issue.4 , pp. 38
    • Dong, X.P.1
  • 48
    • 84890152601 scopus 로고    scopus 로고
    • Selective targeting of human colon cancer stem-like cells by the mTOR inhibitor Torin-1
    • Francipane MG, Lagasse E (2013) Selective targeting of human colon cancer stem-like cells by the mTOR inhibitor Torin-1. Oncotarget 4(11):1948-1962.
    • (2013) Oncotarget , vol.4 , Issue.11 , pp. 1948-1962
    • Francipane, M.G.1    Lagasse, E.2
  • 49
    • 0025173761 scopus 로고
    • Isolation and characterization of Chinese hamster ovary cell mutants defective in intracellular low density lipoprotein-cholesterol trafficking
    • Cadigan KM, Spillane DM, Chang TY (1990) Isolation and characterization of Chinese hamster ovary cell mutants defective in intracellular low density lipoprotein-cholesterol trafficking. J Cell Biol 110(2):295-308.
    • (1990) J Cell Biol , vol.110 , Issue.2 , pp. 295-308
    • Cadigan, K.M.1    Spillane, D.M.2    Chang, T.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.