메뉴 건너뛰기




Volumn 10, Issue 7, 2014, Pages

The Machinery at Endoplasmic Reticulum-Plasma Membrane Contact Sites Contributes to Spatial Regulation of Multiple Legionella Effector Proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; RAB PROTEIN; SIDM PROTEIN, LEGIONELLA PNEUMOPHILA; VIRULENCE FACTOR;

EID: 84905372666     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004222     Document Type: Article
Times cited : (58)

References (77)
  • 1
    • 0035691622 scopus 로고    scopus 로고
    • How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane
    • Tilney LG, Harb OS, Connelly PS, Robinson CG, Roy CR, (2001) How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane. J Cell Sci 114: 4637-4650.
    • (2001) J Cell Sci , vol.114 , pp. 4637-4650
    • Tilney, L.G.1    Harb, O.S.2    Connelly, P.S.3    Robinson, C.G.4    Roy, C.R.5
  • 2
    • 2142758690 scopus 로고    scopus 로고
    • Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system
    • Derre I, Isberg RR, (2004) Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system. Infect Immun 72: 3048-3053.
    • (2004) Infect Immun , vol.72 , pp. 3048-3053
    • Derre, I.1    Isberg, R.R.2
  • 3
    • 0036903907 scopus 로고    scopus 로고
    • Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites
    • Kagan JC, Roy CR, (2002) Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites. Nat Cell Biol 4: 945-954.
    • (2002) Nat Cell Biol , vol.4 , pp. 945-954
    • Kagan, J.C.1    Roy, C.R.2
  • 4
    • 2442537071 scopus 로고    scopus 로고
    • Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle
    • Kagan JC, Stein MP, Pypaert M, Roy CR, (2004) Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle. J Exp Med 199: 1201-1211.
    • (2004) J Exp Med , vol.199 , pp. 1201-1211
    • Kagan, J.C.1    Stein, M.P.2    Pypaert, M.3    Roy, C.R.4
  • 5
    • 77953142013 scopus 로고    scopus 로고
    • Legionella pneumophila promotes functional interactions between plasma membrane syntaxins and Sec22b
    • Arasaki K, Roy CR, (2010) Legionella pneumophila promotes functional interactions between plasma membrane syntaxins and Sec22b. Traffic 11: 587-600.
    • (2010) Traffic , vol.11 , pp. 587-600
    • Arasaki, K.1    Roy, C.R.2
  • 6
    • 84899895138 scopus 로고    scopus 로고
    • The SNARE Sec22b has a non-fusogenic function in plasma membrane expansion
    • Petkovic M, Jemaiel A, Daste F, Specht CG, Izeddin I, et al. (2014) The SNARE Sec22b has a non-fusogenic function in plasma membrane expansion. Nat Cell Biol 16 (5): 434-44.
    • (2014) Nat Cell Biol , vol.16 , Issue.5 , pp. 434-444
    • Petkovic, M.1    Jemaiel, A.2    Daste, F.3    Specht, C.G.4    Izeddin, I.5
  • 7
    • 84889234826 scopus 로고    scopus 로고
    • Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila
    • Machner MP, Isberg RR, (2006) Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Dev Cell 11: 47-56.
    • (2006) Dev Cell , vol.11 , pp. 47-56
    • Machner, M.P.1    Isberg, R.R.2
  • 8
    • 33748172869 scopus 로고    scopus 로고
    • The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor
    • Murata T, Delprato A, Ingmundson A, Toomre DK, Lambright DG, et al. (2006) The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. Nat Cell Biol 8: 971-977.
    • (2006) Nat Cell Biol , vol.8 , pp. 971-977
    • Murata, T.1    Delprato, A.2    Ingmundson, A.3    Toomre, D.K.4    Lambright, D.G.5
  • 9
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H, (2009) Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 10: 513-525.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 10
    • 36249027095 scopus 로고    scopus 로고
    • Legionella pneumophila proteins that regulate Rab1 membrane cycling
    • Ingmundson A, Delprato A, Lambright DG, Roy CR, (2007) Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450: 365-369.
    • (2007) Nature , vol.450 , pp. 365-369
    • Ingmundson, A.1    Delprato, A.2    Lambright, D.G.3    Roy, C.R.4
  • 11
    • 84889234796 scopus 로고    scopus 로고
    • A bifunctional bacterial protein links GDI displacement to Rab1 activation
    • Machner MP, Isberg RR, (2007) A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 318: 974-977.
    • (2007) Science , vol.318 , pp. 974-977
    • Machner, M.P.1    Isberg, R.R.2
  • 12
    • 72449132474 scopus 로고    scopus 로고
    • RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity
    • Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A, (2009) RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Mol Cell 36: 1060-1072.
    • (2009) Mol Cell , vol.36 , pp. 1060-1072
    • Schoebel, S.1    Oesterlin, L.K.2    Blankenfeldt, W.3    Goody, R.S.4    Itzen, A.5
  • 13
    • 84855988874 scopus 로고    scopus 로고
    • The Legionella pneumophila Effector DrrA Is Sufficient to Stimulate SNARE-Dependent Membrane Fusion
    • Arasaki K, Toomre DK, Roy CR, (2012) The Legionella pneumophila Effector DrrA Is Sufficient to Stimulate SNARE-Dependent Membrane Fusion. Cell Host Microbe 11: 46-57.
    • (2012) Cell Host Microbe , vol.11 , pp. 46-57
    • Arasaki, K.1    Toomre, D.K.2    Roy, C.R.3
  • 14
    • 79960699136 scopus 로고    scopus 로고
    • De-AMPylation of the Small GTPase Rab1 by the Pathogen Legionella pneumophila
    • Neunuebel MR, Chen Y, Gaspar AH, Backlund PS Jr, Yergey A, et al. (2011) De-AMPylation of the Small GTPase Rab1 by the Pathogen Legionella pneumophila. Science 333 (6041): 453-6.
    • (2011) Science , vol.333 , Issue.6041 , pp. 453-456
    • Neunuebel, M.R.1    Chen, Y.2    Gaspar, A.H.3    Backlund Jr., P.S.4    Yergey, A.5
  • 15
    • 33645543776 scopus 로고    scopus 로고
    • Attachment and fusion of endoplasmic reticulum with vacuoles containing Legionella pneumophila
    • Robinson CG, Roy CR, (2006) Attachment and fusion of endoplasmic reticulum with vacuoles containing Legionella pneumophila. Cell Microbiol 8: 793-805.
    • (2006) Cell Microbiol , vol.8 , pp. 793-805
    • Robinson, C.G.1    Roy, C.R.2
  • 16
    • 80052399642 scopus 로고    scopus 로고
    • Modulation of Rab GTPase function by a protein phosphocholine transferase
    • Mukherjee S, Liu X, Arasaki K, McDonough J, Galan JE, et al. (2011) Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 477: 103-106.
    • (2011) Nature , vol.477 , pp. 103-106
    • Mukherjee, S.1    Liu, X.2    Arasaki, K.3    McDonough, J.4    Galan, J.E.5
  • 17
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • Muller MP, Peters H, Blumer J, Blankenfeldt W, Goody RS, et al. (2010) The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329: 946-949.
    • (2010) Science , vol.329 , pp. 946-949
    • Muller, M.P.1    Peters, H.2    Blumer, J.3    Blankenfeldt, W.4    Goody, R.S.5
  • 18
    • 84863399784 scopus 로고    scopus 로고
    • Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins
    • Goody PR, Heller K, Oesterlin LK, Muller MP, Itzen A, et al. (2012) Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. Embo J 31: 1774-1784.
    • (2012) Embo J , vol.31 , pp. 1774-1784
    • Goody, P.R.1    Heller, K.2    Oesterlin, L.K.3    Muller, M.P.4    Itzen, A.5
  • 19
    • 84859564863 scopus 로고    scopus 로고
    • Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor
    • Oesterlin LK, Goody RS, Itzen A, (2012) Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor. Proc Natl Acad Sci U S A 109: 5621-5626.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 5621-5626
    • Oesterlin, L.K.1    Goody, R.S.2    Itzen, A.3
  • 20
    • 80052271972 scopus 로고    scopus 로고
    • Identification and modelling of a PPM protein phosphatase fold in the Legionella pneumophila deAMPylase SidD
    • Rigden DJ, (2011) Identification and modelling of a PPM protein phosphatase fold in the Legionella pneumophila deAMPylase SidD. FEBS Lett 585: 2749-2754.
    • (2011) FEBS Lett , vol.585 , pp. 2749-2754
    • Rigden, D.J.1
  • 21
    • 79960929331 scopus 로고    scopus 로고
    • Legionella pneumophila SidD is a deAMPylase that modifies Rab1
    • Tan Y, Luo ZQ, (2011) Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature 475: 506-509.
    • (2011) Nature , vol.475 , pp. 506-509
    • Tan, Y.1    Luo, Z.Q.2
  • 22
    • 84855504174 scopus 로고    scopus 로고
    • Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination
    • Tan Y, Arnold RJ, Luo ZQ, (2011) Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc Natl Acad Sci U S A 108: 21212-21217.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 21212-21217
    • Tan, Y.1    Arnold, R.J.2    Luo, Z.Q.3
  • 23
    • 64149084796 scopus 로고    scopus 로고
    • Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila
    • Brombacher E, Urwyler S, Ragaz C, Weber SS, Kami K, et al. (2009) Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila. J Biol Chem 284: 4846-4856.
    • (2009) J Biol Chem , vol.284 , pp. 4846-4856
    • Brombacher, E.1    Urwyler, S.2    Ragaz, C.3    Weber, S.S.4    Kami, K.5
  • 24
    • 77955057137 scopus 로고    scopus 로고
    • High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA
    • Schoebel S, Blankenfeldt W, Goody RS, Itzen A, (2010) High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. EMBO Rep 11: 598-604.
    • (2010) EMBO Rep , vol.11 , pp. 598-604
    • Schoebel, S.1    Blankenfeldt, W.2    Goody, R.S.3    Itzen, A.4
  • 25
    • 77949498580 scopus 로고    scopus 로고
    • Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA
    • Zhu Y, Hu L, Zhou Y, Yao Q, Liu L, et al. (2010) Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proc Natl Acad Sci U S A 107: 4699-4704.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4699-4704
    • Zhu, Y.1    Hu, L.2    Zhou, Y.3    Yao, Q.4    Liu, L.5
  • 26
    • 84901650366 scopus 로고    scopus 로고
    • A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi
    • Hammond GR, Machner MP, Balla T, (2014) A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi. J Cell Biol 205: 113-126.
    • (2014) J Cell Biol , vol.205 , pp. 113-126
    • Hammond, G.R.1    Machner, M.P.2    Balla, T.3
  • 27
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G, De Camilli P, (2006) Phosphoinositides in cell regulation and membrane dynamics. Nature 443: 651-657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 28
    • 28444482087 scopus 로고    scopus 로고
    • Regulation of protein activities by phosphoinositide phosphates
    • Niggli V, (2005) Regulation of protein activities by phosphoinositide phosphates. Annu Rev Cell Dev Biol 21: 57-79.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 57-79
    • Niggli, V.1
  • 29
    • 53549122990 scopus 로고    scopus 로고
    • Function and dysfunction of the PI system in membrane trafficking
    • Vicinanza M, D'Angelo G, Di Campli A, De Matteis MA, (2008) Function and dysfunction of the PI system in membrane trafficking. Embo J 27: 2457-2470.
    • (2008) Embo J , vol.27 , pp. 2457-2470
    • Vicinanza, M.1    D'Angelo, G.2    Di Campli, A.3    De Matteis, M.A.4
  • 30
    • 52549091027 scopus 로고    scopus 로고
    • Phosphoinositides as regulators of membrane trafficking in health and disease
    • Vicinanza M, D'Angelo G, Di Campli A, De Matteis MA, (2008) Phosphoinositides as regulators of membrane trafficking in health and disease. Cell Mol Life Sci 65: 2833-2841.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2833-2841
    • Vicinanza, M.1    D'Angelo, G.2    Di Campli, A.3    De Matteis, M.A.4
  • 31
    • 1542569606 scopus 로고    scopus 로고
    • Membrane recognition and targeting by lipid-binding domains
    • DiNitto JP, Cronin TC, Lambright DG, (2003) Membrane recognition and targeting by lipid-binding domains. Sci STKE 2003: re16.
    • (2003) Sci STKE , vol.2003
    • DiNitto, J.P.1    Cronin, T.C.2    Lambright, D.G.3
  • 32
    • 7944228843 scopus 로고    scopus 로고
    • Subversion of phosphoinositide metabolism by intracellular bacterial pathogens
    • Pizarro-Cerda J, Cossart P, (2004) Subversion of phosphoinositide metabolism by intracellular bacterial pathogens. Nat Cell Biol 6: 1026-1033.
    • (2004) Nat Cell Biol , vol.6 , pp. 1026-1033
    • Pizarro-Cerda, J.1    Cossart, P.2
  • 33
    • 62449280568 scopus 로고    scopus 로고
    • Pathogen trafficking pathways and host phosphoinositide metabolism
    • Weber SS, Ragaz C, Hilbi H, (2009) Pathogen trafficking pathways and host phosphoinositide metabolism. Mol Microbiol 71: 1341-1352.
    • (2009) Mol Microbiol , vol.71 , pp. 1341-1352
    • Weber, S.S.1    Ragaz, C.2    Hilbi, H.3
  • 34
    • 33646915714 scopus 로고    scopus 로고
    • Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole
    • Weber SS, Ragaz C, Reus K, Nyfeler Y, Hilbi H, (2006) Legionella pneumophila exploits PI(4)P to anchor secreted effector proteins to the replicative vacuole. PLoS Pathog 2: e46.
    • (2006) PLoS Pathog , vol.2
    • Weber, S.S.1    Ragaz, C.2    Reus, K.3    Nyfeler, Y.4    Hilbi, H.5
  • 35
    • 55749101951 scopus 로고    scopus 로고
    • The Legionella pneumophila phosphatidylinositol-4 phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole
    • Ragaz C, Pietsch H, Urwyler S, Tiaden A, Weber SS, et al. (2008) The Legionella pneumophila phosphatidylinositol-4 phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole. Cellular Microbiology 10: 2416-2433.
    • (2008) Cellular Microbiology , vol.10 , pp. 2416-2433
    • Ragaz, C.1    Pietsch, H.2    Urwyler, S.3    Tiaden, A.4    Weber, S.S.5
  • 36
    • 84865303538 scopus 로고    scopus 로고
    • Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase
    • Hsu F, Zhu W, Brennan L, Tao L, Luo ZQ, et al. (2012) Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase. Proc Natl Acad Sci U S A 109: 13567-13572.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 13567-13572
    • Hsu, F.1    Zhu, W.2    Brennan, L.3    Tao, L.4    Luo, Z.Q.5
  • 37
    • 47649123929 scopus 로고    scopus 로고
    • The multiple roles of PtdIns(4)P - not just the precursor of PtdIns(4,5)P2
    • D'Angelo G, Vicinanza M, Di Campli A, De Matteis MA, (2008) The multiple roles of PtdIns(4)P - not just the precursor of PtdIns(4,5)P2. J Cell Sci 121: 1955-1963.
    • (2008) J Cell Sci , vol.121 , pp. 1955-1963
    • D'Angelo, G.1    Vicinanza, M.2    Di Campli, A.3    De Matteis, M.A.4
  • 38
    • 33745933535 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinases: old enzymes with emerging functions
    • Balla A, Balla T, (2006) Phosphatidylinositol 4-kinases: old enzymes with emerging functions. Trends Cell Biol 16: 351-361.
    • (2006) Trends Cell Biol , vol.16 , pp. 351-361
    • Balla, A.1    Balla, T.2
  • 39
    • 0029876888 scopus 로고    scopus 로고
    • Characterization of a soluble adrenal phosphatidylinositol 4-kinase reveals wortmannin sensitivity of type III phosphatidylinositol kinases
    • Downing GJ, Kim S, Nakanishi S, Catt KJ, Balla T, (1996) Characterization of a soluble adrenal phosphatidylinositol 4-kinase reveals wortmannin sensitivity of type III phosphatidylinositol kinases. Biochemistry 35: 3587-3594.
    • (1996) Biochemistry , vol.35 , pp. 3587-3594
    • Downing, G.J.1    Kim, S.2    Nakanishi, S.3    Catt, K.J.4    Balla, T.5
  • 40
    • 14844302797 scopus 로고    scopus 로고
    • A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: studies with the PH domains of the oxysterol binding protein and FAPP1
    • Balla A, Tuymetova G, Tsiomenko A, Varnai P, Balla T, (2005) A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: studies with the PH domains of the oxysterol binding protein and FAPP1. Mol Biol Cell 16: 1282-1295.
    • (2005) Mol Biol Cell , vol.16 , pp. 1282-1295
    • Balla, A.1    Tuymetova, G.2    Tsiomenko, A.3    Varnai, P.4    Balla, T.5
  • 41
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler S, Currie RA, Campbell DG, Deak M, Kular G, et al. (2000) Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem J 351: 19-31.
    • (2000) Biochem J , vol.351 , pp. 19-31
    • Dowler, S.1    Currie, R.A.2    Campbell, D.G.3    Deak, M.4    Kular, G.5
  • 42
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components
    • Levine TP, Munro S, (2002) Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and-independent components. Curr Biol 12: 695-704.
    • (2002) Curr Biol , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 43
    • 1642367563 scopus 로고    scopus 로고
    • Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains
    • Yu JW, Mendrola JM, Audhya A, Singh S, Keleti D, et al. (2004) Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains. Mol Cell 13: 677-688.
    • (2004) Mol Cell , vol.13 , pp. 677-688
    • Yu, J.W.1    Mendrola, J.M.2    Audhya, A.3    Singh, S.4    Keleti, D.5
  • 44
    • 0033258472 scopus 로고    scopus 로고
    • The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi
    • Walch-Solimena C, Novick P, (1999) The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi. Nat Cell Biol 1: 523-525.
    • (1999) Nat Cell Biol , vol.1 , pp. 523-525
    • Walch-Solimena, C.1    Novick, P.2
  • 45
    • 15444363818 scopus 로고    scopus 로고
    • Distinct Golgi populations of phosphatidylinositol 4-phosphate regulated by phosphatidylinositol 4-kinases
    • Weixel KM, Blumental-Perry A, Watkins SC, Aridor M, Weisz OA, (2005) Distinct Golgi populations of phosphatidylinositol 4-phosphate regulated by phosphatidylinositol 4-kinases. J Biol Chem 280: 10501-10508.
    • (2005) J Biol Chem , vol.280 , pp. 10501-10508
    • Weixel, K.M.1    Blumental-Perry, A.2    Watkins, S.C.3    Aridor, M.4    Weisz, O.A.5
  • 46
    • 0030989280 scopus 로고    scopus 로고
    • Subcellular locations of phosphatidylinositol 4-kinase isoforms
    • Wong K, Meyers dd R, Cantley LC, (1997) Subcellular locations of phosphatidylinositol 4-kinase isoforms. J Biol Chem 272: 13236-13241.
    • (1997) J Biol Chem , vol.272 , pp. 13236-13241
    • Wong, K.1    Meyers dd, R.2    Cantley, L.C.3
  • 47
    • 84864848873 scopus 로고    scopus 로고
    • PI4P and PI(4,5)P2 are essential but independent lipid determinants of membrane identity
    • Hammond GR, Fischer MJ, Anderson KE, Holdich J, Koteci A, et al. (2012) PI4P and PI(4,5)P2 are essential but independent lipid determinants of membrane identity. Science 337: 727-730.
    • (2012) Science , vol.337 , pp. 727-730
    • Hammond, G.R.1    Fischer, M.J.2    Anderson, K.E.3    Holdich, J.4    Koteci, A.5
  • 48
    • 85047686708 scopus 로고    scopus 로고
    • PtdIns4P synthesis by PI4KIIIα at the plasma membrane and its impact on plasma membrane identity
    • Nakatsu F, Baskin JM, Chung J, Tanner LB, Shui G, et al. (2012) PtdIns4P synthesis by PI4KIIIα at the plasma membrane and its impact on plasma membrane identity. The Journal of Cell Biology 199: 1003-1016.
    • (2012) The Journal of Cell Biology , vol.199 , pp. 1003-1016
    • Nakatsu, F.1    Baskin, J.M.2    Chung, J.3    Tanner, L.B.4    Shui, G.5
  • 49
    • 58249089034 scopus 로고    scopus 로고
    • Assembly of the PtdIns 4-kinase Stt4 complex at the plasma membrane requires Ypp1 and Efr3
    • Baird D, Stefan C, Audhya A, Weys S, Emr SD, (2008) Assembly of the PtdIns 4-kinase Stt4 complex at the plasma membrane requires Ypp1 and Efr3. J Cell Biol 183: 1061-1074.
    • (2008) J Cell Biol , vol.183 , pp. 1061-1074
    • Baird, D.1    Stefan, C.2    Audhya, A.3    Weys, S.4    Emr, S.D.5
  • 50
    • 33745755614 scopus 로고    scopus 로고
    • Inter-organelle membrane contact sites: through a glass, darkly
    • Levine T, Loewen C, (2006) Inter-organelle membrane contact sites: through a glass, darkly. Curr Opin Cell Biol 18: 371-378.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 371-378
    • Levine, T.1    Loewen, C.2
  • 51
    • 79551674131 scopus 로고    scopus 로고
    • Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites
    • Stefan CJ, Manford AG, Baird D, Yamada-Hanff J, Mao Y, et al. (2011) Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites. Cell 144: 389-401.
    • (2011) Cell , vol.144 , pp. 389-401
    • Stefan, C.J.1    Manford, A.G.2    Baird, D.3    Yamada-Hanff, J.4    Mao, Y.5
  • 52
    • 84896728433 scopus 로고    scopus 로고
    • Structural Basis for PI(4)P-Specific Membrane Recruitment of the Legionella pneumophila Effector DrrA/SidM
    • Del Campo CM, Mishra AK, Wang YH, Roy CR, Janmey PA, et al. (2014) Structural Basis for PI(4)P-Specific Membrane Recruitment of the Legionella pneumophila Effector DrrA/SidM. Structure 22 (3): 397-408.
    • (2014) Structure , vol.22 , Issue.3 , pp. 397-408
    • Del Campo, C.M.1    Mishra, A.K.2    Wang, Y.H.3    Roy, C.R.4    Janmey, P.A.5
  • 53
    • 2342556630 scopus 로고    scopus 로고
    • FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P
    • Godi A, Di Campli A, Konstantakopoulos A, Di Tullio G, Alessi DR, et al. (2004) FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat Cell Biol 6: 393-404.
    • (2004) Nat Cell Biol , vol.6 , pp. 393-404
    • Godi, A.1    Di Campli, A.2    Konstantakopoulos, A.3    Di Tullio, G.4    Alessi, D.R.5
  • 54
    • 0032547744 scopus 로고    scopus 로고
    • Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools
    • Varnai P, Balla T, (1998) Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools. J Cell Biol 143: 501-510.
    • (1998) J Cell Biol , vol.143 , pp. 501-510
    • Varnai, P.1    Balla, T.2
  • 55
    • 77951978964 scopus 로고    scopus 로고
    • Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function
    • Manford A, Xia T, Saxena AK, Stefan C, Hu F, et al. (2010) Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function. Embo J 29: 1489-1498.
    • (2010) Embo J , vol.29 , pp. 1489-1498
    • Manford, A.1    Xia, T.2    Saxena, A.K.3    Stefan, C.4    Hu, F.5
  • 56
    • 84874366009 scopus 로고    scopus 로고
    • RabGEFs are a major determinant for specific Rab membrane targeting
    • Blumer J, Rey J, Dehmelt L, Mazel T, Wu YW, et al. (2013) RabGEFs are a major determinant for specific Rab membrane targeting. J Cell Biol 200: 287-300.
    • (2013) J Cell Biol , vol.200 , pp. 287-300
    • Blumer, J.1    Rey, J.2    Dehmelt, L.3    Mazel, T.4    Wu, Y.W.5
  • 57
    • 84896691337 scopus 로고    scopus 로고
    • Interaction of Fapp1 with Arf1 and PI4P at a membrane surface: an example of coincidence detection
    • Liu Y, Kahn RA, Prestegard JH, (2014) Interaction of Fapp1 with Arf1 and PI4P at a membrane surface: an example of coincidence detection. Structure 22: 421-430.
    • (2014) Structure , vol.22 , pp. 421-430
    • Liu, Y.1    Kahn, R.A.2    Prestegard, J.H.3
  • 58
    • 0026037624 scopus 로고
    • A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins
    • Hancock JF, Cadwallader K, Paterson H, Marshall CJ, (1991) A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. Embo J 10: 4033-4039.
    • (1991) Embo J , vol.10 , pp. 4033-4039
    • Hancock, J.F.1    Cadwallader, K.2    Paterson, H.3    Marshall, C.J.4
  • 59
    • 59849128432 scopus 로고    scopus 로고
    • The inositol polyphosphate 5-phosphatase OCRL1 restricts intracellular growth of Legionella, localizes to the replicative vacuole and binds to the bacterial effector LpnE
    • Weber SS, Ragaz C, Hilbi H, (2009) The inositol polyphosphate 5-phosphatase OCRL1 restricts intracellular growth of Legionella, localizes to the replicative vacuole and binds to the bacterial effector LpnE. Cell Microbiol 11: 442-460.
    • (2009) Cell Microbiol , vol.11 , pp. 442-460
    • Weber, S.S.1    Ragaz, C.2    Hilbi, H.3
  • 60
    • 23044490771 scopus 로고    scopus 로고
    • Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network
    • Choudhury R, Diao A, Zhang F, Eisenberg E, Saint-Pol A, et al. (2005) Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network. Mol Biol Cell 16: 3467-3479.
    • (2005) Mol Biol Cell , vol.16 , pp. 3467-3479
    • Choudhury, R.1    Diao, A.2    Zhang, F.3    Eisenberg, E.4    Saint-Pol, A.5
  • 62
    • 34548210456 scopus 로고    scopus 로고
    • A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway
    • Erdmann KS, Mao Y, McCrea HJ, Zoncu R, Lee S, et al. (2007) A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway. Dev Cell 13: 377-390.
    • (2007) Dev Cell , vol.13 , pp. 377-390
    • Erdmann, K.S.1    Mao, Y.2    McCrea, H.J.3    Zoncu, R.4    Lee, S.5
  • 63
    • 4544273742 scopus 로고    scopus 로고
    • The inositol polyphosphate 5-phosphatase Ocrl associates with endosomes that are partially coated with clathrin
    • Ungewickell A, Ward ME, Ungewickell E, Majerus PW, (2004) The inositol polyphosphate 5-phosphatase Ocrl associates with endosomes that are partially coated with clathrin. Proc Natl Acad Sci U S A 101: 13501-13506.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13501-13506
    • Ungewickell, A.1    Ward, M.E.2    Ungewickell, E.3    Majerus, P.W.4
  • 64
    • 65649144746 scopus 로고    scopus 로고
    • Differential clathrin binding and subcellular localization of OCRL1 splice isoforms
    • Choudhury R, Noakes CJ, McKenzie E, Kox C, Lowe M, (2009) Differential clathrin binding and subcellular localization of OCRL1 splice isoforms. J Biol Chem 284: 9965-9973.
    • (2009) J Biol Chem , vol.284 , pp. 9965-9973
    • Choudhury, R.1    Noakes, C.J.2    McKenzie, E.3    Kox, C.4    Lowe, M.5
  • 65
    • 79955000748 scopus 로고    scopus 로고
    • A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1
    • Hou X, Hagemann N, Schoebel S, Blankenfeldt W, Goody RS, et al. (2011) A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1. Embo J 30: 1659-1670.
    • (2011) Embo J , vol.30 , pp. 1659-1670
    • Hou, X.1    Hagemann, N.2    Schoebel, S.3    Blankenfeldt, W.4    Goody, R.S.5
  • 66
    • 39449085866 scopus 로고    scopus 로고
    • Maintenance of hormone-sensitive phosphoinositide pools in the plasma membrane requires phosphatidylinositol 4-kinase IIIalpha
    • Balla A, Kim YJ, Varnai P, Szentpetery Z, Knight Z, et al. (2008) Maintenance of hormone-sensitive phosphoinositide pools in the plasma membrane requires phosphatidylinositol 4-kinase IIIalpha. Mol Biol Cell 19: 711-721.
    • (2008) Mol Biol Cell , vol.19 , pp. 711-721
    • Balla, A.1    Kim, Y.J.2    Varnai, P.3    Szentpetery, Z.4    Knight, Z.5
  • 67
    • 7244248722 scopus 로고    scopus 로고
    • Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p
    • Roy A, Levine TP, (2004) Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p. J Biol Chem 279: 44683-44689.
    • (2004) J Biol Chem , vol.279 , pp. 44683-44689
    • Roy, A.1    Levine, T.P.2
  • 68
    • 84879383820 scopus 로고    scopus 로고
    • PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins
    • Giordano F, Saheki Y, Idevall-Hagren O, Colombo SF, Pirruccello M, et al. (2013) PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins. Cell 153: 1494-1509.
    • (2013) Cell , vol.153 , pp. 1494-1509
    • Giordano, F.1    Saheki, Y.2    Idevall-Hagren, O.3    Colombo, S.F.4    Pirruccello, M.5
  • 69
    • 58349107899 scopus 로고    scopus 로고
    • Large-scale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways
    • Heidtman M, Chen EJ, Moy MY, Isberg RR, (2009) Large-scale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways. Cell Microbiol 11: 230-248.
    • (2009) Cell Microbiol , vol.11 , pp. 230-248
    • Heidtman, M.1    Chen, E.J.2    Moy, M.Y.3    Isberg, R.R.4
  • 70
    • 0031025290 scopus 로고    scopus 로고
    • Topology of Legionella pneumophila DotA: an inner membrane protein required for replication in macrophages
    • Roy CR, Isberg RR, (1997) Topology of Legionella pneumophila DotA: an inner membrane protein required for replication in macrophages. Infect Immun 65: 571-578.
    • (1997) Infect Immun , vol.65 , pp. 571-578
    • Roy, C.R.1    Isberg, R.R.2
  • 71
    • 0030994460 scopus 로고    scopus 로고
    • Analysis of the Legionella pneumophila fliI gene: intracellular growth of a defined mutant defective for flagellum biosynthesis
    • Merriam JJ, Mathur R, Maxfield-Boumil R, Isberg RR, (1997) Analysis of the Legionella pneumophila fliI gene: intracellular growth of a defined mutant defective for flagellum biosynthesis. Infect Immun 65: 2497-2501.
    • (1997) Infect Immun , vol.65 , pp. 2497-2501
    • Merriam, J.J.1    Mathur, R.2    Maxfield-Boumil, R.3    Isberg, R.R.4
  • 72
    • 34548406570 scopus 로고    scopus 로고
    • Restriction of Legionella pneumophila growth in macrophages requires the concerted action of cytokine and Naip5/Ipaf signalling pathways
    • Coers J, Vance RE, Fontana MF, Dietrich WF, (2007) Restriction of Legionella pneumophila growth in macrophages requires the concerted action of cytokine and Naip5/Ipaf signalling pathways. Cell Microbiol 9: 2344-2357.
    • (2007) Cell Microbiol , vol.9 , pp. 2344-2357
    • Coers, J.1    Vance, R.E.2    Fontana, M.F.3    Dietrich, W.F.4
  • 73
    • 32344443060 scopus 로고    scopus 로고
    • Analysis of Rab1 recruitment to vacuoles containing Legionella pneumophila
    • Kagan JC, Murata T, Roy CR, (2005) Analysis of Rab1 recruitment to vacuoles containing Legionella pneumophila. Meth Enzymol 403: 71-81.
    • (2005) Meth Enzymol , vol.403 , pp. 71-81
    • Kagan, J.C.1    Murata, T.2    Roy, C.R.3
  • 74
    • 78650718978 scopus 로고    scopus 로고
    • A method for generation of bone marrow-derived macrophages from cryopreserved mouse bone marrow cells
    • Marim FM, Silveira TN, Lima DS Jr, Zamboni DS, (2010) A method for generation of bone marrow-derived macrophages from cryopreserved mouse bone marrow cells. PLoS One 5: e15263.
    • (2010) PLoS One , vol.5
    • Marim, F.M.1    Silveira, T.N.2    Lima Jr., D.S.3    Zamboni, D.S.4
  • 75
    • 33645770203 scopus 로고    scopus 로고
    • The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection
    • Zamboni DS, Kobayashi KS, Kohlsdorf T, Ogura Y, Long EM, et al. (2006) The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection. Nature Immunology 7: 318-325.
    • (2006) Nature Immunology , vol.7 , pp. 318-325
    • Zamboni, D.S.1    Kobayashi, K.S.2    Kohlsdorf, T.3    Ogura, Y.4    Long, E.M.5
  • 76
    • 33645791082 scopus 로고    scopus 로고
    • Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity
    • Ren T, Zamboni DS, Roy CR, Dietrich WF, Vance RE, (2006) Flagellin-deficient Legionella mutants evade caspase-1- and Naip5-mediated macrophage immunity. PLoS Pathog 2: e18.
    • (2006) PLoS Pathog , vol.2
    • Ren, T.1    Zamboni, D.S.2    Roy, C.R.3    Dietrich, W.F.4    Vance, R.E.5
  • 77
    • 77955451732 scopus 로고    scopus 로고
    • The inositol 5-phosphatase SHIP2 regulates endocytic clathrin-coated pit dynamics
    • Nakatsu F, Perera RM, Lucast L, Zoncu R, Domin J, et al. (2010) The inositol 5-phosphatase SHIP2 regulates endocytic clathrin-coated pit dynamics. J Cell Biol 190: 307-315.
    • (2010) J Cell Biol , vol.190 , pp. 307-315
    • Nakatsu, F.1    Perera, R.M.2    Lucast, L.3    Zoncu, R.4    Domin, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.