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Volumn 7, Issue 8, 2012, Pages

Class IA phosphatidylinositol 3-kinase p110α regulates phagosome maturation

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; EARLY ENDOSOME ANTIGEN 1; ISOPROTEIN; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; LYSOSOME ENZYME; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE 3 KINASE; PROTEIN P110; PROTEIN P110 ALPHA; PROTEIN VPS16; PROTEIN VPS41; RAB INTERACTING LYSOSOMAL PROTEIN; RAB PROTEIN; RAB7 PROTEIN; UNCLASSIFIED DRUG;

EID: 84865200051     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043668     Document Type: Article
Times cited : (8)

References (92)
  • 1
    • 77954956229 scopus 로고    scopus 로고
    • Initial receptor-ligand interactions modulate gene expression and phagosomal properties during both early and late stages of phagocytosis
    • Hoffmann E, Marion S, Mishra BB, John M, Kratzke R, et al. ((2010)) Initial receptor-ligand interactions modulate gene expression and phagosomal properties during both early and late stages of phagocytosis. Eur J Cell Biol 89:: 693--704.
    • (2010) Eur J Cell Biol , vol.89 , pp. 693-704
    • Hoffmann, E.1    Marion, S.2    Mishra, B.B.3    John, M.4    Kratzke, R.5
  • 2
    • 84891735818 scopus 로고    scopus 로고
    • Defined particle ligands trigger specific defense mechanisms of macrophages
    • Dykstra T, Utermoehlen O, Haas A (2010) Defined particle ligands trigger specific defense mechanisms of macrophages. Innate Immun.
    • (2010) Innate Immun.
    • Dykstra, T.1    Utermoehlen, O.2    Haas, A.3
  • 3
    • 77956958415 scopus 로고    scopus 로고
    • SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages
    • Berger SB, Romero X, Ma C, Wang G, Faubion WA, et al. ((2010)) SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages. Nat Immunol 11:: 920--927.
    • (2010) Nat Immunol , vol.11 , pp. 920-927
    • Berger, S.B.1    Romero, X.2    Ma, C.3    Wang, G.4    Faubion, W.A.5
  • 4
    • 33748848754 scopus 로고    scopus 로고
    • On regulation of phagosome maturation and antigen presentation
    • Blander JM, Medzhitov R, ((2006)) On regulation of phagosome maturation and antigen presentation. Nat Immunol 7:: 1029--1035.
    • (2006) Nat Immunol , vol.7 , pp. 1029-1035
    • Blander, J.M.1    Medzhitov, R.2
  • 5
    • 26644447615 scopus 로고    scopus 로고
    • Phagosome maturation proceeds independently of stimulation of toll-like receptors 2 and 4
    • Yates RM, Russell DG, ((2005)) Phagosome maturation proceeds independently of stimulation of toll-like receptors 2 and 4. Immunity 23:: 409--417.
    • (2005) Immunity , vol.23 , pp. 409-417
    • Yates, R.M.1    Russell, D.G.2
  • 6
    • 0028834530 scopus 로고
    • The two mannose 6-phosphate receptors transport distinct complements of lysosomal proteins
    • Pohlmann R, Boeker MW, von Figura K, ((1995)) The two mannose 6-phosphate receptors transport distinct complements of lysosomal proteins. J Biol Chem 270:: 27311--27318.
    • (1995) J Biol Chem , vol.270 , pp. 27311-27318
    • Pohlmann, R.1    Boeker, M.W.2    von Figura, K.3
  • 7
    • 0035494493 scopus 로고    scopus 로고
    • Distinct roles of class I and class III phosphatidylinositol 3-kinases in phagosome formation and maturation
    • Vieira OV, Botelho RJ, Rameh L, Brachmann SM, Matsuo T, et al. ((2001)) Distinct roles of class I and class III phosphatidylinositol 3-kinases in phagosome formation and maturation. J Cell Biol 155:: 19--25.
    • (2001) J Cell Biol , vol.155 , pp. 19-25
    • Vieira, O.V.1    Botelho, R.J.2    Rameh, L.3    Brachmann, S.M.4    Matsuo, T.5
  • 8
    • 0037378608 scopus 로고    scopus 로고
    • Modulation of Rab5 and Rab7 recruitment to phagosomes by phosphatidylinositol 3-kinase
    • Vieira OV, Bucci C, Harrison RE, Trimble WS, Lanzetti L, et al. ((2003)) Modulation of Rab5 and Rab7 recruitment to phagosomes by phosphatidylinositol 3-kinase. Mol Cell Biol 23:: 2501--2514.
    • (2003) Mol Cell Biol , vol.23 , pp. 2501-2514
    • Vieira, O.V.1    Bucci, C.2    Harrison, R.E.3    Trimble, W.S.4    Lanzetti, L.5
  • 9
    • 0032037616 scopus 로고    scopus 로고
    • Macrophage receptors for Mycobacterium tuberculosis
    • Ernst JD, ((1998)) Macrophage receptors for Mycobacterium tuberculosis. Infect Immun 66:: 1277--1281.
    • (1998) Infect Immun , vol.66 , pp. 1277-1281
    • Ernst, J.D.1
  • 10
    • 0027173039 scopus 로고
    • Macrophage phagocytosis of virulent but not attenuated strains of Mycobacterium tuberculosis is mediated by mannose receptors in addition to complement receptors
    • Schlesinger LS, ((1993)) Macrophage phagocytosis of virulent but not attenuated strains of Mycobacterium tuberculosis is mediated by mannose receptors in addition to complement receptors. J Immunol 150:: 2920--2930.
    • (1993) J Immunol , vol.150 , pp. 2920-2930
    • Schlesinger, L.S.1
  • 11
    • 0034677007 scopus 로고    scopus 로고
    • Inhibition of Ca(2+) signaling by Mycobacterium tuberculosis is associated with reduced phagosome-lysosome fusion and increased survival within human macrophages
    • Malik ZA, Denning GM, Kusner DJ, ((2000)) Inhibition of Ca(2+) signaling by Mycobacterium tuberculosis is associated with reduced phagosome-lysosome fusion and increased survival within human macrophages. J Exp Med 191:: 287--302.
    • (2000) J Exp Med , vol.191 , pp. 287-302
    • Malik, Z.A.1    Denning, G.M.2    Kusner, D.J.3
  • 12
    • 0035284908 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis phagosomes exhibit altered calmodulin-dependent signal transduction: contribution to inhibition of phagosome-lysosome fusion and intracellular survival in human macrophages
    • Malik ZA, Iyer SS, Kusner DJ, ((2001)) Mycobacterium tuberculosis phagosomes exhibit altered calmodulin-dependent signal transduction: contribution to inhibition of phagosome-lysosome fusion and intracellular survival in human macrophages. J Immunol 166:: 3392--3401.
    • (2001) J Immunol , vol.166 , pp. 3392-3401
    • Malik, Z.A.1    Iyer, S.S.2    Kusner, D.J.3
  • 13
    • 0037443426 scopus 로고    scopus 로고
    • Cutting edge: Mycobacterium tuberculosis blocks Ca2+ signaling and phagosome maturation in human macrophages via specific inhibition of sphingosine kinase
    • Malik ZA, Thompson CR, Hashimi S, Porter B, Iyer SS, et al. ((2003)) Cutting edge: Mycobacterium tuberculosis blocks Ca2+ signaling and phagosome maturation in human macrophages via specific inhibition of sphingosine kinase. J Immunol 170:: 2811--2815.
    • (2003) J Immunol , vol.170 , pp. 2811-2815
    • Malik, Z.A.1    Thompson, C.R.2    Hashimi, S.3    Porter, B.4    Iyer, S.S.5
  • 14
    • 0032935608 scopus 로고    scopus 로고
    • The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages
    • Astarie-Dequeker C, N'Diaye EN, Le Cabec V, Rittig MG, Prandi J, et al. ((1999)) The mannose receptor mediates uptake of pathogenic and nonpathogenic mycobacteria and bypasses bactericidal responses in human macrophages. Infect Immun 67:: 469--477.
    • (1999) Infect Immun , vol.67 , pp. 469-477
    • Astarie-Dequeker, C.1    N'Diaye, E.N.2    Le Cabec, V.3    Rittig, M.G.4    Prandi, J.5
  • 15
    • 0037106460 scopus 로고    scopus 로고
    • Phagosome maturation: aging gracefully
    • Vieira OV, Botelho RJ, Grinstein S, ((2002)) Phagosome maturation: aging gracefully. Biochem J 366:: 689--704.
    • (2002) Biochem J , vol.366 , pp. 689-704
    • Vieira, O.V.1    Botelho, R.J.2    Grinstein, S.3
  • 16
    • 1542364488 scopus 로고    scopus 로고
    • Stable gene silencing in human monocytic cell lines using lentiviral-delivered small interference RNA. Silencing of the p110alpha isoform of phosphoinositide 3-kinase reveals differential regulation of adherence induced by 1alpha,25-dihydroxycholecalciferol and bacterial lipopolysaccharide
    • Lee JS, Hmama Z, Mui A, Reiner NE, ((2004)) Stable gene silencing in human monocytic cell lines using lentiviral-delivered small interference RNA. Silencing of the p110alpha isoform of phosphoinositide 3-kinase reveals differential regulation of adherence induced by 1alpha,25-dihydroxycholecalciferol and bacterial lipopolysaccharide. J Biol Chem 279:: 9379--9388.
    • (2004) J Biol Chem , vol.279 , pp. 9379-9388
    • Lee, J.S.1    Hmama, Z.2    Mui, A.3    Reiner, N.E.4
  • 17
    • 0025873132 scopus 로고
    • Interaction of Mycobacterium avium complex with human macrophages: roles of membrane receptors and serum proteins
    • Bermudez LE, Young LS, Enkel H, ((1991)) Interaction of Mycobacterium avium complex with human macrophages: roles of membrane receptors and serum proteins. Infect Immun 59:: 1697--1702.
    • (1991) Infect Immun , vol.59 , pp. 1697-1702
    • Bermudez, L.E.1    Young, L.S.2    Enkel, H.3
  • 18
    • 0027137823 scopus 로고
    • Mycobacteria-macrophage interactions. Macrophage phenotype determines the nonopsonic binding of Mycobacterium tuberculosis to murine macrophages
    • Stokes RW, Haidl ID, Jefferies WA, Speert DP, ((1993)) Mycobacteria-macrophage interactions. Macrophage phenotype determines the nonopsonic binding of Mycobacterium tuberculosis to murine macrophages. J Immunol 151:: 7067--7076.
    • (1993) J Immunol , vol.151 , pp. 7067-7076
    • Stokes, R.W.1    Haidl, I.D.2    Jefferies, W.A.3    Speert, D.P.4
  • 19
    • 24144475288 scopus 로고    scopus 로고
    • Mycobacteria use their surface-exposed glycolipids to infect human macrophages through a receptor-dependent process
    • Villeneuve C, Gilleron M, Maridonneau-Parini I, Daffe M, Astarie-Dequeker C, et al. ((2005)) Mycobacteria use their surface-exposed glycolipids to infect human macrophages through a receptor-dependent process. J Lipid Res 46:: 475--483.
    • (2005) J Lipid Res , vol.46 , pp. 475-483
    • Villeneuve, C.1    Gilleron, M.2    Maridonneau-Parini, I.3    Daffe, M.4    Astarie-Dequeker, C.5
  • 20
    • 0033555931 scopus 로고    scopus 로고
    • A requirement for phosphatidylinositol 3-kinase in pseudopod extension
    • Cox D, Tseng CC, Bjekic G, Greenberg S, ((1999)) A requirement for phosphatidylinositol 3-kinase in pseudopod extension. J Biol Chem 274:: 1240--1247.
    • (1999) J Biol Chem , vol.274 , pp. 1240-1247
    • Cox, D.1    Tseng, C.C.2    Bjekic, G.3    Greenberg, S.4
  • 21
    • 17444415369 scopus 로고    scopus 로고
    • The kinetics of phagosome maturation as a function of phagosome/lysosome fusion and acquisition of hydrolytic activity
    • Yates RM, Hermetter A, Russell DG, ((2005)) The kinetics of phagosome maturation as a function of phagosome/lysosome fusion and acquisition of hydrolytic activity. Traffic 6:: 413--420.
    • (2005) Traffic , vol.6 , pp. 413-420
    • Yates, R.M.1    Hermetter, A.2    Russell, D.G.3
  • 22
    • 33644831090 scopus 로고    scopus 로고
    • The Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 replicates in mature phagolysosomes within J774 macrophages
    • Bringer MA, Glasser AL, Tung CH, Meresse S, Darfeuille-Michaud A, ((2006)) The Crohn's disease-associated adherent-invasive Escherichia coli strain LF82 replicates in mature phagolysosomes within J774 macrophages. Cell Microbiol 8:: 471--484.
    • (2006) Cell Microbiol , vol.8 , pp. 471-484
    • Bringer, M.A.1    Glasser, A.L.2    Tung, C.H.3    Meresse, S.4    Darfeuille-Michaud, A.5
  • 23
    • 33947126020 scopus 로고    scopus 로고
    • Birc1e/Naip5 rapidly antagonizes modulation of phagosome maturation by Legionella pneumophila
    • Fortier A, de Chastellier C, Balor S, Gros P, ((2007)) Birc1e/Naip5 rapidly antagonizes modulation of phagosome maturation by Legionella pneumophila. Cell Microbiol 9:: 910--923.
    • (2007) Cell Microbiol , vol.9 , pp. 910-923
    • Fortier, A.1    de Chastellier, C.2    Balor, S.3    Gros, P.4
  • 24
    • 77955300012 scopus 로고    scopus 로고
    • Coxiella burnetii phase I and II variants replicate with similar kinetics in degradative phagolysosome-like compartments of human macrophages
    • Howe D, Shannon JG, Winfree S, Dorward DW, Heinzen RA, ((2010)) Coxiella burnetii phase I and II variants replicate with similar kinetics in degradative phagolysosome-like compartments of human macrophages. Infect Immun 78:: 3465--3474.
    • (2010) Infect Immun , vol.78 , pp. 3465-3474
    • Howe, D.1    Shannon, J.G.2    Winfree, S.3    Dorward, D.W.4    Heinzen, R.A.5
  • 25
    • 73449094255 scopus 로고    scopus 로고
    • The Leishmania donovani lipophosphoglycan excludes the vesicular proton-ATPase from phagosomes by impairing the recruitment of synaptotagmin V
    • Vinet AF, Fukuda M, Turco SJ, Descoteaux A, ((2009)) The Leishmania donovani lipophosphoglycan excludes the vesicular proton-ATPase from phagosomes by impairing the recruitment of synaptotagmin V. PLoS Pathog. 5:: e1000628.
    • (2009) PLoS Pathog , vol.5
    • Vinet, A.F.1    Fukuda, M.2    Turco, S.J.3    Descoteaux, A.4
  • 26
    • 0021978631 scopus 로고
    • Processing of human cathepsin D in lysosomes in vitro
    • Gieselmann V, Hasilik A, von Figura K, ((1985)) Processing of human cathepsin D in lysosomes in vitro. J Biol Chem 260:: 3215--3220.
    • (1985) J Biol Chem , vol.260 , pp. 3215-3220
    • Gieselmann, V.1    Hasilik, A.2    von Figura, K.3
  • 27
    • 0032925550 scopus 로고    scopus 로고
    • Regulation of membrane transport through the endocytic pathway by rabGTPases
    • Mohrmann K, van der Sluijs P, ((1999)) Regulation of membrane transport through the endocytic pathway by rabGTPases. Mol Membr Biol 16:: 81--87.
    • (1999) Mol Membr Biol , vol.16 , pp. 81-87
    • Mohrmann, K.1    van der Sluijs, P.2
  • 28
    • 77953809435 scopus 로고    scopus 로고
    • Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes
    • Wu YW, Oesterlin LK, Tan KT, Waldmann H, Alexandrov K, et al. ((2010)) Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes. Nat Chem Biol 6:: 534--540.
    • (2010) Nat Chem Biol , vol.6 , pp. 534-540
    • Wu, Y.W.1    Oesterlin, L.K.2    Tan, K.T.3    Waldmann, H.4    Alexandrov, K.5
  • 29
    • 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 CB, Bucci C, ((2001)) Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. EMBO J 20:: 683--693.
    • (2001) EMBO J , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 30
    • 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, Rocha N, Zwart W, Jordens I, Janssen L, et al. ((2007)) 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) J Cell Biol , vol.176 , pp. 459-471
    • Johansson, M.1    Rocha, N.2    Zwart, W.3    Jordens, I.4    Janssen, L.5
  • 31
    • 0035975946 scopus 로고    scopus 로고
    • The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors
    • Jordens I, Fernandez-Borja M, Marsman M, Dusseljee S, Janssen L, et al. ((2001)) The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors. Curr Biol 11:: 1680--1685.
    • (2001) Curr Biol , vol.11 , pp. 1680-1685
    • Jordens, I.1    Fernandez-Borja, M.2    Marsman, M.3    Dusseljee, S.4    Janssen, L.5
  • 32
    • 0035126830 scopus 로고    scopus 로고
    • Vam3p structure reveals conserved and divergent properties of syntaxins
    • Dulubova I, Yamaguchi T, Wang Y, Sudhof TC, Rizo J, ((2001)) Vam3p structure reveals conserved and divergent properties of syntaxins. Nat Struct Biol 8:: 258--264.
    • (2001) Nat Struct Biol , vol.8 , pp. 258-264
    • Dulubova, I.1    Yamaguchi, T.2    Wang, Y.3    Sudhof, T.C.4    Rizo, J.5
  • 33
    • 0035201213 scopus 로고    scopus 로고
    • The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion
    • Laage R, Ungermann C, ((2001)) The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion. Mol Biol Cell 12:: 3375--3385.
    • (2001) Mol Biol Cell , vol.12 , pp. 3375-3385
    • Laage, R.1    Ungermann, C.2
  • 34
    • 77956490410 scopus 로고    scopus 로고
    • Defined Subunit Arrangement and Rab Interactions Are Required for Functionality of the HOPS Tethering Complex
    • Ostrowicz CW, Brocker C, Ahnert F, Nordmann M, Lachmann J, et al. ((2010)) Defined Subunit Arrangement and Rab Interactions Are Required for Functionality of the HOPS Tethering Complex. Traffic 11:: 1334--1346.
    • (2010) Traffic , vol.11 , pp. 1334-1346
    • Ostrowicz, C.W.1    Brocker, C.2    Ahnert, F.3    Nordmann, M.4    Lachmann, J.5
  • 35
    • 0033634646 scopus 로고    scopus 로고
    • Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion
    • Sato TK, Rehling P, Peterson MR, Emr SD, ((2000)) Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Mol Cell 6:: 661--671.
    • (2000) Mol Cell , vol.6 , pp. 661-671
    • Sato, T.K.1    Rehling, P.2    Peterson, M.R.3    Emr, S.D.4
  • 36
    • 0034735539 scopus 로고    scopus 로고
    • New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
    • Wurmser AE, Sato TK, Emr SD, ((2000)) New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J Cell Biol 151:: 551--562.
    • (2000) J Cell Biol , vol.151 , pp. 551-562
    • Wurmser, A.E.1    Sato, T.K.2    Emr, S.D.3
  • 37
    • 0042592913 scopus 로고    scopus 로고
    • Deletion of the SNARE vti1b in mice results in the loss of a single SNARE partner, syntaxin 8
    • Atlashkin V, Kreykenbohm V, Eskelinen EL, Wenzel D, Fayyazi A, et al. ((2003)) Deletion of the SNARE vti1b in mice results in the loss of a single SNARE partner, syntaxin 8. Mol Cell Biol 23:: 5198--5207.
    • (2003) Mol Cell Biol , vol.23 , pp. 5198-5207
    • Atlashkin, V.1    Kreykenbohm, V.2    Eskelinen, E.L.3    Wenzel, D.4    Fayyazi, A.5
  • 38
    • 70450224446 scopus 로고    scopus 로고
    • Multiple roles of the vesicular-SNARE TI-VAMP in post-Golgi and endosomal trafficking
    • Chaineau M, Danglot L, Galli T, ((2009)) Multiple roles of the vesicular-SNARE TI-VAMP in post-Golgi and endosomal trafficking. FEBS Lett 583:: 3817--3826.
    • (2009) FEBS Lett , vol.583 , pp. 3817-3826
    • Chaineau, M.1    Danglot, L.2    Galli, T.3
  • 39
    • 34547464792 scopus 로고    scopus 로고
    • Trans-SNARE complex assembly and yeast vacuole membrane fusion
    • Collins KM, Wickner WT, ((2007)) Trans-SNARE complex assembly and yeast vacuole membrane fusion. Proc Natl Acad Sci U S A 104:: 8755--8760.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 8755-8760
    • Collins, K.M.1    Wickner, W.T.2
  • 40
    • 67651177960 scopus 로고    scopus 로고
    • Snapin associates with late endocytic compartments and interacts with late endosomal SNAREs
    • Lu L, Cai Q, Tian JH, Sheng ZH, ((2009)) Snapin associates with late endocytic compartments and interacts with late endosomal SNAREs. Biosci Rep 29:: 261--269.
    • (2009) Biosci Rep , vol.29 , pp. 261-269
    • Lu, L.1    Cai, Q.2    Tian, J.H.3    Sheng, Z.H.4
  • 43
    • 70349499329 scopus 로고    scopus 로고
    • Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion
    • Mima J, Wickner W, ((2009)) Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion. Proc Natl Acad Sci U S A 106:: 16191--16196.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16191-16196
    • Mima, J.1    Wickner, W.2
  • 44
    • 73949099816 scopus 로고    scopus 로고
    • Organelle docking: R-SNAREs are late
    • Verhage M, ((2009)) Organelle docking: R-SNAREs are late. Proc Natl Acad Sci U S A 106:: 19745--19746.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19745-19746
    • Verhage, M.1
  • 45
    • 78649821097 scopus 로고    scopus 로고
    • Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly
    • Xu H, Wickner W (2010) Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly. J Biol Chem.
    • (2010) J Biol Chem.
    • Xu, H.1    Wickner, W.2
  • 46
    • 78649649128 scopus 로고    scopus 로고
    • Class I and class III phosphoinositide 3-kinases are required for actin polymerization that propels phagosomes
    • Bohdanowicz M, Cosio G, Backer JM, Grinstein S, ((2010)) Class I and class III phosphoinositide 3-kinases are required for actin polymerization that propels phagosomes. J Cell Biol 191:: 999--1012.
    • (2010) J Cell Biol , vol.191 , pp. 999-1012
    • Bohdanowicz, M.1    Cosio, G.2    Backer, J.M.3    Grinstein, S.4
  • 47
    • 10344232033 scopus 로고    scopus 로고
    • The p85alpha subunit of phosphatidylinositol 3′-kinase binds to and stimulates the GTPase activity of Rab proteins
    • Chamberlain MD, Berry TR, Pastor MC, Anderson DH, ((2004)) The p85alpha subunit of phosphatidylinositol 3′-kinase binds to and stimulates the GTPase activity of Rab proteins. J Biol Chem 279:: 48607--48614.
    • (2004) J Biol Chem , vol.279 , pp. 48607-48614
    • Chamberlain, M.D.1    Berry, T.R.2    Pastor, M.C.3    Anderson, D.H.4
  • 48
    • 0034947026 scopus 로고    scopus 로고
    • Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
    • Cheever ML, Sato TK, de Beer T, Kutateladze TG, Emr SD, et al. ((2001)) Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nat Cell Biol 3:: 613--618.
    • (2001) Nat Cell Biol , vol.3 , pp. 613-618
    • Cheever, M.L.1    Sato, T.K.2    de Beer, T.3    Kutateladze, T.G.4    Emr, S.D.5
  • 50
    • 0032877340 scopus 로고    scopus 로고
    • Regulation of early-endosome dynamics by phosphatidylinositol 3-phosphate binding proteins
    • Clague MJ, Jones AT, Mills IG, Walker DM, Urbe S, ((1999)) Regulation of early-endosome dynamics by phosphatidylinositol 3-phosphate binding proteins. Biochem Soc Trans 27:: 662--666.
    • (1999) Biochem Soc Trans , vol.27 , pp. 662-666
    • Clague, M.J.1    Jones, A.T.2    Mills, I.G.3    Walker, D.M.4    Urbe, S.5
  • 51
    • 67349163727 scopus 로고    scopus 로고
    • Phosphoinositides and the endocytic pathway
    • Clague MJ, Urbe S, de Lartigue J, ((2009)) Phosphoinositides and the endocytic pathway. Exp Cell Res 315:: 1627--1631.
    • (2009) Exp Cell Res , vol.315 , pp. 1627-1631
    • Clague, M.J.1    Urbe, S.2    de Lartigue, J.3
  • 52
    • 72049110528 scopus 로고    scopus 로고
    • Rethinking phosphatidylinositol 3-monophosphate
    • Falasca M, Maffucci T, ((2009)) Rethinking phosphatidylinositol 3-monophosphate. Biochim Biophys Acta 1793:: 1795--1803.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1795-1803
    • Falasca, M.1    Maffucci, T.2
  • 53
    • 0035817635 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinase and Rab5 effectors in phagosomal biogenesis and mycobacterial phagosome maturation arrest
    • Fratti RA, Backer JM, Gruenberg J, Corvera S, Deretic V, ((2001)) Role of phosphatidylinositol 3-kinase and Rab5 effectors in phagosomal biogenesis and mycobacterial phagosome maturation arrest. J Cell Biol 154:: 631--644.
    • (2001) J Cell Biol , vol.154 , pp. 631-644
    • Fratti, R.A.1    Backer, J.M.2    Gruenberg, J.3    Corvera, S.4    Deretic, V.5
  • 54
    • 2942605971 scopus 로고    scopus 로고
    • Quantitative analysis of phagolysosome fusion in intact cells: inhibition by mycobacterial lipoarabinomannan and rescue by an 1alpha,25-dihydroxyvitamin D3-phosphoinositide 3-kinase pathway
    • Hmama Z, Sendide K, Talal A, Garcia R, Dobos K, et al. ((2004)) Quantitative analysis of phagolysosome fusion in intact cells: inhibition by mycobacterial lipoarabinomannan and rescue by an 1alpha,25-dihydroxyvitamin D3-phosphoinositide 3-kinase pathway. J Cell Sci 117:: 2131--2140.
    • (2004) J Cell Sci , vol.117 , pp. 2131-2140
    • Hmama, Z.1    Sendide, K.2    Talal, A.3    Garcia, R.4    Dobos, K.5
  • 55
    • 20944450964 scopus 로고    scopus 로고
    • The type Ialpha inositol polyphosphate 4-phosphatase generates and terminates phosphoinositide 3-kinase signals on endosomes and the plasma membrane
    • Ivetac I, Munday AD, Kisseleva MV, Zhang XM, Luff S, et al. ((2005)) The type Ialpha inositol polyphosphate 4-phosphatase generates and terminates phosphoinositide 3-kinase signals on endosomes and the plasma membrane. Mol Biol Cell 16:: 2218--2233.
    • (2005) Mol Biol Cell , vol.16 , pp. 2218-2233
    • Ivetac, I.1    Munday, A.D.2    Kisseleva, M.V.3    Zhang, X.M.4    Luff, S.5
  • 56
    • 33646789810 scopus 로고    scopus 로고
    • Gene silencing reveals a specific function of hVps34 phosphatidylinositol 3-kinase in late versus early endosomes
    • Johnson EE, Overmeyer JH, Gunning WT, Maltese WA, ((2006)) Gene silencing reveals a specific function of hVps34 phosphatidylinositol 3-kinase in late versus early endosomes. J Cell Sci 119:: 1219--1232.
    • (2006) J Cell Sci , vol.119 , pp. 1219-1232
    • Johnson, E.E.1    Overmeyer, J.H.2    Gunning, W.T.3    Maltese, W.A.4
  • 57
    • 66349123530 scopus 로고    scopus 로고
    • Eps15 homology domain 1-associated tubules contain phosphatidylinositol-4-phosphate and phosphatidylinositol-(4,5)-bisphosphate and are required for efficient recycling
    • Jovic M, Kieken F, Naslavsky N, Sorgen PL, Caplan S, ((2009)) Eps15 homology domain 1-associated tubules contain phosphatidylinositol-4-phosphate and phosphatidylinositol-(4,5)-bisphosphate and are required for efficient recycling. Mol Biol Cell 20:: 2731--2743.
    • (2009) Mol Biol Cell , vol.20 , pp. 2731-2743
    • Jovic, M.1    Kieken, F.2    Naslavsky, N.3    Sorgen, P.L.4    Caplan, S.5
  • 58
    • 0038758990 scopus 로고    scopus 로고
    • PtdIns(3,5)P2 is required for delivery of endocytic cargo into the multivesicular body
    • Shaw JD, Hama H, Sohrabi F, DeWald DB, Wendland B, ((2003)) PtdIns(3,5)P2 is required for delivery of endocytic cargo into the multivesicular body. Traffic 4:: 479--490.
    • (2003) Traffic , vol.4 , pp. 479-490
    • Shaw, J.D.1    Hama, H.2    Sohrabi, F.3    DeWald, D.B.4    Wendland, B.5
  • 59
    • 23944437499 scopus 로고    scopus 로고
    • An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway
    • Shin HW, Hayashi M, Christoforidis S, Lacas-Gervais S, Hoepfner S, et al. ((2005)) An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway. J Cell Biol 170:: 607--618.
    • (2005) J Cell Biol , vol.170 , pp. 607-618
    • Shin, H.W.1    Hayashi, M.2    Christoforidis, S.3    Lacas-Gervais, S.4    Hoepfner, S.5
  • 60
    • 0032581654 scopus 로고    scopus 로고
    • EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
    • Simonsen A, Lippe R, Christoforidis S, Gaullier JM, Brech A, et al. ((1998)) EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 394:: 494--498.
    • (1998) Nature , vol.394 , pp. 494-498
    • Simonsen, A.1    Lippe, R.2    Christoforidis, S.3    Gaullier, J.M.4    Brech, A.5
  • 61
    • 53849103269 scopus 로고    scopus 로고
    • Mycobacterial phenolic glycolipid inhibits phagosome maturation and subverts the pro-inflammatory cytokine response
    • Robinson N, Kolter T, Wolke M, Rybniker J, Hartmann P, et al. ((2008)) Mycobacterial phenolic glycolipid inhibits phagosome maturation and subverts the pro-inflammatory cytokine response. Traffic 9:: 1936--1947.
    • (2008) Traffic , vol.9 , pp. 1936-1947
    • Robinson, N.1    Kolter, T.2    Wolke, M.3    Rybniker, J.4    Hartmann, P.5
  • 62
    • 77952592198 scopus 로고    scopus 로고
    • Lipopolysaccharide of Legionella pneumophila shed in a liquid culture as a nonvesicular fraction arrests phagosome maturation in amoeba and monocytic host cells
    • Seeger EM, Thuma M, Fernandez-Moreira E, Jacobs E, Schmitz M, et al. ((2010)) Lipopolysaccharide of Legionella pneumophila shed in a liquid culture as a nonvesicular fraction arrests phagosome maturation in amoeba and monocytic host cells. FEMS Microbiol Lett 307:: 113--119.
    • (2010) FEMS Microbiol Lett , vol.307 , pp. 113-119
    • Seeger, E.M.1    Thuma, M.2    Fernandez-Moreira, E.3    Jacobs, E.4    Schmitz, M.5
  • 63
    • 0032537835 scopus 로고    scopus 로고
    • Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes
    • Mills IG, Jones AT, Clague MJ, ((1998)) Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes. Curr Biol 8:: 881--884.
    • (1998) Curr Biol , vol.8 , pp. 881-884
    • Mills, I.G.1    Jones, A.T.2    Clague, M.J.3
  • 64
    • 0034988109 scopus 로고    scopus 로고
    • Relationships between EEA1 binding partners and their role in endosome fusion
    • Mills IG, Urbe S, Clague MJ, ((2001)) Relationships between EEA1 binding partners and their role in endosome fusion. J Cell Sci 114:: 1959--1965.
    • (2001) J Cell Sci , vol.114 , pp. 1959-1965
    • Mills, I.G.1    Urbe, S.2    Clague, M.J.3
  • 65
    • 0030873250 scopus 로고    scopus 로고
    • Identification of an early endosomal protein regulated by phosphatidylinositol 3-kinase
    • Patki V, Virbasius J, Lane WS, Toh BH, Shpetner HS, et al. ((1997)) Identification of an early endosomal protein regulated by phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A 94:: 7326--7330.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 7326-7330
    • Patki, V.1    Virbasius, J.2    Lane, W.S.3    Toh, B.H.4    Shpetner, H.S.5
  • 66
    • 27244457353 scopus 로고    scopus 로고
    • Kinetics of phosphatidylinositol-3-phosphate acquisition differ between IgG bead-containing phagosomes and Mycobacterium tuberculosis-containing phagosomes
    • Purdy GE, Owens RM, Bennett L, Russell DG, Butcher BA, ((2005)) Kinetics of phosphatidylinositol-3-phosphate acquisition differ between IgG bead-containing phagosomes and Mycobacterium tuberculosis-containing phagosomes. Cell Microbiol 7:: 1627--1634.
    • (2005) Cell Microbiol , vol.7 , pp. 1627-1634
    • Purdy, G.E.1    Owens, R.M.2    Bennett, L.3    Russell, D.G.4    Butcher, B.A.5
  • 67
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis S, McBride HM, Burgoyne RD, Zerial M, ((1999)) The Rab5 effector EEA1 is a core component of endosome docking. Nature 397:: 621--625.
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 68
    • 0038784437 scopus 로고    scopus 로고
    • Essential role of Ca2+/calmodulin in Early Endosome Antigen-1 localization
    • Lawe DC, Sitouah N, Hayes S, Chawla A, Virbasius JV, et al. ((2003)) Essential role of Ca2+/calmodulin in Early Endosome Antigen-1 localization. Mol Biol Cell 14:: 2935--2945.
    • (2003) Mol Biol Cell , vol.14 , pp. 2935-2945
    • Lawe, D.C.1    Sitouah, N.2    Hayes, S.3    Chawla, A.4    Virbasius, J.V.5
  • 69
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride HM, Rybin V, Murphy C, Giner A, Teasdale R, et al. ((1999)) Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 98:: 377--386.
    • (1999) Cell , vol.98 , pp. 377-386
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5
  • 70
    • 0032879685 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 interacts directly with syntaxin-6
    • Simonsen A, Gaullier JM, D'Arrigo A, Stenmark H, ((1999)) The Rab5 effector EEA1 interacts directly with syntaxin-6. J Biol Chem 274:: 28857--28860.
    • (1999) J Biol Chem , vol.274 , pp. 28857-28860
    • Simonsen, A.1    Gaullier, J.M.2    D'Arrigo, A.3    Stenmark, H.4
  • 71
    • 0032563130 scopus 로고    scopus 로고
    • Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/gamma-adaptin vesicles at the trans-Golgi network
    • Karlsson K, Carlsson SR, ((1998)) Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/gamma-adaptin vesicles at the trans-Golgi network. J Biol Chem 273:: 18966--18973.
    • (1998) J Biol Chem , vol.273 , pp. 18966-18973
    • Karlsson, K.1    Carlsson, S.R.2
  • 72
    • 33846471307 scopus 로고    scopus 로고
    • LAMP proteins are required for fusion of lysosomes with phagosomes
    • Huynh KK, Eskelinen EL, Scott CC, Malevanets A, Saftig P, et al. ((2007)) LAMP proteins are required for fusion of lysosomes with phagosomes. EMBO J 26:: 313--324.
    • (2007) EMBO J , vol.26 , pp. 313-324
    • Huynh, K.K.1    Eskelinen, E.L.2    Scott, C.C.3    Malevanets, A.4    Saftig, P.5
  • 73
    • 58149092914 scopus 로고    scopus 로고
    • Cholesterol accumulation by macrophages impairs phagosome maturation
    • Huynh KK, Gershenzon E, Grinstein S, ((2008)) Cholesterol accumulation by macrophages impairs phagosome maturation. J Biol Chem 283:: 35745--35755.
    • (2008) J Biol Chem , vol.283 , pp. 35745-35755
    • Huynh, K.K.1    Gershenzon, E.2    Grinstein, S.3
  • 74
    • 0027330919 scopus 로고
    • Targeted disruption of the M(r) 46,000 mannose 6-phosphate receptor gene in mice results in misrouting of lysosomal proteins
    • Koster A, Saftig P, Matzner U, von Figura K, Peters C, et al. ((1993)) Targeted disruption of the M(r) 46,000 mannose 6-phosphate receptor gene in mice results in misrouting of lysosomal proteins. EMBO J 12:: 5219--5223.
    • (1993) EMBO J , vol.12 , pp. 5219-5223
    • Koster, A.1    Saftig, P.2    Matzner, U.3    von Figura, K.4    Peters, C.5
  • 75
    • 0027932822 scopus 로고
    • Differential sorting of lysosomal enzymes in mannose 6-phosphate receptor-deficient fibroblasts
    • Ludwig T, Munier-Lehmann H, Bauer U, Hollinshead M, Ovitt C, et al. ((1994)) Differential sorting of lysosomal enzymes in mannose 6-phosphate receptor-deficient fibroblasts. EMBO J 13:: 3430--3437.
    • (1994) EMBO J , vol.13 , pp. 3430-3437
    • Ludwig, T.1    Munier-Lehmann, H.2    Bauer, U.3    Hollinshead, M.4    Ovitt, C.5
  • 76
    • 0022555844 scopus 로고
    • Lysosomal enzymes and their receptors
    • von Figura K, Hasilik A, ((1986)) Lysosomal enzymes and their receptors. Annu Rev Biochem 55:: 167--193.
    • (1986) Annu Rev Biochem , vol.55 , pp. 167-193
    • von Figura, K.1    Hasilik, A.2
  • 78
    • 0026777811 scopus 로고
    • The cystic fibrosis transmembrane regulator is present and functional in endosomes. Role as a determinant of endosomal pH
    • Lukacs GL, Chang XB, Kartner N, Rotstein OD, Riordan JR, et al. ((1992)) The cystic fibrosis transmembrane regulator is present and functional in endosomes. Role as a determinant of endosomal pH. J Biol Chem 267:: 14568--14572.
    • (1992) J Biol Chem , vol.267 , pp. 14568-14572
    • Lukacs, G.L.1    Chang, X.B.2    Kartner, N.3    Rotstein, O.D.4    Riordan, J.R.5
  • 79
    • 0033771836 scopus 로고    scopus 로고
    • Altered membrane trafficking in activated bone marrow-derived macrophages
    • Tsang AW, Oestergaard K, Myers JT, Swanson JA, ((2000)) Altered membrane trafficking in activated bone marrow-derived macrophages. J Leukoc Biol 68:: 487--494.
    • (2000) J Leukoc Biol , vol.68 , pp. 487-494
    • Tsang, A.W.1    Oestergaard, K.2    Myers, J.T.3    Swanson, J.A.4
  • 80
    • 33947107878 scopus 로고    scopus 로고
    • Macrophage activation downregulates the degradative capacity of the phagosome
    • Yates RM, Hermetter A, Taylor GA, Russell DG, ((2007)) Macrophage activation downregulates the degradative capacity of the phagosome. Traffic 8:: 241--250.
    • (2007) Traffic , vol.8 , pp. 241-250
    • Yates, R.M.1    Hermetter, A.2    Taylor, G.A.3    Russell, D.G.4
  • 81
    • 0032751602 scopus 로고    scopus 로고
    • Direct delivery of procathepsin D to phagosomes: implications for phagosome biogenesis and parasitism by Mycobacterium
    • Ullrich HJ, Beatty WL, Russell DG, ((1999)) Direct delivery of procathepsin D to phagosomes: implications for phagosome biogenesis and parasitism by Mycobacterium. Eur J Cell Biol 78:: 739--748.
    • (1999) Eur J Cell Biol , vol.78 , pp. 739-748
    • Ullrich, H.J.1    Beatty, W.L.2    Russell, D.G.3
  • 82
    • 0037053292 scopus 로고    scopus 로고
    • Cellubrevin alterations and Mycobacterium tuberculosis phagosome maturation arrest
    • Fratti RA, Chua J, Deretic V, ((2002)) Cellubrevin alterations and Mycobacterium tuberculosis phagosome maturation arrest. J Biol Chem 277:: 17320--17326.
    • (2002) J Biol Chem , vol.277 , pp. 17320-17326
    • Fratti, R.A.1    Chua, J.2    Deretic, V.3
  • 83
    • 0037627408 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis glycosylated phosphatidylinositol causes phagosome maturation arrest
    • Fratti RA, Chua J, Vergne I, Deretic V, ((2003)) Mycobacterium tuberculosis glycosylated phosphatidylinositol causes phagosome maturation arrest. Proc Natl Acad Sci U S A 100:: 5437--5442.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5437-5442
    • Fratti, R.A.1    Chua, J.2    Vergne, I.3    Deretic, V.4
  • 84
    • 0032498795 scopus 로고    scopus 로고
    • Mutant Rab7 causes the accumulation of cathepsin D and cation-independent mannose 6-phosphate receptor in an early endocytic compartment
    • Press B, Feng Y, Hoflack B, Wandinger-Ness A, ((1998)) Mutant Rab7 causes the accumulation of cathepsin D and cation-independent mannose 6-phosphate receptor in an early endocytic compartment. J Cell Biol 140:: 1075--1089.
    • (1998) J Cell Biol , vol.140 , pp. 1075-1089
    • Press, B.1    Feng, Y.2    Hoflack, B.3    Wandinger-Ness, A.4
  • 86
    • 79952807443 scopus 로고    scopus 로고
    • Rab GTPases Regulating Phagosome Maturation are Differentially Recruited to Mycobacterial Phagosomes
    • Seto S, Tsujimura K, Koide Y (2011) Rab GTPases Regulating Phagosome Maturation are Differentially Recruited to Mycobacterial Phagosomes. Traffic.
    • (2011) Traffic
    • Seto, S.1    Tsujimura, K.2    Koide, Y.3
  • 87
    • 67949091245 scopus 로고    scopus 로고
    • Vps-C complexes: gatekeepers of endolysosomal traffic
    • Nickerson DP, Brett CL, Merz AJ, ((2009)) Vps-C complexes: gatekeepers of endolysosomal traffic. Curr Opin Cell Biol 21:: 543--551.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 543-551
    • Nickerson, D.P.1    Brett, C.L.2    Merz, A.J.3
  • 88
    • 0034662876 scopus 로고    scopus 로고
    • A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
    • Seals DF, Eitzen G, Margolis N, Wickner WT, Price A, ((2000)) A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc Natl Acad Sci U S A 97:: 9402--9407.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9402-9407
    • Seals, D.F.1    Eitzen, G.2    Margolis, N.3    Wickner, W.T.4    Price, A.5
  • 89
    • 52249085200 scopus 로고    scopus 로고
    • Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase
    • Brett CL, Plemel RL, Lobinger BT, Vignali M, Fields S, et al. ((2008)) Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase. J Cell Biol 182:: 1141--1151.
    • (2008) J Cell Biol , vol.182 , pp. 1141-1151
    • Brett, C.L.1    Plemel, R.L.2    Lobinger, B.T.3    Vignali, M.4    Fields, S.5
  • 90
    • 65249126973 scopus 로고    scopus 로고
    • Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites
    • Cabrera M, Ostrowicz CW, Mari M, LaGrassa TJ, Reggiori F, et al. ((2009)) Vps41 phosphorylation and the Rab Ypt7 control the targeting of the HOPS complex to endosome-vacuole fusion sites. Mol Biol Cell 20:: 1937--1948.
    • (2009) Mol Biol Cell , vol.20 , pp. 1937-1948
    • Cabrera, M.1    Ostrowicz, C.W.2    Mari, M.3    LaGrassa, T.J.4    Reggiori, F.5
  • 91
    • 13444251066 scopus 로고    scopus 로고
    • The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex
    • LaGrassa TJ, Ungermann C, ((2005)) The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex. J Cell Biol 168:: 401--414.
    • (2005) J Cell Biol , vol.168 , pp. 401-414
    • LaGrassa, T.J.1    Ungermann, C.2
  • 92
    • 65649126758 scopus 로고    scopus 로고
    • Detection of activated Rab7 GTPase with an immobilized RILP probe
    • Sun J, Deghmane AE, Bucci C, Hmama Z, ((2009)) Detection of activated Rab7 GTPase with an immobilized RILP probe. Methods Mol Biol 531:: 57--69.
    • (2009) Methods Mol Biol , vol.531 , pp. 57-69
    • Sun, J.1    Deghmane, A.E.2    Bucci, C.3    Hmama, Z.4


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