메뉴 건너뛰기




Volumn 18, Issue 4, 2016, Pages 404-417

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

Author keywords

[No Author keywords available]

Indexed keywords

ALG 2 PROTEIN; CALCIUM CHANNEL; CALCIUM ION; CHOLESTEROL; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; PHOSPHATIDYLINOSITIDE; RAB7 PROTEIN; RILP PROTEIN; TRPML1 PROTEIN; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN; CALCIUM; CALCIUM BINDING PROTEIN; MCOLN1 PROTEIN, MOUSE; PDCD6 PROTEIN, MOUSE; PHOSPHATIDYLINOSITOL 3,5-DIPHOSPHATE; PHOTOPROTEIN; POLYPHOSPHOINOSITIDE; RAB PROTEIN; RILP PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL;

EID: 84960158035     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb3324     Document Type: Article
Times cited : (291)

References (70)
  • 2
    • 84901670787 scopus 로고    scopus 로고
    • Lysosomal exocytosis and lipid storage disorders
    • Samie, M. A., & Xu, H. Lysosomal exocytosis and lipid storage disorders. J. Lipid Res. 55, 995-1009 (2014
    • (2014) J. Lipid Res , vol.55 , pp. 995-1009
    • Samie, M.A.1    Xu, H.2
  • 3
    • 84884154195 scopus 로고    scopus 로고
    • A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis
    • Samie, M., et al. A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis. Dev. Cell 26, 511-524 (2013
    • (2013) Dev. Cell , vol.26 , pp. 511-524
    • Samie, M.1
  • 4
    • 77953699711 scopus 로고    scopus 로고
    • Termination of autophagy and reformation of lysosomes regulated by mTOR
    • Yu, L., et al. Termination of autophagy and reformation of lysosomes regulated by mTOR. Nature 465, 942-946 (2010
    • (2010) Nature , vol.465 , pp. 942-946
    • Yu, L.1
  • 5
    • 77955057326 scopus 로고    scopus 로고
    • 3rd Linking molecular motors to membrane cargo
    • Akhmanova, A., & Hammer, J. A. 3rd Linking molecular motors to membrane cargo. Curr. Opin. Cell Biol. 22, 479-487 (2010
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 479-487
    • Akhmanova, A.1    Hammer, J.A.2
  • 6
    • 79953316595 scopus 로고    scopus 로고
    • Lysosomal positioning coordinates cellular nutrient responses
    • Korolchuk, V. I., et al. Lysosomal positioning coordinates cellular nutrient responses. Nat. Cell Biol. 13, 453-460 (2011
    • (2011) Nat. Cell Biol , vol.13 , pp. 453-460
    • Korolchuk, V.I.1
  • 7
    • 0032559260 scopus 로고    scopus 로고
    • And dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa, N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526 (1998
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1    Kinesin2
  • 8
    • 0034677929 scopus 로고    scopus 로고
    • The dynein microtubule motor
    • King, S. M. The dynein microtubule motor. Biochim. Biophys. Acta 1496, 60-75 (2000
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 60-75
    • King, S.M.1
  • 10
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • Dong, X. P., et al. The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 455, 992-996 (2008
    • (2008) Nature , vol.455 , pp. 992-996
    • Dong, X.P.1
  • 11
    • 77949696020 scopus 로고    scopus 로고
    • Mucolipins: Intracellular TRPML1-3 channels
    • Cheng, X., Shen, D., Samie, M., & Xu, H. Mucolipins: intracellular TRPML1-3 channels. FEBS Lett. 584, 2013-2021 (2010
    • (2010) FEBS Lett , vol.584 , pp. 2013-2021
    • Cheng, X.1    Shen, D.2    Samie, M.3    Xu, H.4
  • 12
    • 0033760264 scopus 로고    scopus 로고
    • Cloning of the gene encoding a novel integral membrane protein, mucolipidin-and identification of the two major founder mutations causing mucolipidosis type IV
    • Bassi, M. T., et al. Cloning of the gene encoding a novel integral membrane protein, mucolipidin-and identification of the two major founder mutations causing mucolipidosis type IV. Am. J. Human Genet. 67, 1110-1120 (2000
    • (2000) Am. J. Human Genet , vol.67 , pp. 1110-1120
    • Bassi, M.T.1
  • 13
    • 0032568565 scopus 로고    scopus 로고
    • Abnormal transport along the lysosomal pathway in mucolipidosis, type IV disease
    • Chen, C. S., Bach, G., & Pagano, R. E. Abnormal transport along the lysosomal pathway in mucolipidosis, type IV disease. Proc. Natl Acad. Sci. USA 95, 6373-6378 (1998
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6373-6378
    • Chen, C.S.1    Bach, G.2    Pagano, R.E.3
  • 14
    • 35348829780 scopus 로고    scopus 로고
    • Neurologic, gastric, and opthalmologic pathologies in a murine model of mucolipidosis type IV
    • Venugopal, B., et al. Neurologic, gastric, and opthalmologic pathologies in a murine model of mucolipidosis type IV. Am. J. Human Genet. 81, 1070-1083 (2007
    • (2007) Am. J. Human Genet , vol.81 , pp. 1070-1083
    • Venugopal, B.1
  • 15
    • 84939778375 scopus 로고    scopus 로고
    • The phosphoinositide-gated lysosomal Ca(2+) channel, TRPML1, is required for phagosome maturation
    • Dayam, R. M., Saric, A., Shilliday, R. E., & Botelho, R. J. The phosphoinositide-gated lysosomal Ca(2+) channel, TRPML1, is required for phagosome maturation. Traffic 16, 1010-1026 (2015)
    • (2015) Traffic , vol.16 , pp. 1010-1026
    • Dayam, R.M.1    Saric, A.2    Shilliday, R.E.3    Botelho, R.J.4
  • 16
    • 84922794140 scopus 로고    scopus 로고
    • Lysosomal physiology
    • Xu, H., & Ren, D. Lysosomal physiology. Annu. Rev. Physiol. 77, 57-80 (2015
    • (2015) Annu. Rev. Physiol. , vol.77 , pp. 57-80
    • Xu, H.1    Ren, D.2
  • 17
    • 84885821254 scopus 로고    scopus 로고
    • Regulation of autophagic flux by dynein-mediated autophagosomes trafficking in mouse coronary arterial myocytes
    • Xu, M., et al. Regulation of autophagic flux by dynein-mediated autophagosomes trafficking in mouse coronary arterial myocytes. Biochim. Biophys. Acta 1833, 3228-3236 (2013
    • (2013) Biochim. Biophys. Acta 1833 , pp. 3228-3236
    • Xu, M.1
  • 18
    • 47149089713 scopus 로고    scopus 로고
    • Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes
    • Kimura, S., Noda, T., & Yoshimori, T. Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes. Cell Struct. Funct. 33, 109-122 (2008
    • (2008) Cell Struct. Funct , vol.33 , pp. 109-122
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 19
    • 65549145048 scopus 로고    scopus 로고
    • An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1
    • Thoreen, C. C., et al. An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1. J. Biol. Chem. 284, 8023-8032 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 8023-8032
    • Thoreen, C.C.1
  • 20
    • 79955075253 scopus 로고    scopus 로고
    • Macroautophagy is defective in mucolipin-1-deficient mouse neurons
    • Curcio-Morelli, C., et al. Macroautophagy is defective in mucolipin-1-deficient mouse neurons. Neurobiol. Dis. 40, 370-377 (2010
    • (2010) Neurobiol. Dis , vol.40 , pp. 370-377
    • Curcio-Morelli, C.1
  • 22
    • 84921960605 scopus 로고    scopus 로고
    • The intracellular Ca channel MCOLN1 is required for sarcolemma repair to prevent muscular dystrophy
    • Cheng, X., et al. The intracellular Ca channel MCOLN1 is required for sarcolemma repair to prevent muscular dystrophy. Nat. Med. 20, 1187-1192 (2014
    • (2014) Nat. Med , vol.20 , pp. 1187-1192
    • Cheng, X.1
  • 23
    • 84925324770 scopus 로고    scopus 로고
    • Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation
    • Wang, W., et al. Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation. Proc. Natl Acad. Sci. USA 112, E1373-E1381 (2015
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E1373-E1381
    • Wang, W.1
  • 24
    • 84859175854 scopus 로고    scopus 로고
    • Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release
    • Shen, D., et al. Lipid storage disorders block lysosomal trafficking by inhibiting a TRP channel and lysosomal calcium release. Nat. Commun. 3, 731 (2012
    • (2012) Nat. Commun , vol.3 , pp. 731
    • Shen, D.1
  • 25
    • 38949156866 scopus 로고    scopus 로고
    • Cholesterol level regulates endosome motility via Rab proteins
    • Chen, H., Yang, J., Low, P. S., & Cheng, J. X. Cholesterol level regulates endosome motility via Rab proteins. Biophys. J. 94, 1508-1520 (2008
    • (2008) Biophys. J. , vol.94 , pp. 1508-1520
    • Chen, H.1    Yang, J.2    Low, P.S.3    Cheng, J.X.4
  • 26
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning
    • Rocha, N., et al. Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning. J. Cell Biol. 185, 1209-1225 (2009
    • (2009) J. Cell Biol , vol.185 , pp. 1209-1225
    • Rocha, N.1
  • 27
    • 84899976153 scopus 로고    scopus 로고
    • Visualization of cholesterol deposits in lysosomes of Niemann- Pick type C fibroblasts using recombinant perfringolysin O
    • Kwiatkowska, K., et al. Visualization of cholesterol deposits in lysosomes of Niemann- Pick type C fibroblasts using recombinant perfringolysin O. Orphanet J. Rare Dis. 9, 64 (2014
    • (2014) Orphanet J. Rare Dis , vol.9 , pp. 64
    • Kwiatkowska, K.1
  • 28
    • 0042163785 scopus 로고    scopus 로고
    • Trafficking defects in endogenously synthesized cholesterol in fibroblasts, macrophages, hepatocytes, and glial cells from Niemann- Pick type C1 mice
    • Reid, P. C., Sugii, S., & Chang, T. Y. Trafficking defects in endogenously synthesized cholesterol in fibroblasts, macrophages, hepatocytes, and glial cells from Niemann- Pick type C1 mice. J. Lipid Res. 44, 1010-1019 (2003
    • (2003) J. Lipid Res , vol.44 , pp. 1010-1019
    • Reid, P.C.1    Sugii, S.2    Chang, T.Y.3
  • 30
    • 39549098329 scopus 로고    scopus 로고
    • Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease
    • Spinosa, M. R., et al. Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J. Neurosci. 28, 1640-1648 (2008
    • (2008) J. Neurosci , vol.28 , pp. 1640-1648
    • Spinosa, M.R.1
  • 31
    • 0035865135 scopus 로고    scopus 로고
    • Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • Cantalupo, G., Alifano, P., Roberti, V., Bruni, C. B., & Bucci, C. Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. EMBO J. 20, 683-693 (2001
    • (2001) EMBO J. , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 33
    • 84891368628 scopus 로고    scopus 로고
    • Genetically encoded fluorescent probe to visualize intracellular phosphatidylinositol 3,5-bisphosphate localization and dynamics
    • Li, X., et al. Genetically encoded fluorescent probe to visualize intracellular phosphatidylinositol 3,5-bisphosphate localization and dynamics. Proc. Natl Acad. Sci. USA 110, 21165-21170 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 21165-21170
    • Li, X.1
  • 34
    • 84921615639 scopus 로고    scopus 로고
    • PI(5)P regulates autophagosome biogenesis
    • Vicinanza, M., et al. PI(5)P regulates autophagosome biogenesis. Mol. Cell 57, 219-234 (2015
    • (2015) Mol. Cell , vol.57 , pp. 219-234
    • Vicinanza, M.1
  • 35
    • 80051473235 scopus 로고    scopus 로고
    • PI(35)P(2) controls membrane trafficking by direct activation of mucolipin Ca2C release channels in the endolysosome
    • Dong, X. P., et al. PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca2C release channels in the endolysosome. Nat. Commun. 1, 38 (2010
    • (2010) Nat. Commun. , vol.1 , pp. 38
    • Dong, X.P.1
  • 36
    • 84863922724 scopus 로고    scopus 로고
    • Phosphoinositide isoforms determine compartment-specific ion channel activity
    • Zhang, X., Li, X., & Xu, H. Phosphoinositide isoforms determine compartment-specific ion channel activity. Proc. Natl Acad. Sci. USA 109, 11384-11389 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 11384-11389
    • Zhang, X.1    Li, X.2    Xu, H.3
  • 37
    • 38949207192 scopus 로고    scopus 로고
    • A selective PIKfyve inhibitor blocks PtdIns(35)P2 production and disrupts endomembrane transport and retroviral budding
    • Jefferies, H. B., et al. A selective PIKfyve inhibitor blocks PtdIns(3,5)P2 production and disrupts endomembrane transport and retroviral budding. EMBO Rep. 9, 164-170 (2008
    • (2008) EMBO Rep. , vol.9 , pp. 164-170
    • Jefferies, H.B.1
  • 38
    • 84875435923 scopus 로고    scopus 로고
    • Inhibition of PIKfyve by YM-201636 dysregulates autophagy and leads to apoptosis-independent neuronal cell death
    • Martin, S., et al. Inhibition of PIKfyve by YM-201636 dysregulates autophagy and leads to apoptosis-independent neuronal cell death. PLoS ONE 8, e60152 (2013
    • (2013) PLoS ONE , vol.8 , pp. e60152
    • Martin, S.1
  • 39
    • 84926644537 scopus 로고    scopus 로고
    • The Fab1/PIKfyve phosphoinositide phosphate kinase is not necessary to maintain the pH of lysosomes and of the yeast vacuole
    • Ho, C. Y., Choy, C. H., Wattson, C. A., Johnson, D. E., & Botelho, R. J. The Fab1/PIKfyve phosphoinositide phosphate kinase is not necessary to maintain the pH of lysosomes and of the yeast vacuole. J. Biol. Chem. 290, 9919-9928 (2015
    • (2015) J. Biol. Chem , vol.290 , pp. 9919-9928
    • Ho, C.Y.1    Choy, C.H.2    Wattson, C.A.3    Johnson, D.E.4    Botelho, R.J.5
  • 40
    • 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. 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, 912-921 (2013
    • (2013) Chem. Biol , vol.20 , pp. 912-921
    • Cai, X.1
  • 41
    • 70350446761 scopus 로고    scopus 로고
    • Traffic control: Regulation of kinesin motors
    • Verhey, K. J., & Hammond, J. W. Traffic control: regulation of kinesin motors. Nat. Rev. Mol. Cell Biol. 10, 765-777 (2009
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 765-777
    • Verhey, K.J.1    Hammond, J.W.2
  • 42
    • 83455229793 scopus 로고    scopus 로고
    • Arl8 and SKIP act together to link lysosomes to kinesin-1
    • Rosa-Ferreira, C., & Munro, S. Arl8 and SKIP act together to link lysosomes to kinesin-1. Dev. Cell 21, 1171-1178 (2011
    • (2011) Dev. Cell , vol.21 , pp. 1171-1178
    • Rosa-Ferreira, C.1    Munro, S.2
  • 43
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria
    • Tanaka, Y., et al. Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 93, 1147-1158 (1998
    • (1998) Cell , vol.93 , pp. 1147-1158
    • Tanaka, Y.1
  • 44
    • 0035975946 scopus 로고    scopus 로고
    • The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors
    • Jordens, I., et al. The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors. Curr. Biol. 11, 1680-1685 (2001
    • (2001) Curr. Biol , vol.11 , pp. 1680-1685
    • Jordens, I.1
  • 45
    • 33847003020 scopus 로고    scopus 로고
    • Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued ORP1L and the receptor betalll spectrin
    • Johansson, M., et al. Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin. J. Cell Biol. 176, 459-471 (2007
    • (2007) J. Cell Biol , vol.176 , pp. 459-471
    • Johansson, M.1
  • 46
    • 79251563457 scopus 로고    scopus 로고
    • Kinesin 5B is necessary for delivery of membrane and receptors during FcgammaR-mediated phagocytosis
    • Silver, K. E., & Harrison, R. E. Kinesin 5B is necessary for delivery of membrane and receptors during FcgammaR-mediated phagocytosis. J. Immunol. 186, 816-825 (2011
    • (2011) J. Immunol , vol.186 , pp. 816-825
    • Silver, K.E.1    Harrison, R.E.2
  • 48
    • 84931022346 scopus 로고    scopus 로고
    • The dynein inhibitor Ciliobrevin D inhibits the bidirectional transport of organelles along sensory axons and impairs NGF-mediated regulation of growth cones and axon branches
    • Sainath, R., & Gallo, G. The dynein inhibitor Ciliobrevin D inhibits the bidirectional transport of organelles along sensory axons and impairs NGF-mediated regulation of growth cones and axon branches. Dev. Neurobiol. 75, 757-777 (2014
    • (2014) Dev. Neurobiol , vol.75 , pp. 757-777
    • Sainath, R.1    Gallo, G.2
  • 49
    • 84862814996 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the AAAC ATPase motor cytoplasmic dynein
    • Firestone, A. J., et al. Small-molecule inhibitors of the AAAC ATPase motor cytoplasmic dynein. Nature 484, 125-129 (2012
    • (2012) Nature , vol.484 , pp. 125-129
    • Firestone, A.J.1
  • 50
    • 79960623087 scopus 로고    scopus 로고
    • Structure and function of ALG-2, a penta-EFhand calcium-dependent adaptor protein
    • Maki, M., Suzuki, H., & Shibata, H. Structure and function of ALG-2, a penta-EFhand calcium-dependent adaptor protein. Sci. China Life Sci. 54, 770-779 (2011
    • (2011) Sci. China Life Sci , vol.54 , pp. 770-779
    • Maki, M.1    Suzuki, H.2    Shibata, H.3
  • 51
    • 73649127260 scopus 로고    scopus 로고
    • Identification of the penta-EFhand protein ALG-2 as a Ca2C-dependent interactor of mucolipin-1
    • Vergarajauregui, S., Martina, J. A., & Puertollano, R. Identification of the penta-EFhand protein ALG-2 as a Ca2C-dependent interactor of mucolipin-1. J. Biol. Chem. 284, 36357-36366 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 36357-36366
    • Vergarajauregui, S.1    Martina, J.A.2    Puertollano, R.3
  • 52
    • 84950126700 scopus 로고    scopus 로고
    • Genome engineering using CRISPR-Cas9 system
    • Cong, L., & Zhang, F. Genome engineering using CRISPR-Cas9 system. Methods Mol. Biol. 1239, 197-217 (2015
    • (2015) Methods Mol. Biol , vol.1239 , pp. 197-217
    • Cong, L.1    Zhang, F.2
  • 53
    • 84955200036 scopus 로고    scopus 로고
    • Rab7 and Arl8 GTPases are necessary for lysosome tubulation in macrophages
    • Mrakovic, A., Kay, J. G., Furuya, W., Brumell, J. H., & Botelho, R. J. Rab7 and Arl8 GTPases are necessary for lysosome tubulation in macrophages. Traffic 13, 1667-1679 (2012
    • (2012) Traffic , vol.13 , pp. 1667-1679
    • Mrakovic, A.1    Kay, J.G.2    Furuya, W.3    Brumell, J.H.4    Botelho, R.J.5
  • 54
    • 0019333905 scopus 로고
    • New calcium indicators and buffers with high selectivity against magnesium and protons: Design synthesis and properties of prototype structures
    • Tsien, R. Y. New calcium indicators and buffers with high selectivity against magnesium and protons: design, synthesis, and properties of prototype structures. Biochemistry 19, 2396-2404 (1980
    • (1980) Biochemistry , vol.19 , pp. 2396-2404
    • Tsien, R.Y.1
  • 55
    • 58049198294 scopus 로고    scopus 로고
    • VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(35)P(2) in yeast and mouse
    • Jin, N., et al. VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse. EMBO J. 27, 3221-3234 (2008
    • (2008) EMBO J. , vol.27 , pp. 3221-3234
    • Jin, N.1
  • 56
    • 84867908738 scopus 로고    scopus 로고
    • In vivo Pikfyve generates PI(35)P2, which serves as both a signaling lipid and the major precursor for PI5P
    • Zolov, S. N., et al. 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, 17472-17477 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 17472-17477
    • Zolov, S.N.1
  • 57
    • 84941354274 scopus 로고    scopus 로고
    • The mucolipidosis IV Ca2C channel TRPML1 (MCOLN1) is regulated by the TOR kinase
    • Onyenwoke, R. U., et al. The mucolipidosis IV Ca2C channel TRPML1 (MCOLN1) is regulated by the TOR kinase. Biochem. J. 470, 331-342 (2015
    • (2015) Biochem. J. , vol.470 , pp. 331-342
    • Onyenwoke, R.U.1
  • 58
    • 84866163103 scopus 로고    scopus 로고
    • Drosophila TRPML is required for TORC1 activation
    • Wong, C. O., Li, R., Montell, C., & Venkatachalam, K. Drosophila TRPML is required for TORC1 activation. Curr. Biol. 22, 1616-1621 (2012
    • (2012) Curr. Biol , vol.22 , pp. 1616-1621
    • Wong, C.O.1    Li, R.2    Montell, C.3    Venkatachalam, K.4
  • 59
    • 84923228346 scopus 로고    scopus 로고
    • Mucolipidosis type IV protein TRPML1-dependent lysosome formation
    • Miller, A., et al. Mucolipidosis type IV protein TRPML1-dependent lysosome formation. Traffic 16, 284-297 (2014
    • (2014) Traffic , vol.16 , pp. 284-297
    • Miller, A.1
  • 60
    • 84923820926 scopus 로고    scopus 로고
    • Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB
    • Medina, D. L., et al. Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB. Nat. Cell Biol. 17, 288-299 (2015
    • (2015) Nat. Cell Biol , vol.17 , pp. 288-299
    • Medina, D.L.1
  • 61
    • 84906544287 scopus 로고    scopus 로고
    • Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: A potential effector pathway for luminal calcium
    • Helm, J. R., et al. Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: a potential effector pathway for luminal calcium. J. Biol. Chem. 289, 23609-23628 (2014
    • (2014) J. Biol. Chem , vol.289 , pp. 23609-23628
    • Helm, J.R.1
  • 62
    • 0346018912 scopus 로고
    • Tubular lysosome morphology and distribution within macrophages depend on the integrity of cytoplasmic microtubules
    • Swanson, J., Bushnell, A., & Silverstein, S. C. Tubular lysosome morphology and distribution within macrophages depend on the integrity of cytoplasmic microtubules. Proc. Natl Acad. Sci. USA 84, 1921-1925 (1987
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1921-1925
    • Swanson, J.1    Bushnell, A.2    Silverstein, S.C.3
  • 63
    • 84870730914 scopus 로고    scopus 로고
    • Autophagic lysosome reformation
    • Chen, Y., & Yu, L. Autophagic lysosome reformation. Exp. Cell Res. 319, 142-146 (2013
    • (2013) Exp. Cell Res , vol.319 , pp. 142-146
    • Chen, Y.1    Yu, L.2
  • 64
    • 84865776097 scopus 로고    scopus 로고
    • Clathrin and phosphatidylinositol-4,5-bisphosphate regulate autophagic lysosome reformation
    • Rong, Y., et al. Clathrin and phosphatidylinositol-4,5-bisphosphate regulate autophagic lysosome reformation. Nat. Cell Biol. 14, 924-934 (2012
    • (2012) Nat. Cell Biol , vol.14 , pp. 924-934
    • Rong, Y.1
  • 65
    • 79956346329 scopus 로고    scopus 로고
    • Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation
    • Rong, Y., et al. Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation. Proc. Natl Acad. Sci. USA 108, 7826-7831 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 7826-7831
    • Rong, Y.1
  • 66
    • 84915793059 scopus 로고    scopus 로고
    • Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation
    • Chang, J., Lee, S., & Blackstone, C. Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation. J. Clin. Invest. 124, 5249-5262 (2014
    • (2014) J. Clin. Invest , vol.124 , pp. 5249-5262
    • Chang, J.1    Lee, S.2    Blackstone, C.3
  • 67
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt, J. K., Echeverri, C. J., Nilsson, T., & Vallee, R. B. Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 139, 469-484 (1997
    • (1997) J. Cell Biol , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 68
    • 83255193923 scopus 로고    scopus 로고
    • The enlarged lysosomes in beigej cells result from decreased lysosome fission and not increased lysosome fusion
    • Durchfort, N., et al. The enlarged lysosomes in beigej cells result from decreased lysosome fission and not increased lysosome fusion. Traffic 13, 108-119 (2012
    • (2012) Traffic , vol.13 , pp. 108-119
    • Durchfort, N.1
  • 69
    • 84927126103 scopus 로고    scopus 로고
    • Cholesterol transport through lysosome-peroxisome membrane contacts
    • Chu, B. B., et al. Cholesterol transport through lysosome-peroxisome membrane contacts. Cell 161, 291-306 (2015
    • (2015) Cell , vol.161 , pp. 291-306
    • Chu, B.B.1
  • 70
    • 84867565289 scopus 로고    scopus 로고
    • TPC proteins are phosphoinositide-activated sodium-selective ion channels in endosomes and lysosomes
    • Wang, X., et al. TPC proteins are phosphoinositide-activated sodium-selective ion channels in endosomes and lysosomes. Cell 151, 372-383 (2012
    • (2012) Cell , vol.151 , pp. 372-383
    • Wang, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.