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Volumn 6, Issue , 2015, Pages

Autophagosome-lysosome fusion is independent of V-ATPase-mediated acidification

Author keywords

[No Author keywords available]

Indexed keywords

BAFILOMYCIN A1; CALCIUM ION; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; ACID; MACROLIDE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84929193242     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8007     Document Type: Article
Times cited : (309)

References (70)
  • 3
    • 84891748139 scopus 로고    scopus 로고
    • A current perspective of autophagosome biogenesis
    • Shibutani, S. T. & Yoshimori, T. A current perspective of autophagosome biogenesis. Cell Res. 24, 58-68 (2014).
    • (2014) Cell Res. , vol.24 , pp. 58-68
    • Shibutani, S.T.1    Yoshimori, T.2
  • 4
    • 77955405903 scopus 로고    scopus 로고
    • Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase
    • Dechant, R. et al. Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase. EMBO J. 29, 2515-2526 (2010).
    • (2010) EMBO J. , vol.29 , pp. 2515-2526
    • Dechant, R.1
  • 5
    • 77955292351 scopus 로고    scopus 로고
    • PKA regulates vacuolar H+-ATPase localization and activity via direct phosphorylation of the a subunit in kidney cells
    • Alzamora, R. et al. PKA regulates vacuolar H+-ATPase localization and activity via direct phosphorylation of the a subunit in kidney cells. J. Biol. Chem. 285, 24676-24685 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 24676-24685
    • Alzamora, R.1
  • 6
    • 47349120492 scopus 로고    scopus 로고
    • The V-type H+-ATPase in vesicular trafficking: Targeting, regulation and function
    • Marshansky, V. & Futai, M. The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function. Curr. Opin. Cell Biol. 20, 415-426 (2008).
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 7
    • 84903902451 scopus 로고    scopus 로고
    • Regulation of endothelial signaling and migration by v-ATPase
    • Rath, S., Liebl, J., Furst, R., Vollmar, A. M. & Zahler, S. Regulation of endothelial signaling and migration by v-ATPase. Angiogenesis 17, 587-601 (2014).
    • (2014) Angiogenesis , vol.17 , pp. 587-601
    • Rath, S.1    Liebl, J.2    Furst, R.3    Vollmar, A.M.4    Zahler, S.5
  • 8
    • 62149142874 scopus 로고    scopus 로고
    • V-ATPase functions in normal and disease processes
    • Hinton, A., Bond, S. & Forgac, M. V-ATPase functions in normal and disease processes. Pflugers Arch. 457, 589-598 (2009).
    • (2009) Pflugers Arch. , vol.457 , pp. 589-598
    • Hinton, A.1    Bond, S.2    Forgac, M.3
  • 9
    • 0027978351 scopus 로고
    • Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase
    • Zhang, J., Feng, Y. & Forgac, M. Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase. J. Biol. Chem. 269, 23518-23523 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 23518-23523
    • Zhang, J.1    Feng, Y.2    Forgac, M.3
  • 10
    • 0025925091 scopus 로고
    • Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells
    • Yoshimori, T., Yamamoto, A., Moriyama, Y., Futai, M. & Tashiro, Y. Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells. J. Biol. Chem. 266, 17707-17712 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 17707-17712
    • Yoshimori, T.1    Yamamoto, A.2    Moriyama, Y.3    Futai, M.4    Tashiro, Y.5
  • 11
    • 84901667197 scopus 로고    scopus 로고
    • Ca2+-calmodulin regulates SNARE assembly and spontaneous neurotransmitter release via v-ATPase subunit V0a1
    • Wang, D. et al. Ca2+-Calmodulin regulates SNARE assembly and spontaneous neurotransmitter release via v-ATPase subunit V0a1. J. Cell Biol. 205, 21-31 (2014).
    • (2014) J. Cell Biol. , vol.205 , pp. 21-31
    • Wang, D.1
  • 12
    • 84896692098 scopus 로고    scopus 로고
    • Eukaryotic V-ATPase: Novel structural findings and functional insights
    • Marshansky, V., Rubinstein, J. L. & Gruber, G. Eukaryotic V-ATPase: novel structural findings and functional insights. Biochim. Biophys. Acta. 1837, 857-879 (2014).
    • (2014) Biochim. Biophys. Acta. , vol.1837 , pp. 857-879
    • Marshansky, V.1    Rubinstein, J.L.2    Gruber, G.3
  • 13
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 14
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • Klionsky, D. J. et al. Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy 8, 445-544 (2012).
    • (2012) Autophagy , vol.8 , pp. 445-544
    • Klionsky, D.J.1
  • 15
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvationinduced autophagy in the drosophila fat body
    • Scott, R. C., Schuldiner, O. & Neufeld, T. P. Role and regulation of starvationinduced autophagy in the Drosophila fat body. Dev. Cell 7, 167-178 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 167-178
    • Scott, R.C.1    Schuldiner, O.2    Neufeld, T.P.3
  • 16
    • 4344608793 scopus 로고    scopus 로고
    • Programmed autophagy in the drosophila fat body is induced by ecdysone through regulation of the PI3K pathway
    • Rusten, T. E. et al. Programmed autophagy in the Drosophila fat body is induced by ecdysone through regulation of the PI3K pathway. Dev. Cell 7, 179-192 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 179-192
    • Rusten, T.E.1
  • 17
    • 77955903343 scopus 로고    scopus 로고
    • Autophagic degradation of dBruce controls DNA fragmentation in nurse cells during late drosophila melanogaster oogenesis
    • Nezis, I. P. et al. Autophagic degradation of dBruce controls DNA fragmentation in nurse cells during late Drosophila melanogaster oogenesis. J. Cell Biol. 190, 523-531 (2010).
    • (2010) J. Cell Biol. , vol.190 , pp. 523-531
    • Nezis, I.P.1
  • 18
    • 34548077575 scopus 로고    scopus 로고
    • Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3
    • Kimura, S., Noda, T. & Yoshimori, T. Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3. Autophagy 3, 452-460 (2007).
    • (2007) Autophagy , vol.3 , pp. 452-460
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 19
    • 43949092111 scopus 로고    scopus 로고
    • The PI 3-kinase regulator vps15 is required for autophagic clearance of protein aggregates
    • Lindmo, K. et al. The PI 3-kinase regulator Vps15 is required for autophagic clearance of protein aggregates. Autophagy 4, 500-506 (2008).
    • (2008) Autophagy , vol.4 , pp. 500-506
    • Lindmo, K.1
  • 20
    • 65249155441 scopus 로고    scopus 로고
    • An atg1/Atg13 complex with multiple roles in TOR-mediated autophagy regulation
    • Chang, Y. Y. & Neufeld, T. P. An Atg1/Atg13 complex with multiple roles in TOR-mediated autophagy regulation. Mol. Biol. Cell 20, 2004-2014 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2004-2014
    • Chang, Y.Y.1    Neufeld, T.P.2
  • 21
    • 41549151641 scopus 로고    scopus 로고
    • Ref(2)P, the drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain
    • Nezis, I. P. et al. Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain. J. Cell Biol. 180, 1065-1071 (2008).
    • (2008) J. Cell Biol. , vol.180 , pp. 1065-1071
    • Nezis, I.P.1
  • 22
    • 84865623676 scopus 로고    scopus 로고
    • Advantages and limitations of different p62-based assays for estimating autophagic activity in drosophila
    • Pircs, K. et al. Advantages and limitations of different p62-based assays for estimating autophagic activity in Drosophila. PLoS ONE 7, e44214 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e44214
    • Pircs, K.1
  • 23
    • 0020040519 scopus 로고
    • Accumulation of autophagosomes after inhibition of hepatocytic protein degradation by vinblastine, leupeptin or a lysosomotropic amine
    • Kovacs, A. L., Reith, A. & Seglen, P. O. Accumulation of autophagosomes after inhibition of hepatocytic protein degradation by vinblastine, leupeptin or a lysosomotropic amine. Exp. Cell Res. 137, 191-201 (1982).
    • (1982) Exp. Cell Res. , vol.137 , pp. 191-201
    • Kovacs, A.L.1    Reith, A.2    Seglen, P.O.3
  • 24
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto, A. et al. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct. Funct. 23, 33-42 (1998).
    • (1998) Cell Struct. Funct. , vol.23 , pp. 33-42
    • Yamamoto, A.1
  • 25
    • 53549084325 scopus 로고    scopus 로고
    • Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?
    • Klionsky, D. J., Elazar, Z., Seglen, P. O. & Rubinsztein, D. C. Does bafilomycin A1 block the fusion of autophagosomes with lysosomes? Autophagy 4, 849-850 (2008).
    • (2008) Autophagy , vol.4 , pp. 849-850
    • Klionsky, D.J.1    Elazar, Z.2    Seglen, P.O.3    Rubinsztein, D.C.4
  • 26
    • 0040117958 scopus 로고    scopus 로고
    • Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases
    • Drose, S. & Altendorf, K. Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases. J. Exp. Biol. 200, 1-8 (1997).
    • (1997) J. Exp. Biol. , vol.200 , pp. 1-8
    • Drose, S.1    Altendorf, K.2
  • 27
    • 84878615771 scopus 로고    scopus 로고
    • Autophagosomal syntaxin17-dependent lysosomal degradation maintains neuronal function in drosophila
    • Takats, S. et al. Autophagosomal Syntaxin17-dependent lysosomal degradation maintains neuronal function in Drosophila. J. Cell Biol. 201, 531-539 (2013).
    • (2013) J. Cell Biol. , vol.201 , pp. 531-539
    • Takats, S.1
  • 28
    • 84870880174 scopus 로고    scopus 로고
    • The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • Itakura, E., Kishi-Itakura, C. & Mizushima, N. The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell 151, 1256-1269 (2012).
    • (2012) Cell , vol.151 , pp. 1256-1269
    • Itakura, E.1    Kishi-Itakura, C.2    Mizushima, N.3
  • 29
    • 0029414780 scopus 로고
    • Analysis of the membrane structures involved in autophagy in yeast by freeze-replica method
    • Baba, M., Osumi, M. & Ohsumi, Y. Analysis of the membrane structures involved in autophagy in yeast by freeze-replica method. Cell Struct. Funct. 20, 465-471 (1995).
    • (1995) Cell Struct. Funct. , vol.20 , pp. 465-471
    • Baba, M.1    Osumi, M.2    Ohsumi, Y.3
  • 30
    • 0026668042 scopus 로고
    • Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
    • Takeshige, K., Baba, M., Tsuboi, S., Noda, T. & Ohsumi, Y. Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J. Cell Biol. 119, 301-311 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 301-311
    • Takeshige, K.1    Baba, M.2    Tsuboi, S.3    Noda, T.4    Ohsumi, Y.5
  • 31
    • 0037040244 scopus 로고    scopus 로고
    • Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site
    • Bowman, B. J. & Bowman, E. J. Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site. J. Biol. Chem. 277, 3965-3972 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 3965-3972
    • Bowman, B.J.1    Bowman, E.J.2
  • 32
    • 40449139980 scopus 로고    scopus 로고
    • The itinerary of autophagosomes: From peripheral formation to kiss-and-run fusion with lysosomes
    • Jahreiss, L., Menzies, F. M. & Rubinsztein, D. C. The itinerary of autophagosomes: from peripheral formation to kiss-and-run fusion with lysosomes. Traffic. 9, 574-587 (2008).
    • (2008) Traffic. , vol.9 , pp. 574-587
    • Jahreiss, L.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 33
    • 84928139826 scopus 로고    scopus 로고
    • Dietary sugar promotes systemic TOR activation in drosophila through AKH-dependent selective secretion of dilp3
    • Kim, J. & Neufeld, T. P. Dietary sugar promotes systemic TOR activation in Drosophila through AKH-dependent selective secretion of Dilp3. Nat. Commun. doi:10.1038/ncomms7846 (2015).
    • (2015) Nat. Commun.
    • Kim, J.1    Neufeld, T.P.2
  • 34
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman, E. J., Siebers, A. & Altendorf, K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl Acad. Sci. USA 85, 7972-7976 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 35
    • 0023819315 scopus 로고
    • A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene
    • Gunteski-Hamblin, A. M., Greeb, J. & Shull, G. E. A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. J. Biol. Chem. 263, 15032-15040 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 15032-15040
    • Gunteski-Hamblin, A.M.1    Greeb, J.2    Shull, G.E.3
  • 36
    • 84885664839 scopus 로고    scopus 로고
    • Modulation of intracellular calcium homeostasis blocks autophagosome formation
    • Engedal, N. et al. Modulation of intracellular calcium homeostasis blocks autophagosome formation. Autophagy 9, 1475-1490 (2013).
    • (2013) Autophagy , vol.9 , pp. 1475-1490
    • Engedal, N.1
  • 37
    • 0026050850 scopus 로고
    • Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps
    • Lytton, J., Westlin, M. & Hanley, M. R. Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps. J. Biol. Chem. 266, 17067-17071 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 17067-17071
    • Lytton, J.1    Westlin, M.2    Hanley, M.R.3
  • 38
    • 79959346132 scopus 로고    scopus 로고
    • Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest
    • Ganley, I. G., Wong, P. M., Gammoh, N. & Jiang, X. Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol. Cell 42, 731-743 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 731-743
    • Ganley, I.G.1    Wong, P.M.2    Gammoh, N.3    Jiang, X.4
  • 39
    • 84899942026 scopus 로고    scopus 로고
    • Seipin promotes adipose tissue fat storage through the ER Ca(2)(+)- ATPase SERCA
    • Bi, J. et al. Seipin promotes adipose tissue fat storage through the ER Ca(2)(+)- ATPase SERCA. Cell Metab. 19, 861-871 (2014).
    • (2014) Cell Metab. , vol.19 , pp. 861-871
    • Bi, J.1
  • 40
    • 43149104361 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of lysosomal membrane transporters
    • Sagne, C. & Gasnier, B. Molecular physiology and pathophysiology of lysosomal membrane transporters. J. Inherit. Metab. Dis. 31, 258-266 (2008).
    • (2008) J. Inherit. Metab. Dis. , vol.31 , pp. 258-266
    • Sagne, C.1    Gasnier, B.2
  • 41
    • 0036472494 scopus 로고    scopus 로고
    • PH-dependent regulation of lysosomal calcium in macrophages
    • Christensen, K. A., Myers, J. T. & Swanson, J. A. pH-dependent regulation of lysosomal calcium in macrophages. J. Cell Sci. 115, 599-607 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 599-607
    • Christensen, K.A.1    Myers, J.T.2    Swanson, J.A.3
  • 42
    • 0034729167 scopus 로고    scopus 로고
    • The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • Pryor, P. R., Mullock, B. M., Bright, N. A., Gray, S. R. & Luzio, J. P. The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol. 149, 1053-1062 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 43
    • 80054953356 scopus 로고    scopus 로고
    • The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles
    • Strasser, B., Iwaszkiewicz, J., Michielin, O. & Mayer, A. The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles. EMBO J. 30, 4126-4141 (2011).
    • (2011) EMBO J. , vol.30 , pp. 4126-4141
    • Strasser, B.1    Iwaszkiewicz, J.2    Michielin, O.3    Mayer, A.4
  • 44
    • 77953165886 scopus 로고    scopus 로고
    • A dual function of V0-ATPase a1 provides an endolysosomal degradation mechanism in drosophila melanogaster photoreceptors
    • Williamson, W. R., Wang, D., Haberman, A. S. & Hiesinger, P. R. A dual function of V0-ATPase a1 provides an endolysosomal degradation mechanism in Drosophila melanogaster photoreceptors. J. Cell Biol. 189, 885-899 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 885-899
    • Williamson, W.R.1    Wang, D.2    Haberman, A.S.3    Hiesinger, P.R.4
  • 45
    • 34948873616 scopus 로고    scopus 로고
    • Role of the V-ATPase in regulation of the vacuolar fission-fusion equilibrium
    • Baars, T. L., Petri, S., Peters, C. & Mayer, A. Role of the V-ATPase in regulation of the vacuolar fission-fusion equilibrium. Mol. Biol. Cell. 18, 3873-3882 (2007).
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 3873-3882
    • Baars, T.L.1    Petri, S.2    Peters, C.3    Mayer, A.4
  • 46
    • 84888181788 scopus 로고    scopus 로고
    • Homotypic vacuole fusion in yeast requires organelle acidification and not the V-ATPase membrane domain
    • Coonrod, E. M. et al. Homotypic vacuole fusion in yeast requires organelle acidification and not the V-ATPase membrane domain. Dev. Cell 27, 462-468 (2013).
    • (2013) Dev. Cell , vol.27 , pp. 462-468
    • Coonrod, E.M.1
  • 47
    • 84887531850 scopus 로고    scopus 로고
    • The V-ATPase membrane domain is a sensor of granular pH that controls the exocytotic machinery
    • Poea-Guyon, S. et al. The V-ATPase membrane domain is a sensor of granular pH that controls the exocytotic machinery. J. Cell Biol. 203, 283-298 (2013).
    • (2013) J. Cell Biol. , vol.203 , pp. 283-298
    • Poea-Guyon, S.1
  • 48
    • 33947401472 scopus 로고    scopus 로고
    • Autophagosome-lysosome fusion depends on the pH in acidic compartments in CHO cells
    • Kawai, A., Uchiyama, H., Takano, S., Nakamura, N. & Ohkuma, S. Autophagosome-lysosome fusion depends on the pH in acidic compartments in CHO cells. Autophagy 3, 154-157 (2007).
    • (2007) Autophagy , vol.3 , pp. 154-157
    • Kawai, A.1    Uchiyama, H.2    Takano, S.3    Nakamura, N.4    Ohkuma, S.5
  • 49
    • 84898871064 scopus 로고    scopus 로고
    • ATP6V0C knockdown in neuroblastoma cells alters autophagy-lysosome pathway function and metabolism of proteins that accumulate in neurodegenerative disease
    • Mangieri, L. R. et al. ATP6V0C knockdown in neuroblastoma cells alters autophagy-lysosome pathway function and metabolism of proteins that accumulate in neurodegenerative disease. PLoS ONE 9, e93257 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e93257
    • Mangieri, L.R.1
  • 50
    • 70350374082 scopus 로고    scopus 로고
    • Inhibitors of the V0 subunit of the vacuolar H+-ATPase prevent segregation of lysosomal- and secretorypathway proteins
    • Sobota, J. A., Back, N., Eipper, B. A. & Mains, R. E. Inhibitors of the V0 subunit of the vacuolar H+-ATPase prevent segregation of lysosomal- and secretorypathway proteins. J. Cell Sci. 122, 3542-3553 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 3542-3553
    • Sobota, J.A.1    Back, N.2    Eipper, B.A.3    Mains, R.E.4
  • 52
    • 33645100369 scopus 로고    scopus 로고
    • Bafilomycin A1 inhibits chloroquine-induced death of cerebellar granule neurons
    • Shacka, J. J. et al. Bafilomycin A1 inhibits chloroquine-induced death of cerebellar granule neurons. Mol. Pharmacol. 69, 1125-1136 (2006).
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1125-1136
    • Shacka, J.J.1
  • 53
    • 23944478891 scopus 로고    scopus 로고
    • Ca2+ accumulation into acidic organelles mediated by Ca2+- and vacuolar H+-ATPases in human platelets
    • Lopez, J. J., Camello-Almaraz, C., Pariente, J. A., Salido, G. M. & Rosado, J. A. Ca2+ accumulation into acidic organelles mediated by Ca2+- and vacuolar H+-ATPases in human platelets. Biochem. J. 390, 243-252 (2005).
    • (2005) Biochem. J. , vol.390 , pp. 243-252
    • Lopez, J.J.1    Camello-Almaraz, C.2    Pariente, J.A.3    Salido, G.M.4    Rosado, J.A.5
  • 54
    • 0034210661 scopus 로고    scopus 로고
    • Hydroxychloroquine inhibits calcium signals in T cells: A new mechanism to explain its immunomodulatory properties
    • Goldman, F. D. et al. Hydroxychloroquine inhibits calcium signals in T cells: a new mechanism to explain its immunomodulatory properties. Blood 95, 3460-3466 (2000).
    • (2000) Blood , vol.95 , pp. 3460-3466
    • Goldman, F.D.1
  • 55
    • 0033964806 scopus 로고    scopus 로고
    • Ammonium triggers calcium elevation in cultured mouse microglial cells by initiating Ca(2+) release from thapsigargin-sensitive intracellular stores
    • Minelli, A., Lyons, S., Nolte, C., Verkhratsky, A. & Kettenmann, H. Ammonium triggers calcium elevation in cultured mouse microglial cells by initiating Ca(2+) release from thapsigargin-sensitive intracellular stores. Pflugers Arch. 439, 370-377 (2000).
    • (2000) Pflugers Arch. , vol.439 , pp. 370-377
    • Minelli, A.1    Lyons, S.2    Nolte, C.3    Verkhratsky, A.4    Kettenmann, H.5
  • 56
    • 84891345615 scopus 로고    scopus 로고
    • Calcium-dependent regulation of rab activation and vesicle fusion by an intracellular P2X ion channel
    • Parkinson, K. et al. Calcium-dependent regulation of Rab activation and vesicle fusion by an intracellular P2X ion channel. Nat. Cell. Biol. 16, 87-98 (2014).
    • (2014) Nat. Cell. Biol. , vol.16 , pp. 87-98
    • Parkinson, K.1
  • 57
    • 79960962456 scopus 로고    scopus 로고
    • Role of SNAREs in membrane fusion
    • Jena, B. P. Role of SNAREs in membrane fusion. Adv. Exp. Med. Biol. 713, 13-32 (2011).
    • (2011) Adv. Exp. Med. Biol. , vol.713 , pp. 13-32
    • Jena, B.P.1
  • 58
    • 33847388051 scopus 로고    scopus 로고
    • Calcium: A fundamental regulator of intracellular membrane fusion?
    • Hay, J. C. Calcium: a fundamental regulator of intracellular membrane fusion? EMBO Rep. 8, 236-240 (2007).
    • (2007) EMBO Rep. , vol.8 , pp. 236-240
    • Hay, J.C.1
  • 60
    • 84876335322 scopus 로고    scopus 로고
    • Bidirectional Ca(2)(+) signaling occurs between the endoplasmic reticulum and acidic organelles
    • Morgan, A. J. et al. Bidirectional Ca(2)(+) signaling occurs between the endoplasmic reticulum and acidic organelles. J. Cell Biol. 200, 789-805 (2013).
    • (2013) J. Cell Biol. , vol.200 , pp. 789-805
    • Morgan, A.J.1
  • 61
    • 84875583989 scopus 로고    scopus 로고
    • Lysosomes shape ins(1,4,5)P3-evoked Ca2+ signals by selectively sequestering Ca2+ released from the endoplasmic reticulum
    • Lopez-Sanjurjo, C. I., Tovey, S. C., Prole, D. L. & Taylor, C. W. Lysosomes shape Ins(1,4,5)P3-evoked Ca2+ signals by selectively sequestering Ca2+ released from the endoplasmic reticulum. J. Cell Sci. 126, 289-300 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 289-300
    • Lopez-Sanjurjo, C.I.1    Tovey, S.C.2    Prole, D.L.3    Taylor, C.W.4
  • 62
    • 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
  • 63
    • 84922133228 scopus 로고    scopus 로고
    • Pharmacological correction of obesity-induced autophagy arrest using calcium channel blockers
    • Park, H. W. et al. Pharmacological correction of obesity-induced autophagy arrest using calcium channel blockers. Nat. Commun. 5, 4834 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4834
    • Park, H.W.1
  • 64
    • 80052638037 scopus 로고    scopus 로고
    • A dual role for Ca(2+) in autophagy regulation
    • Decuypere, J. P., Bultynck, G. & Parys, J. B. A dual role for Ca(2+) in autophagy regulation. Cell Calcium 50, 242-250 (2011).
    • (2011) Cell Calcium , vol.50 , pp. 242-250
    • Decuypere, J.P.1    Bultynck, G.2    Parys, J.B.3
  • 65
    • 67650649726 scopus 로고    scopus 로고
    • A genetic screen in drosophila reveals novel cytoprotective functions of the autophagy-lysosome pathway
    • Arsham, A. M. & Neufeld, T. P. A genetic screen in Drosophila reveals novel cytoprotective functions of the autophagy-lysosome pathway. PLoS ONE 4, e6068 (2009).
    • (2009) PLoS ONE , vol.4 , pp. e6068
    • Arsham, A.M.1    Neufeld, T.P.2
  • 66
    • 34250731404 scopus 로고    scopus 로고
    • Thirty-one flavors of drosophila rab proteins
    • Zhang, J. et al. Thirty-one flavors of Drosophila rab proteins. Genetics 176, 1307-1322 (2007).
    • (2007) Genetics , vol.176 , pp. 1307-1322
    • Zhang, J.1
  • 67
    • 77956635784 scopus 로고    scopus 로고
    • Wnt/frizzled signaling requires dPRR, the drosophila homolog of the prorenin receptor
    • Buechling, T. et al. Wnt/Frizzled signaling requires dPRR, the Drosophila homolog of the prorenin receptor. Curr. Biol. 20, 1263-1268 (2010).
    • (2010) Curr. Biol. , vol.20 , pp. 1263-1268
    • Buechling, T.1
  • 68
    • 24944583279 scopus 로고    scopus 로고
    • Drosophila vps16a is required for trafficking to lysosomes and biogenesis of pigment granules
    • Pulipparacharuvil, S. et al. Drosophila Vps16A is required for trafficking to lysosomes and biogenesis of pigment granules. J. Cell. Sci. 118, 3663-3673 (2005).
    • (2005) J. Cell. Sci. , vol.118 , pp. 3663-3673
    • Pulipparacharuvil, S.1
  • 69
    • 84883390990 scopus 로고    scopus 로고
    • Fast GCaMPs for improved tracking of neuronal activity
    • Sun, X. R. et al. Fast GCaMPs for improved tracking of neuronal activity. Nat. Commun. 4, 2170 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 2170
    • Sun, X.R.1
  • 70
    • 33745235142 scopus 로고    scopus 로고
    • TOR coordinates bulk and targeted endocytosis in the drosophila melanogaster fat body to regulate cell growth
    • Hennig, K. M., Colombani, J. & Neufeld, T. P. TOR coordinates bulk and targeted endocytosis in the Drosophila melanogaster fat body to regulate cell growth. J. Cell Biol. 173, 963-974 (2006).
    • (2006) J. Cell Biol. , vol.173 , pp. 963-974
    • Hennig, K.M.1    Colombani, J.2    Neufeld, T.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.