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Volumn 22, Issue 13, 2013, Pages 2689-2704

Increased levels of phosphoinositides cause neurodegeneration in a Drosophila model of amyotrophic lateral sclerosis

Author keywords

[No Author keywords available]

Indexed keywords

ADDUCIN; PHOSPHATIDYLINOSITIDE; SAC1 PROTEIN; SPECTRIN; SPECTRIN BETA SUBUNIT; SYNAPTOBREVIN; UNCLASSIFIED DRUG;

EID: 84878906794     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddt118     Document Type: Article
Times cited : (52)

References (82)
  • 1
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: insights from genetics
    • Pasinelli, P. and Brown, R.H. (2006) Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci., 7, 710-723.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 4
    • 44649186815 scopus 로고    scopus 로고
    • The VAP protein family: from cellular functions to motor neuron disease
    • Lev, S., Ben Halevy, D., Peretti, D. and Dahan, N. (2008) The VAP protein family: from cellular functions to motor neuron disease. Trends Cell Biol., 18, 282-290.
    • (2008) Trends Cell Biol. , vol.18 , pp. 282-290
    • Lev, S.1    Ben Halevy, D.2    Peretti, D.3    Dahan, N.4
  • 5
    • 0037130456 scopus 로고    scopus 로고
    • Drosophila VAP-33A directs bouton formation at neuromuscular junctions in a dosage-dependent manner
    • Pennetta, G., Hiesinger, P.R., Fabian-Fine, R., Meinertzhagen, I.A. and Bellen, H.J. (2002) Drosophila VAP-33A directs bouton formation at neuromuscular junctions in a dosage-dependent manner. Neuron, 35, 291-306.
    • (2002) Neuron , vol.35 , pp. 291-306
    • Pennetta, G.1    Hiesinger, P.R.2    Fabian-Fine, R.3    Meinertzhagen, I.A.4    Bellen, H.J.5
  • 6
    • 37849053294 scopus 로고    scopus 로고
    • hVAPB, the causative gene of a heterogeneous group of motor neuron diseases in humans, is functionally interchangeable with its Drosophila homologue DVAP-33A at the neuromuscular junction
    • Chai, A., Withers, J., Koh, Y.H., Parry, K., Bao, H., Zhang, B., Budnik, V. and Pennetta, G. (2008) hVAPB, the causative gene of a heterogeneous group of motor neuron diseases in humans, is functionally interchangeable with its Drosophila homologue DVAP-33A at the neuromuscular junction. Hum. Mol. Genet., 17, 266-280.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 266-280
    • Chai, A.1    Withers, J.2    Koh, Y.H.3    Parry, K.4    Bao, H.5    Zhang, B.6    Budnik, V.7    Pennetta, G.8
  • 7
    • 43449099127 scopus 로고    scopus 로고
    • The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors
    • Tsuda, H., Han, S.M., Yang, Y., Tong, C., Lin, Y.Q., Mohan, K., Haueter, C., Zoghbi, A., Harati, Y., Kwan, J. et al. (2008) The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell, 133, 963-977.
    • (2008) Cell , vol.133 , pp. 963-977
    • Tsuda, H.1    Han, S.M.2    Yang, Y.3    Tong, C.4    Lin, Y.Q.5    Mohan, K.6    Haueter, C.7    Zoghbi, A.8    Harati, Y.9    Kwan, J.10
  • 8
    • 84862777321 scopus 로고    scopus 로고
    • Secreted VAPB/ ALS8 major sperm protein domains modulate mitochondrial localization and morphology via growth cone guidance receptors
    • Han, S.M., Tsuda, H., Yang, Y., Vibbert, J., Cottee, P., Lee, S.-J., Winek, J., Haueter, C., Bellen, H.J. and Miller, M.A. (2012) Secreted VAPB/ ALS8 major sperm protein domains modulate mitochondrial localization and morphology via growth cone guidance receptors. Dev. Cell, 22, 348-362.
    • (2012) Dev. Cell , vol.22 , pp. 348-362
    • Han, S.M.1    Tsuda, H.2    Yang, Y.3    Vibbert, J.4    Cottee, P.5    Lee, S.-J.6    Winek, J.7    Haueter, C.8    Bellen, H.J.9    Miller, M.A.10
  • 9
    • 48449098142 scopus 로고    scopus 로고
    • A Drosophila model of ALS: human ALS-associated mutation in VAP33A suggests a dominant negative mechanism
    • Ratnaparkhi, A., Lawless, G.M., Schweizer, F.E., Golshani, P. and Jackson, G.R. (2008) A Drosophila model of ALS: human ALS-associated mutation in VAP33A suggests a dominant negative mechanism. PLoS ONE, 3, e2334.
    • (2008) PLoS ONE , vol.3
    • Ratnaparkhi, A.1    Lawless, G.M.2    Schweizer, F.E.3    Golshani, P.4    Jackson, G.R.5
  • 10
    • 33749554133 scopus 로고    scopus 로고
    • Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8)
    • Kanekura, K., Nishimoto, I., Aiso, S. and Matsuoka, M. (2006) Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8). J. Biol. Chem., 281, 30223-30233.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30223-30233
    • Kanekura, K.1    Nishimoto, I.2    Aiso, S.3    Matsuoka, M.4
  • 11
    • 77954324616 scopus 로고    scopus 로고
    • AAV-mediated expression of wild-type and ALS-linked mutant VAPB selectively triggers death of motoneurons through a Ca2+-dependent ER-associated pathway
    • Langou, K., Moumen, A., Pellegrino, C., Aebischer, J., Medina, I., Aebischer, P. and Raoul, C. (2010) AAV-mediated expression of wild-type and ALS-linked mutant VAPB selectively triggers death of motoneurons through a Ca2+-dependent ER-associated pathway. J. Neurochem., 114, 795-809.
    • (2010) J. Neurochem. , vol.114 , pp. 795-809
    • Langou, K.1    Moumen, A.2    Pellegrino, C.3    Aebischer, J.4    Medina, I.5    Aebischer, P.6    Raoul, C.7
  • 12
    • 58549088349 scopus 로고    scopus 로고
    • ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB
    • Suzuki, H., Kanekura, K., Levine, T.P., Kohno, K., Olkkonen, V.M., Aiso, S. and Matsuoka, M. (2009) ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB. J. Neurochem., 108, 973-985.
    • (2009) J. Neurochem. , vol.108 , pp. 973-985
    • Suzuki, H.1    Kanekura, K.2    Levine, T.P.3    Kohno, K.4    Olkkonen, V.M.5    Aiso, S.6    Matsuoka, M.7
  • 14
    • 84859246580 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria
    • Mórotz, G.M., De Vos, K.J., Vagnoni, A., Ackerley, S., Shaw, C.E. and Miller, C.C.J. (2012) Amyotrophic lateral sclerosis-associated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria. Hum. Mol. Genet., 21, 1979-1988.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1979-1988
    • Mórotz, G.M.1    De Vos, K.J.2    Vagnoni, A.3    Ackerley, S.4    Shaw, C.E.5    Miller, C.C.J.6
  • 15
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo, G. and 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
  • 16
    • 0033532062 scopus 로고    scopus 로고
    • SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
    • Guo, S., Stolz, L.E., Lemrow, S.M. and York, J.D. (1999) SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases. J. Biol. Chem., 274, 12990-12995.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12990-12995
    • Guo, S.1    Stolz, L.E.2    Lemrow, S.M.3    York, J.D.4
  • 17
    • 0035172107 scopus 로고    scopus 로고
    • Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology
    • Foti, M., Audhya, A. and Emr, S.D. (2001) Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology. Mol. Biol. Cell, 12, 2396-2411.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2396-2411
    • Foti, M.1    Audhya, A.2    Emr, S.D.3
  • 18
    • 65549133823 scopus 로고    scopus 로고
    • Modulation of sphingolipid metabolism by the phosphatidylinositol-4-phosphate phosphatase Sac1p through regulation of phosphatidylinositol in Saccharomyces cerevisiae
    • Brice, S.E., Alford, C.W. and Cowart, L.A. (2009) Modulation of sphingolipid metabolism by the phosphatidylinositol-4-phosphate phosphatase Sac1p through regulation of phosphatidylinositol in Saccharomyces cerevisiae. J. Biol. Chem., 284, 7588-7596.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7588-7596
    • Brice, S.E.1    Alford, C.W.2    Cowart, L.A.3
  • 19
    • 0242318325 scopus 로고    scopus 로고
    • The Sac1 lipid phosphatase regulates cell shape change and the JNK cascade during dorsal closure in Drosophila
    • Wei, H.-C., Sanny, J., Shu, H., Baillie, D.L., Brill, J.A., Price, J.V. and Harden, N. (2003) The Sac1 lipid phosphatase regulates cell shape change and the JNK cascade during dorsal closure in Drosophila. Curr. Biol., 13, 1882-1887.
    • (2003) Curr. Biol. , vol.13 , pp. 1882-1887
    • Wei, H.-C.1    Sanny, J.2    Shu, H.3    Baillie, D.L.4    Brill, J.A.5    Price, J.V.6    Harden, N.7
  • 20
    • 84855715100 scopus 로고    scopus 로고
    • The phosphoinositide phosphatase Sac1 is required for midline axon guidance
    • Lee, S., Kim, S., Nahm, M., Kim, E., Kim, T.-I., Yoon, J.H. and Lee, S. (2011) The phosphoinositide phosphatase Sac1 is required for midline axon guidance. Mol. Cell, 32, 477-482.
    • (2011) Mol. Cell , vol.32 , pp. 477-482
    • Lee, S.1    Kim, S.2    Nahm, M.3    Kim, E.4    Kim, T.-I.5    Yoon, J.H.6    Lee, S.7
  • 21
    • 51349106229 scopus 로고    scopus 로고
    • The Sac1 phosphoinositide phosphatase regulates Golgi membrane morphology and mitotic spindle organization in mammals
    • Liu, Y., Boukhelifa, M., Tribble, E., Morin-Kensicki, E., Uetrecht, A., Bear, J.E. and Bankaitis, V.A. (2008) The Sac1 phosphoinositide phosphatase regulates Golgi membrane morphology and mitotic spindle organization in mammals. Mol. Biol. Cell, 19, 3080-3096.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3080-3096
    • Liu, Y.1    Boukhelifa, M.2    Tribble, E.3    Morin-Kensicki, E.4    Uetrecht, A.5    Bear, J.E.6    Bankaitis, V.A.7
  • 25
    • 0033710887 scopus 로고    scopus 로고
    • Drosophila Futsch regulates synaptic microtubule organization and is necessary for synaptic growth
    • Roos, J., Hummel, T., Ng, N., Klämbt, C. and Davis, G.W. (2000) Drosophila Futsch regulates synaptic microtubule organization and is necessary for synaptic growth. Neuron, 26, 371-382.
    • (2000) Neuron , vol.26 , pp. 371-382
    • Roos, J.1    Hummel, T.2    Ng, N.3    Klämbt, C.4    Davis, G.W.5
  • 26
    • 13944280702 scopus 로고    scopus 로고
    • Drosophila spastin regulates synaptic microtubule networks and is required for normal motor function
    • Sherwood, N.T., Sun, Q., Xue, M., Zhang, B. and Zinn, K. (2004) Drosophila spastin regulates synaptic microtubule networks and is required for normal motor function. PLoS Biol., 2, e429.
    • (2004) PLoS Biol. , vol.2
    • Sherwood, N.T.1    Sun, Q.2    Xue, M.3    Zhang, B.4    Zinn, K.5
  • 27
    • 33644870049 scopus 로고    scopus 로고
    • Bruchpilot, a protein with homology to ELKS/CAST, is required for structural integrity and function of synaptic active zones in Drosophila
    • Wagh, D.A., Rasse, T.M., Asan, E., Hofbauer, A., Schwenkert, I., Dürrbeck, H., Buchner, S., Dabauvalle, M.-C., Schmidt, M., Qin, G. et al. (2006) Bruchpilot, a protein with homology to ELKS/CAST, is required for structural integrity and function of synaptic active zones in Drosophila. Neuron, 49, 833-844.
    • (2006) Neuron , vol.49 , pp. 833-844
    • Wagh, D.A.1    Rasse, T.M.2    Asan, E.3    Hofbauer, A.4    Schwenkert, I.5    Dürrbeck, H.6    Buchner, S.7    Dabauvalle, M.-C.8    Schmidt, M.9    Qin, G.10
  • 28
    • 79952770603 scopus 로고    scopus 로고
    • Hts/Adducin controls synaptic elaboration and elimination
    • Pielage, J., Bulat, V., Zuchero, J.B., Fetter, R.D. and Davis, G.W. (2011) Hts/Adducin controls synaptic elaboration and elimination. Neuron, 69, 1114-1131.
    • (2011) Neuron , vol.69 , pp. 1114-1131
    • Pielage, J.1    Bulat, V.2    Zuchero, J.B.3    Fetter, R.D.4    Davis, G.W.5
  • 29
    • 0037072757 scopus 로고    scopus 로고
    • Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions
    • Wang, J., Gambhir, A., Hangyás-Mihályné, G., Murray, D., Golebiewska, U. and McLaughlin, S. (2002) Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions. J. Biol. Chem., 277, 34401-34412.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34401-34412
    • Wang, J.1    Gambhir, A.2    Hangyás-Mihályné, G.3    Murray, D.4    Golebiewska, U.5    McLaughlin, S.6
  • 30
    • 33750719949 scopus 로고    scopus 로고
    • A postsynaptic spectrin scaffold defines active zone size, spacing, and efficacy at the Drosophila neuromuscular junction
    • Pielage, J., Fetter, R.D. and Davis, G.W. (2006) A postsynaptic spectrin scaffold defines active zone size, spacing, and efficacy at the Drosophila neuromuscular junction. J. Cell Biol., 175, 491-503.
    • (2006) J. Cell Biol. , vol.175 , pp. 491-503
    • Pielage, J.1    Fetter, R.D.2    Davis, G.W.3
  • 32
    • 80052154328 scopus 로고    scopus 로고
    • Drosophila adducin regulates Dlg phosphorylation and targeting of Dlg to the synapse and epithelial membrane
    • Wang, S., Yang, J., Tsai, A., Kuca, T., Sanny, J., Lee, J., Dong, K., Harden, N. and Krieger, C. (2011) Drosophila adducin regulates Dlg phosphorylation and targeting of Dlg to the synapse and epithelial membrane. Dev. Biol., 357, 392-403.
    • (2011) Dev. Biol. , vol.357 , pp. 392-403
    • Wang, S.1    Yang, J.2    Tsai, A.3    Kuca, T.4    Sanny, J.5    Lee, J.6    Dong, K.7    Harden, N.8    Krieger, C.9
  • 33
    • 0035875699 scopus 로고    scopus 로고
    • Drosophila alpha- and beta-spectrin mutations disrupt presynaptic neurotransmitter release
    • Featherstone, D.E., Davis, W.S., Dubreuil, R.R. and Broadie, K. (2001) Drosophila alpha- and beta-spectrin mutations disrupt presynaptic neurotransmitter release. J. Neurosci., 21, 4215-4224.
    • (2001) J. Neurosci. , vol.21 , pp. 4215-4224
    • Featherstone, D.E.1    Davis, W.S.2    Dubreuil, R.R.3    Broadie, K.4
  • 34
    • 2442477424 scopus 로고    scopus 로고
    • New synaptic bouton formation is disrupted by misregulation of microtubule stability in aPKC mutants
    • Ruiz-Canada, C., Ashley, J., Moeckel-Cole, S., Drier, E., Yin, J. and Budnik, V. (2004) New synaptic bouton formation is disrupted by misregulation of microtubule stability in aPKC mutants. Neuron, 42, 567-580.
    • (2004) Neuron , vol.42 , pp. 567-580
    • Ruiz-Canada, C.1    Ashley, J.2    Moeckel-Cole, S.3    Drier, E.4    Yin, J.5    Budnik, V.6
  • 35
    • 0027269974 scopus 로고
    • SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast
    • Whitters, E.A., Cleves, A.E., McGee, T.P., Skinner, H.B. and Bankaitis, V.A. (1993) SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast. J. Cell Biol., 122, 79-94.
    • (1993) J. Cell Biol. , vol.122 , pp. 79-94
    • Whitters, E.A.1    Cleves, A.E.2    McGee, T.P.3    Skinner, H.B.4    Bankaitis, V.A.5
  • 36
    • 0034602319 scopus 로고    scopus 로고
    • Functional characterization of a mammalian Sac1 and mutants exhibiting substrate-specific defects in phosphoinositide phosphatase activity
    • Nemoto, Y., Kearns, B.G., Wenk, M.R., Chen, H., Mori, K., Alb, J.G. Jr, De Camilli, P. and Bankaitis, V.A. (2000) Functional characterization of a mammalian Sac1 and mutants exhibiting substrate-specific defects in phosphoinositide phosphatase activity. J. Biol. Chem., 275, 34293-34305.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34293-34305
    • Nemoto, Y.1    Kearns, B.G.2    Wenk, M.R.3    Chen, H.4    Mori, K.5    Alb Jr., J.G.6    De Camilli, P.7    Bankaitis, V.A.8
  • 37
    • 0037423256 scopus 로고    scopus 로고
    • Boca, an endoplasmic reticulum protein required for wingless signaling and trafficking of LDL receptor family members in Drosophila
    • Culi, J. and Mann, R.S. (2003) Boca, an endoplasmic reticulum protein required for wingless signaling and trafficking of LDL receptor family members in Drosophila. Cell, 112, 343-354.
    • (2003) Cell , vol.112 , pp. 343-354
    • Culi, J.1    Mann, R.S.2
  • 38
    • 84856251270 scopus 로고    scopus 로고
    • Growth and metabolic control of lipid signalling at the Golgi
    • Piao, H. and Mayinger, P. (2012) Growth and metabolic control of lipid signalling at the Golgi. Biochem. Soc. Trans., 40, 205-209.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 205-209
    • Piao, H.1    Mayinger, P.2
  • 39
    • 79551674131 scopus 로고    scopus 로고
    • Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites
    • Stefan, C.J., Manford, A.G., Baird, D., Yamada-Hanff, J., Mao, Y. and Emr, S.D. (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    Emr, S.D.6
  • 40
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick, J.M., Chan, H.Y., Gray-Board, G.L., Chai, Y., Paulson, H.L. and Bonini, N.M. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet., 23, 425-428.
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 43
    • 0032562705 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase and phosphatidylinositol transfer protein act synergistically in formation of constitutive transport vesicles from the trans-Golgi network
    • Jones, S.M., Alb, J.G. Jr, Phillips, S.E., Bankaitis, V.A. and Howell, K.E. (1998) A phosphatidylinositol 3-kinase and phosphatidylinositol transfer protein act synergistically in formation of constitutive transport vesicles from the trans-Golgi network. J. Biol. Chem., 273, 10349-10354.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10349-10354
    • Jones, S.M.1    Alb Jr., J.G.2    Phillips, S.E.3    Bankaitis, V.A.4    Howell, K.E.5
  • 44
    • 36048939802 scopus 로고    scopus 로고
    • The yeast VAP homolog Scs2p has a phosphoinositide-binding ability that is correlated with its activity
    • Kagiwada, S. and Hashimoto, M. (2007) The yeast VAP homolog Scs2p has a phosphoinositide-binding ability that is correlated with its activity. Biochem. Biophys. Res. Commun., 364, 870-876.
    • (2007) Biochem. Biophys. Res. Commun. , vol.364 , pp. 870-876
    • Kagiwada, S.1    Hashimoto, M.2
  • 45
    • 84870793680 scopus 로고    scopus 로고
    • ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology
    • Manford, A.G., Stefan, C.J., Yuan, H.L., Macgurn, J.A. and Emr, S.D. (2012) ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology. Dev. Cell, 23, 1129-1140.
    • (2012) Dev. Cell , vol.23 , pp. 1129-1140
    • Manford, A.G.1    Stefan, C.J.2    Yuan, H.L.3    Macgurn, J.A.4    Emr, S.D.5
  • 47
    • 35348910763 scopus 로고    scopus 로고
    • Growth control of Golgi phosphoinositides by reciprocal localization of sac1 lipid phosphatase and pik1 4-kinase
    • Faulhammer, F., Kanjilal-Kolar, S., Knödler, A., Lo, J., Lee, Y., Konrad, G. and Mayinger, P. (2007) Growth control of Golgi phosphoinositides by reciprocal localization of sac1 lipid phosphatase and pik1 4-kinase. Traffic, 8, 1554-1567.
    • (2007) Traffic , vol.8 , pp. 1554-1567
    • Faulhammer, F.1    Kanjilal-Kolar, S.2    Knödler, A.3    Lo, J.4    Lee, Y.5    Konrad, G.6    Mayinger, P.7
  • 49
    • 76749088358 scopus 로고    scopus 로고
    • Pathological roles of MAPK signaling pathways in human diseases
    • Kim, E.K. and Choi, E.-J. (2010) Pathological roles of MAPK signaling pathways in human diseases. Biochim. Biophys. Acta, 1802, 396-405.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 396-405
    • Kim, E.K.1    Choi, E.-J.2
  • 50
    • 79960739849 scopus 로고    scopus 로고
    • Lipid transfer and signaling at organelle contact sites: the tip of the iceberg
    • Toulmay, A. and Prinz, W.A. (2011) Lipid transfer and signaling at organelle contact sites: the tip of the iceberg. Curr. Opin. Cell Biol., 23, 458-463.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 458-463
    • Toulmay, A.1    Prinz, W.A.2
  • 51
    • 41149145117 scopus 로고    scopus 로고
    • Cell- and stimulus-dependent heterogeneity of synaptic vesicle endocytic recycling mechanisms revealed by studies of dynamin 1-null neurons
    • Hayashi, M., Raimondi, A., O'Toole, E., Paradise, S., Collesi, C., Cremona, O., Ferguson, S.M. and De Camilli, P. (2008) Cell- and stimulus-dependent heterogeneity of synaptic vesicle endocytic recycling mechanisms revealed by studies of dynamin 1-null neurons. Proc. Natl Acad. Sci. USA, 105, 2175-2180.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 2175-2180
    • Hayashi, M.1    Raimondi, A.2    O'Toole, E.3    Paradise, S.4    Collesi, C.5    Cremona, O.6    Ferguson, S.M.7    De Camilli, P.8
  • 52
    • 0028484074 scopus 로고
    • Immunolocalization of a Drosophila phosphatidylinositol transfer protein (rdgB) in normal and rdgA mutant photoreceptor cells with special reference to the subrhabdomeric cisternae
    • Suzuki, E. and Hirosawa, K. (1994) Immunolocalization of a Drosophila phosphatidylinositol transfer protein (rdgB) in normal and rdgA mutant photoreceptor cells with special reference to the subrhabdomeric cisternae. J. Electron Microsc. (Tokyo), 43, 183-189.
    • (1994) J. Electron Microsc. (Tokyo) , vol.43 , pp. 183-189
    • Suzuki, E.1    Hirosawa, K.2
  • 53
    • 55549111249 scopus 로고    scopus 로고
    • Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport
    • Peretti, D., Dahan, N., Shimoni, E., Hirschberg, K. and Lev, S. (2008) Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport. Mol. Biol. Cell, 19, 3871-3884.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3871-3884
    • Peretti, D.1    Dahan, N.2    Shimoni, E.3    Hirschberg, K.4    Lev, S.5
  • 54
    • 67649600680 scopus 로고    scopus 로고
    • Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning
    • Rocha, N., Kuijl, C., Van der Kant, R., Janssen, L., Houben, D., Janssen, H., Zwart, W. and Neefjes, J. (2009) Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning. J. Cell Biol., 185, 1209-1225.
    • (2009) J. Cell Biol. , vol.185 , pp. 1209-1225
    • Rocha, N.1    Kuijl, C.2    Van der Kant, R.3    Janssen, L.4    Houben, D.5    Janssen, H.6    Zwart, W.7    Neefjes, J.8
  • 56
    • 0033840656 scopus 로고    scopus 로고
    • Distinct roles for the yeast phosphatidylinositol 4-kinases, Stt4p and Pik1p, in secretion, cell growth, and organelle membrane dynamics
    • Audhya, A., Foti, M. and Emr, S.D. (2000) Distinct roles for the yeast phosphatidylinositol 4-kinases, Stt4p and Pik1p, in secretion, cell growth, and organelle membrane dynamics. Mol. Biol. Cell, 11, 2673-2689.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2673-2689
    • Audhya, A.1    Foti, M.2    Emr, S.D.3
  • 57
    • 0036001334 scopus 로고    scopus 로고
    • Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkc1-mediated MAP kinase cascade
    • Audhya, A. and Emr, S.D. (2002) Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkc1-mediated MAP kinase cascade. Dev. Cell, 2, 593-605.
    • (2002) Dev. Cell , vol.2 , pp. 593-605
    • Audhya, A.1    Emr, S.D.2
  • 58
    • 29144458344 scopus 로고    scopus 로고
    • Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus
    • Strahl, T., Hama, H., DeWald, D.B. and Thorner, J. (2005) Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus. J. Cell Biol., 171, 967-979.
    • (2005) J. Cell Biol. , vol.171 , pp. 967-979
    • Strahl, T.1    Hama, H.2    DeWald, D.B.3    Thorner, J.4
  • 59
    • 0033258472 scopus 로고    scopus 로고
    • The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi
    • Walch-Solimena, C. and 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
  • 60
    • 77955370261 scopus 로고    scopus 로고
    • Pheromone-induced anisotropy in yeast plasma membrane phosphatidylinositol-4,5-bisphosphate distribution is required for MAPK signaling
    • Garrenton, L.S., Stefan, C.J., McMurray, M.A., Emr, S.D. and Thorner, J. (2010) Pheromone-induced anisotropy in yeast plasma membrane phosphatidylinositol-4,5-bisphosphate distribution is required for MAPK signaling. Proc. Natl Acad. Sci. USA, 107, 11805-11810.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 11805-11810
    • Garrenton, L.S.1    Stefan, C.J.2    McMurray, M.A.3    Emr, S.D.4    Thorner, J.5
  • 61
    • 79955432520 scopus 로고    scopus 로고
    • Selective regulation of MAP kinase signaling by an endomembrane phosphatidylinositol 4-kinase
    • Cappell, S.D. and Dohlman, H.G. (2011) Selective regulation of MAP kinase signaling by an endomembrane phosphatidylinositol 4-kinase. J. Biol. Chem., 286, 14852-14860.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14852-14860
    • Cappell, S.D.1    Dohlman, H.G.2
  • 62
    • 79955427372 scopus 로고    scopus 로고
    • Drosophila PI4KIIIalpha is required in follicle cells for oocyte polarization and Hippo signaling
    • Yan, Y., Denef, N., Tang, C. and Schüpbach, T. (2011) Drosophila PI4KIIIalpha is required in follicle cells for oocyte polarization and Hippo signaling. Development, 138, 1697-1703.
    • (2011) Development , vol.138 , pp. 1697-1703
    • Yan, Y.1    Denef, N.2    Tang, C.3    Schüpbach, T.4
  • 63
    • 0033824820 scopus 로고    scopus 로고
    • A phospholipid kinase regulates actin organization and intercellular bridge formation during germline cytokinesis
    • Brill, J.A., Hime, G.R., Scharer-Schuksz, M. and Fuller, M.T. (2000) A phospholipid kinase regulates actin organization and intercellular bridge formation during germline cytokinesis. Development, 127, 3855-3864.
    • (2000) Development , vol.127 , pp. 3855-3864
    • Brill, J.A.1    Hime, G.R.2    Scharer-Schuksz, M.3    Fuller, M.T.4
  • 65
    • 0027768699 scopus 로고
    • Phosphatidylinositol 4-kinase: gene structure and requirement for yeast cell viability
    • Flanagan, C.A., Schnieders, E.A., Emerick, A.W., Kunisawa, R., Admon, A. and Thorner, J. (1993) Phosphatidylinositol 4-kinase: gene structure and requirement for yeast cell viability. Science, 262, 1444-1448.
    • (1993) Science , vol.262 , pp. 1444-1448
    • Flanagan, C.A.1    Schnieders, E.A.2    Emerick, A.W.3    Kunisawa, R.4    Admon, A.5    Thorner, J.6
  • 66
    • 0027979837 scopus 로고
    • A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1 protein kinase pathway of Saccharomyces cerevisiae
    • Yoshida, S., Ohya, Y., Goebl, M., Nakano, A. and Anraku, Y. (1994) A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1 protein kinase pathway of Saccharomyces cerevisiae. J. Biol. Chem., 269, 1166-1172.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1166-1172
    • Yoshida, S.1    Ohya, Y.2    Goebl, M.3    Nakano, A.4    Anraku, Y.5
  • 67
    • 79151470948 scopus 로고    scopus 로고
    • Coordination of Golgi functions by phosphatidylinositol 4-kinases
    • Graham, T.R. and Burd, C.G. (2011) Coordination of Golgi functions by phosphatidylinositol 4-kinases. Trends Cell Biol., 21, 113-121.
    • (2011) Trends Cell Biol. , vol.21 , pp. 113-121
    • Graham, T.R.1    Burd, C.G.2
  • 68
    • 17644412381 scopus 로고    scopus 로고
    • PI(4,5)P2-dependent microdomain assemblies capture microtubules to promote and control leading edge motility
    • Golub, T. and Caroni, P. (2005) PI(4,5)P2-dependent microdomain assemblies capture microtubules to promote and control leading edge motility. J. Cell Biol., 169, 151-165.
    • (2005) J. Cell Biol. , vol.169 , pp. 151-165
    • Golub, T.1    Caroni, P.2
  • 69
    • 3342965153 scopus 로고    scopus 로고
    • The lipid binding pleckstrin homology domain in UNC-104 kinesin is necessary for synaptic vesicle transport in Caenorhabditis elegans
    • Klopfenstein, D.R. and Vale, R.D. (2004) The lipid binding pleckstrin homology domain in UNC-104 kinesin is necessary for synaptic vesicle transport in Caenorhabditis elegans. Mol. Biol. Cell, 15, 3729-3739.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3729-3739
    • Klopfenstein, D.R.1    Vale, R.D.2
  • 73
    • 78649373124 scopus 로고    scopus 로고
    • Membranes in balance: mechanisms of sphingolipid homeostasis
    • Breslow, D.K. and Weissman, J.S. (2010) Membranes in balance: mechanisms of sphingolipid homeostasis. Mol. Cell, 40, 267-279.
    • (2010) Mol. Cell , vol.40 , pp. 267-279
    • Breslow, D.K.1    Weissman, J.S.2
  • 74
    • 33744728346 scopus 로고    scopus 로고
    • Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein
    • Perry, R.J. and Ridgway, N.D. (2006) Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein. Mol. Biol. Cell, 17, 2604-2616.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2604-2616
    • Perry, R.J.1    Ridgway, N.D.2
  • 75
    • 33646227441 scopus 로고    scopus 로고
    • Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide
    • Hanada, K. (2006) Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide. Mol. Cell. Biochem., 286, 23-31.
    • (2006) Mol. Cell. Biochem. , vol.286 , pp. 23-31
    • Hanada, K.1
  • 76
    • 77957352699 scopus 로고    scopus 로고
    • The diverse functions of oxysterol-binding proteins
    • Raychaudhuri, S. and Prinz, W.A. (2010) The diverse functions of oxysterol-binding proteins. Annu. Rev. Cell Dev. Biol., 26, 157-177.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 157-177
    • Raychaudhuri, S.1    Prinz, W.A.2
  • 78
    • 0033118555 scopus 로고    scopus 로고
    • Watching a synapse grow: noninvasive confocal imaging of synaptic growth in Drosophila
    • Zito, K., Parnas, D., Fetter, R.D., Isacoff, E.Y. and Goodman, C.S. (1999) Watching a synapse grow: noninvasive confocal imaging of synaptic growth in Drosophila. Neuron, 22, 719-729.
    • (1999) Neuron , vol.22 , pp. 719-729
    • Zito, K.1    Parnas, D.2    Fetter, R.D.3    Isacoff, E.Y.4    Goodman, C.S.5
  • 79
    • 33845294390 scopus 로고    scopus 로고
    • A house divided: ceramide, sphingosine, and sphingosine-1-phosphate in programmed cell death
    • Taha, T.A., Mullen, T.D. and Obeid, L.M. (2006) A house divided: ceramide, sphingosine, and sphingosine-1-phosphate in programmed cell death. Biochim. Biophys. Acta, 1758, 2027-2036.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 2027-2036
    • Taha, T.A.1    Mullen, T.D.2    Obeid, L.M.3
  • 80
    • 84868310958 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinases are required for autophagic membrane trafficking
    • Wang, K., Yang, Z., Liu, X., Mao, K., Nair, U. and Klionsky, D.J. (2012) Phosphatidylinositol 4-kinases are required for autophagic membrane trafficking. J. Biol. Chem., 287, 37964-37972.
    • (2012) J. Biol. Chem. , vol.287 , pp. 37964-37972
    • Wang, K.1    Yang, Z.2    Liu, X.3    Mao, K.4    Nair, U.5    Klionsky, D.J.6
  • 81
    • 33749555280 scopus 로고    scopus 로고
    • Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT
    • Kawano, M., Kumagai, K., Nishijima, M. and Hanada, K. (2006) Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT. J. Biol. Chem., 281, 30279-30288.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30279-30288
    • Kawano, M.1    Kumagai, K.2    Nishijima, M.3    Hanada, K.4
  • 82
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S. and Cordelieres, F.P. (2006) A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc, 224, 213-232.
    • (2006) J. Microsc , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2


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