메뉴 건너뛰기




Volumn 297, Issue 1, 2004, Pages 1-10

The role of the Nir/rdgB protein family in membrane trafficking and cytoskeleton remodeling

Author keywords

Cytokinesis; Golgi; Membrane trafficking; Nir; Phosphoinositides; PITP; RdgB; Sec14

Indexed keywords

NIR PROTEIN; PHOSPHATIDYLINOSITOL; PROTEIN; RETINAL DEGENERATION B PROTEIN; UNCLASSIFIED DRUG;

EID: 2942518361     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.02.033     Document Type: Review
Times cited : (54)

References (78)
  • 1
    • 0014691624 scopus 로고
    • Abnormal electroretinograms in visual mutants of Drosophila
    • Hotta Y., Benzer S. Abnormal electroretinograms in visual mutants of Drosophila. Nature. 222:1969;354-356
    • (1969) Nature , vol.222 , pp. 354-356
    • Hotta, Y.1    Benzer, S.2
  • 2
    • 0014876697 scopus 로고
    • Genetic dissection of the Drosophila nervous system by means of mosaics
    • Hotta Y., Benzer S. Genetic dissection of the Drosophila nervous system by means of mosaics. Proc. Natl. Acad. Sci. U. S. A. 67:1970;1156-1163
    • (1970) Proc. Natl. Acad. Sci. U. S. A. , vol.67 , pp. 1156-1163
    • Hotta, Y.1    Benzer, S.2
  • 3
    • 0017332739 scopus 로고
    • Hereditary retinal degeneration in Drosophila melanogaster. A mutant defect associated with the phototransduction process
    • Harris W.A., Stark W.S. Hereditary retinal degeneration in Drosophila melanogaster. A mutant defect associated with the phototransduction process. J. Gen. Physiol. 69:1977;261-291
    • (1977) J. Gen. Physiol. , vol.69 , pp. 261-291
    • Harris, W.A.1    Stark, W.S.2
  • 4
    • 0023180920 scopus 로고
    • Ultrastructure of the retina of Drosophila melanogaster: The mutant ora (outer rhabdomeres absent) and its inhibition of degeneration in rdgB (retinal degeneration-B)
    • Stark W.S., Sapp R. Ultrastructure of the retina of Drosophila melanogaster: the mutant ora (outer rhabdomeres absent) and its inhibition of degeneration in rdgB (retinal degeneration-B). J. Neurogenet. 4:1987;227-240
    • (1987) J. Neurogenet. , vol.4 , pp. 227-240
    • Stark, W.S.1    Sapp, R.2
  • 5
    • 0024892203 scopus 로고
    • Light-induced retinal degeneration in rdgB (retinal degeneration B) mutant of Drosophila: Electrophysiological and morphological manifestations of degeneration
    • Rubinstein C.T., Bar-Nachum S., Selinger Z., Minke B. Light-induced retinal degeneration in rdgB (retinal degeneration B) mutant of Drosophila: electrophysiological and morphological manifestations of degeneration. Vis. Neurosci. 2:1989;529-539
    • (1989) Vis. Neurosci. , vol.2 , pp. 529-539
    • Rubinstein, C.T.1    Bar-Nachum, S.2    Selinger, Z.3    Minke, B.4
  • 6
    • 0027216545 scopus 로고
    • Localization of Drosophila retinal degeneration B, a membrane-associated phosphatidylinositol transfer protein
    • Vihtelic T.S., Goebl M., Milligan S., O'Tousa J.E., Hyde D.R. Localization of Drosophila retinal degeneration B, a membrane-associated phosphatidylinositol transfer protein. J. Cell Biol. 122:1993;1013-1022
    • (1993) J. Cell Biol. , vol.122 , pp. 1013-1022
    • Vihtelic, T.S.1    Goebl, M.2    Milligan, S.3    O'Tousa, J.E.4    Hyde, D.R.5
  • 8
    • 0030741252 scopus 로고    scopus 로고
    • Cloning and characterization of human homologue of Drosophila retinal degeneration B: A candidate gene for degenerative retinal diseases
    • Guo J., Yu F.X. Cloning and characterization of human homologue of Drosophila retinal degeneration B: a candidate gene for degenerative retinal diseases. Dev. Genet. 20:1997;235-245
    • (1997) Dev. Genet. , vol.20 , pp. 235-245
    • Guo, J.1    Yu, F.X.2
  • 9
    • 0031591657 scopus 로고    scopus 로고
    • Molecular cloning and characterization of mammalian homologues of the Drosophila retinal degeneration B gene
    • Aikawa Y., Hara H., Watanabe T. Molecular cloning and characterization of mammalian homologues of the Drosophila retinal degeneration B gene. Biochem. Biophys. Res. Commun. 236:1997;559-564
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 559-564
    • Aikawa, Y.1    Hara, H.2    Watanabe, T.3
  • 10
    • 0034053578 scopus 로고    scopus 로고
    • Cloning and tissue localization of a novel zebrafish RdgB homolog that lacks a phospholipid transfer domain
    • Elagin V.A., Elagina R.B., Doro C.J., Vihtelic T.S., Hyde D.R. Cloning and tissue localization of a novel zebrafish RdgB homolog that lacks a phospholipid transfer domain. Vis. Neurosci. 17:2000;303-311
    • (2000) Vis. Neurosci. , vol.17 , pp. 303-311
    • Elagin, V.A.1    Elagina, R.B.2    Doro, C.J.3    Vihtelic, T.S.4    Hyde, D.R.5
  • 11
    • 0031151235 scopus 로고    scopus 로고
    • A mammalian homologue of the Drosophila retinal degeneration B gene: Implications for the evolution of phototransduction mechanisms
    • Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M., Borsani G., Ballabio A., Banfi S. A mammalian homologue of the Drosophila retinal degeneration B gene: implications for the evolution of phototransduction mechanisms. Genes Funct. 1:1997;205-213
    • (1997) Genes Funct. , vol.1 , pp. 205-213
    • Rubboli, F.1    Bulfone, A.2    Bogni, S.3    Marchitiello, A.4    Zollo, M.5    Borsani, G.6    Ballabio, A.7    Banfi, S.8
  • 12
    • 0032981482 scopus 로고    scopus 로고
    • Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein
    • Lev S., Hernandez J., Martinez R., Chen A., Plowman G., Schlessinger J. Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol. Cell. Biol. 19:1999;2278-2288
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2278-2288
    • Lev, S.1    Hernandez, J.2    Martinez, R.3    Chen, A.4    Plowman, G.5    Schlessinger, J.6
  • 13
    • 0035834805 scopus 로고    scopus 로고
    • The mammalian retinal degeneration B2 gene is not required for photoreceptor function and survival
    • Lu C., Peng Y.W., Shang J., Pawlyk B.S., Yu F., Li T. The mammalian retinal degeneration B2 gene is not required for photoreceptor function and survival. Neuroscience. 107:2001;35-41
    • (2001) Neuroscience , vol.107 , pp. 35-41
    • Lu, C.1    Peng, Y.W.2    Shang, J.3    Pawlyk, B.S.4    Yu, F.5    Li, T.6
  • 14
    • 0033198297 scopus 로고    scopus 로고
    • A neuronal-specific mammalian homolog of the Drosophila retinal degeneration B gene with expression restricted to the retina and dentate gyrus
    • Lu C., Vihtelic T.S., Hyde D.R., Li T. A neuronal-specific mammalian homolog of the Drosophila retinal degeneration B gene with expression restricted to the retina and dentate gyrus. J. Neurosci. 19:1999;7317-7325
    • (1999) J. Neurosci. , vol.19 , pp. 7317-7325
    • Lu, C.1    Vihtelic, T.S.2    Hyde, D.R.3    Li, T.4
  • 15
    • 0033615601 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human phosphatidylinositol transfer protein, rdgBbeta
    • Fullwood Y., dos Santos M., Hsuan J.J. Cloning and characterization of a novel human phosphatidylinositol transfer protein, rdgBbeta. J. Biol. Chem. 274:1999;31553-31558
    • (1999) J. Biol. Chem. , vol.274 , pp. 31553-31558
    • Fullwood, Y.1    Dos Santos, M.2    Hsuan, J.J.3
  • 16
    • 0035782882 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins couple lipid transport to phosphoinositide synthesis
    • Cockcroft S. Phosphatidylinositol transfer proteins couple lipid transport to phosphoinositide synthesis. Semin. Cell Dev. Biol. 12:2001;183-191
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 183-191
    • Cockcroft, S.1
  • 17
    • 0034815386 scopus 로고    scopus 로고
    • The PITP family of phosphatidylinositol transfer proteins
    • Hsuan J., Cockcroft S. The PITP family of phosphatidylinositol transfer proteins. Genome Biol. 2:2001;S3011.1-S3011.8
    • (2001) Genome Biol. , vol.2
    • Hsuan, J.1    Cockcroft, S.2
  • 20
    • 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., Howell K.E. A phosphatidylinositol 3-kinase and phosphatidylinositol transfer protein act synergistically in formation of constitutive transport vesicles from the trans-Golgi network. J. Biol. Chem. 273:1998;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
  • 21
    • 0027765507 scopus 로고
    • Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion
    • Hay J.C., Martin T.F. Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion. Nature. 366:1993;572-575
    • (1993) Nature , vol.366 , pp. 572-575
    • Hay, J.C.1    Martin, T.F.2
  • 23
    • 0042780282 scopus 로고    scopus 로고
    • Mice lacking phosphatidylinositol transfer protein-alpha exhibit spinocerebellar degeneration, intestinal and hepatic steatosis, and hypoglycemia
    • Alb J.G. Jr., Cortese J.D., Phillips S.E., Albin R.L., Nagy T.R., Hamilton B.A., Bankaitis V.A. Mice lacking phosphatidylinositol transfer protein-alpha exhibit spinocerebellar degeneration, intestinal and hepatic steatosis, and hypoglycemia. J. Biol. Chem. 278:2003;33501-33518
    • (2003) J. Biol. Chem. , vol.278 , pp. 33501-33518
    • Alb Jr., J.G.1    Cortese, J.D.2    Phillips, S.E.3    Albin, R.L.4    Nagy, T.R.5    Hamilton, B.A.6    Bankaitis, V.A.7
  • 25
    • 0030806560 scopus 로고    scopus 로고
    • The phosphatidylinositol transfer protein domain of Drosophila retinal degeneration B protein is essential for photoreceptor cell survival and recovery from light stimulation
    • Milligan S.C., Alb J.G. Jr., Elagina R.B., Bankaitis V.A., Hyde D.R. The phosphatidylinositol transfer protein domain of Drosophila retinal degeneration B protein is essential for photoreceptor cell survival and recovery from light stimulation. J. Cell Biol. 139:1997;351-363
    • (1997) J. Cell Biol. , vol.139 , pp. 351-363
    • Milligan, S.C.1    Alb Jr., J.G.2    Elagina, R.B.3    Bankaitis, V.A.4    Hyde, D.R.5
  • 26
    • 0025833537 scopus 로고
    • Isolation and characterization of the Drosophila retinal degeneration B (rdgB) gene
    • Vihtelic T.S., Hyde D.R., O'Tousa J.E. Isolation and characterization of the Drosophila retinal degeneration B (rdgB) gene. Genetics. 127:1991;761-768
    • (1991) Genetics , vol.127 , pp. 761-768
    • Vihtelic, T.S.1    Hyde, D.R.2    O'Tousa, J.E.3
  • 27
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • Loewen C.J., Roy A., Levine T.P. A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP. EMBO J. 22:2003;2025-2035
    • (2003) EMBO J. , vol.22 , pp. 2025-2035
    • Loewen, C.J.1    Roy, A.2    Levine, T.P.3
  • 29
    • 0037605881 scopus 로고    scopus 로고
    • Phospholipase A2 (PLA2) enzymes in membrane trafficking: Mediators of membrane shape and function
    • Brown W.J., Chambers K., Doody A. Phospholipase A2 (PLA2) enzymes in membrane trafficking: mediators of membrane shape and function. Traffic. 4:2003;214-221
    • (2003) Traffic , vol.4 , pp. 214-221
    • Brown, W.J.1    Chambers, K.2    Doody, A.3
  • 30
    • 0036271299 scopus 로고    scopus 로고
    • Cellular and developmental distribution of human homologues of the Drosophila rdgB protein in the rat retina
    • Tian D., Lev S. Cellular and developmental distribution of human homologues of the Drosophila rdgB protein in the rat retina. Investig. Ophthalmol. Vis. Sci. 43:2002;1946-1953
    • (2002) Investig. Ophthalmol. Vis. Sci. , vol.43 , pp. 1946-1953
    • Tian, D.1    Lev, S.2
  • 31
    • 0037015277 scopus 로고    scopus 로고
    • Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain
    • Litvak V., Shaul Y.D., Shulewitz M., Amarilio R., Carmon S., Lev S. Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain. Curr. Biol. 12:2002;1513-1518
    • (2002) Curr. Biol. , vol.12 , pp. 1513-1518
    • Litvak, V.1    Shaul, Y.D.2    Shulewitz, M.3    Amarilio, R.4    Carmon, S.5    Lev, S.6
  • 32
    • 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., Hirosawa K. 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). 43:1994;183-189
    • (1994) J. Electron Microsc. (Tokyo) , vol.43 , pp. 183-189
    • Suzuki, E.1    Hirosawa, K.2
  • 33
    • 0020000128 scopus 로고
    • Ca2+-sequestering smooth endoplasmic reticulum in an invertebrate photoreceptor. I. Intracellular topography as revealed by OsFeCN staining and in situ Ca accumulation
    • Walz B. Ca2+-sequestering smooth endoplasmic reticulum in an invertebrate photoreceptor. I. Intracellular topography as revealed by OsFeCN staining and in situ Ca accumulation. J. Cell Biol. 93:1982;839-848
    • (1982) J. Cell Biol. , vol.93 , pp. 839-848
    • Walz, B.1
  • 34
    • 0033575219 scopus 로고    scopus 로고
    • Involvement of PITPnm, a mammalian homologue of Drosophila rdgB, in phosphoinositide synthesis on Golgi membranes
    • Aikawa Y., Kuraoka A., Kondo H., Kawabuchi M., Watanabe T. Involvement of PITPnm, a mammalian homologue of Drosophila rdgB, in phosphoinositide synthesis on Golgi membranes. J. Biol. Chem. 274:1999;20569-20577
    • (1999) J. Biol. Chem. , vol.274 , pp. 20569-20577
    • Aikawa, Y.1    Kuraoka, A.2    Kondo, H.3    Kawabuchi, M.4    Watanabe, T.5
  • 35
    • 0032911957 scopus 로고    scopus 로고
    • Mechanisms of lipid-body formation
    • Murphy D.J., Vance J. Mechanisms of lipid-body formation. Trends Biochem. Sci. 24:1999;109-115
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 109-115
    • Murphy, D.J.1    Vance, J.2
  • 36
    • 0035810964 scopus 로고    scopus 로고
    • Lipid droplets: Proteins floating on a pool of fat
    • Brown D.A. Lipid droplets: proteins floating on a pool of fat. Curr. Biol. 11:2001;R446-R449
    • (2001) Curr. Biol. , vol.11
    • Brown, D.A.1
  • 37
    • 0032404324 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins: The long and winding road to physiological function
    • Kearns B.G., Alb J.G. Jr., Bankaitis V. Phosphatidylinositol transfer proteins: the long and winding road to physiological function. Trends. Cell Biol. 8:1998;276-282
    • (1998) Trends. Cell Biol. , vol.8 , pp. 276-282
    • Kearns, B.G.1    Alb Jr., J.G.2    Bankaitis, V.3
  • 38
    • 0029045576 scopus 로고
    • Mutant rat phosphatidylinositol/phosphatidylcholine transfer proteins specifically defective in phosphatidylinositol transfer: Implications for the regulation of phospholipid transfer activity
    • Alb J.G. Jr., Gedvilaite A., Cartee R.T., Skinner H.B., Bankaitis V.A. Mutant rat phosphatidylinositol/phosphatidylcholine transfer proteins specifically defective in phosphatidylinositol transfer: implications for the regulation of phospholipid transfer activity. Proc. Natl. Acad. Sci. U. S. A. 92:1995;8826-8830
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8826-8830
    • Alb Jr., J.G.1    Gedvilaite, A.2    Cartee, R.T.3    Skinner, H.B.4    Bankaitis, V.A.5
  • 39
    • 0034647526 scopus 로고    scopus 로고
    • The protein kinase C-dependent phosphorylation of serine 166 is controlled by the phospholipid species bound to the phosphatidylinositol transfer protein alpha
    • van Tiel C.M., Westerman J., Paasman M., Wirtz K.W., Snoek G.T. The protein kinase C-dependent phosphorylation of serine 166 is controlled by the phospholipid species bound to the phosphatidylinositol transfer protein alpha. J. Biol. Chem. 275:2000;21532-21538
    • (2000) J. Biol. Chem. , vol.275 , pp. 21532-21538
    • Van Tiel, C.M.1    Westerman, J.2    Paasman, M.3    Wirtz, K.W.4    Snoek, G.T.5
  • 40
    • 0037151111 scopus 로고    scopus 로고
    • The Golgi localization of phosphatidylinositol transfer protein beta requires the protein kinase C-dependent phosphorylation of serine 262 and is essential for maintaining plasma membrane sphingomyelin levels
    • van Tiel C.M., Westerman J., Paasman M.A., Hoebens M.M., Wirtz K.W., Snoek G.T. The Golgi localization of phosphatidylinositol transfer protein beta requires the protein kinase C-dependent phosphorylation of serine 262 and is essential for maintaining plasma membrane sphingomyelin levels. J. Biol. Chem. 277:2002;22447-22452
    • (2002) J. Biol. Chem. , vol.277 , pp. 22447-22452
    • Van Tiel, C.M.1    Westerman, J.2    Paasman, M.A.3    Hoebens, M.M.4    Wirtz, K.W.5    Snoek, G.T.6
  • 41
    • 0036565983 scopus 로고    scopus 로고
    • Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association
    • Schouten A., Agianian B., Westerman J., Kroon J., Wirtz K.W., Gros P. Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association. EMBO J. 21:2002;2117-2121
    • (2002) EMBO J. , vol.21 , pp. 2117-2121
    • Schouten, A.1    Agianian, B.2    Westerman, J.3    Kroon, J.4    Wirtz, K.W.5    Gros, P.6
  • 42
    • 0035937732 scopus 로고    scopus 로고
    • Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine
    • Yoder M.D., Thomas L.M., Tremblay J.M., Oliver R.L., Yarbrough L.R., Helmkamp G.M. Jr. Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine. J. Biol. Chem. 276:2001;9246-9252
    • (2001) J. Biol. Chem. , vol.276 , pp. 9246-9252
    • Yoder, M.D.1    Thomas, L.M.2    Tremblay, J.M.3    Oliver, R.L.4    Yarbrough, L.R.5    Helmkamp Jr., G.M.6
  • 43
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • Liljedahl M., Maeda Y., Colanzi A., Ayala I., Van Lint J., Malhotra V. Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell. 104:2001;409-420
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    Van Lint, J.5    Malhotra, V.6
  • 44
    • 0033063819 scopus 로고    scopus 로고
    • Mammalian phosphatidylinositol transfer proteins: Emerging roles in signal transduction and vesicular traffic
    • Cockcroft S. Mammalian phosphatidylinositol transfer proteins: emerging roles in signal transduction and vesicular traffic. Chem. Phys. Lipids. 98:1999;23-33
    • (1999) Chem. Phys. Lipids , vol.98 , pp. 23-33
    • Cockcroft, S.1
  • 45
    • 0032077354 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins: A requirement in signal transduction and vesicle traffic
    • Cockcroft S. Phosphatidylinositol transfer proteins: a requirement in signal transduction and vesicle traffic. BioEssays. 20:1998;423-432
    • (1998) BioEssays , vol.20 , pp. 423-432
    • Cockcroft, S.1
  • 46
    • 0034158024 scopus 로고    scopus 로고
    • Lipid metabolism and regulation of membrane trafficking
    • Huijbregts R.P., Topalof L., Bankaitis V.A. Lipid metabolism and regulation of membrane trafficking. Traffic. 1:2000;195-202
    • (2000) Traffic , vol.1 , pp. 195-202
    • Huijbregts, R.P.1    Topalof, L.2    Bankaitis, V.A.3
  • 47
    • 0024518932 scopus 로고
    • The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
    • Bankaitis V.A., Malehorn D.E., Emr S.D., Greene R. The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. J. Cell Biol. 108:1989;1271-1281
    • (1989) J. Cell Biol. , vol.108 , pp. 1271-1281
    • Bankaitis, V.A.1    Malehorn, D.E.2    Emr, S.D.3    Greene, R.4
  • 48
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis V.A., Aitken J.R., Cleves A.E., Dowhan W. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature. 347:1990;561-562
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 49
    • 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., Emr S.D. Distinct roles for the yeast phosphatidylinositol 4-kinases, Stt4p and Pik1p, in secretion, cell growth, and organelle membrane dynamics. Mol. Biol. Cell. 11:2000;2673-2689
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2673-2689
    • Audhya, A.1    Foti, M.2    Emr, S.D.3
  • 50
    • 0037127301 scopus 로고    scopus 로고
    • Multiple roles for phosphatidylinositol 4-kinase in biosynthetic transport in polarized Madin-Darby canine kidney cells
    • Bruns J.R., Ellis M.A., Jeromin A., Weisz O.A. Multiple roles for phosphatidylinositol 4-kinase in biosynthetic transport in polarized Madin-Darby canine kidney cells. J. Biol. Chem. 277:2002;2012-2018
    • (2002) J. Biol. Chem. , vol.277 , pp. 2012-2018
    • Bruns, J.R.1    Ellis, M.A.2    Jeromin, A.3    Weisz, O.A.4
  • 52
    • 0028890858 scopus 로고
    • Signal transduction. Phospholipids in action
    • Hurley J.B. Signal transduction. Phospholipids in action. Nature. 373:1995;194-195
    • (1995) Nature , vol.373 , pp. 194-195
    • Hurley, J.B.1
  • 53
    • 0030051943 scopus 로고    scopus 로고
    • The biology of vision of Drosophila
    • Zuker C.S. The biology of vision of Drosophila. Proc. Natl. Acad. Sci. U. S. A. 93:1996;571-576
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 571-576
    • Zuker, C.S.1
  • 55
    • 0027954911 scopus 로고
    • A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes
    • McGee T.P., Skinner H.B., Whitters E.A., Henry S.A., Bankaitis V.A. A phosphatidylinositol transfer protein controls the phosphatidylcholine content of yeast Golgi membranes. J. Cell Biol. 124:1994;273-287
    • (1994) J. Cell Biol. , vol.124 , pp. 273-287
    • McGee, T.P.1    Skinner, H.B.2    Whitters, E.A.3    Henry, S.A.4    Bankaitis, V.A.5
  • 56
    • 0028906430 scopus 로고
    • The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity
    • Skinner H.B., McGee T.P., McMaster C.R., Fry M.R., Bell R.M., Bankaitis V.A. The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity. Proc. Natl. Acad. Sci. U. S. A. 92:1995;112-116
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 112-116
    • Skinner, H.B.1    McGee, T.P.2    McMaster, C.R.3    Fry, M.R.4    Bell, R.M.5    Bankaitis, V.A.6
  • 58
    • 0037059448 scopus 로고    scopus 로고
    • Cell biology. Slick recruitment to the Golgi
    • Bankaitis V.A. Cell biology. Slick recruitment to the Golgi. Science. 295:2002;290-291
    • (2002) Science , vol.295 , pp. 290-291
    • Bankaitis, V.A.1
  • 59
    • 0038644177 scopus 로고    scopus 로고
    • Light adaptation through phosphoinositide-regulated translocation of Drosophila visual arrestin
    • Lee S.J., Xu H., Kang L.W., Amzel L.M., Montell C. Light adaptation through phosphoinositide-regulated translocation of Drosophila visual arrestin. Neuron. 39:2003;121-132
    • (2003) Neuron , vol.39 , pp. 121-132
    • Lee, S.J.1    Xu, H.2    Kang, L.W.3    Amzel, L.M.4    Montell, C.5
  • 60
    • 0029148242 scopus 로고
    • A VAMP-binding protein from Aplysia required for neurotransmitter release
    • Skehel P.A., Martin K.C., Kandel E.R., Bartsch D. A VAMP-binding protein from Aplysia required for neurotransmitter release. Science. 269:1995;1580-1583
    • (1995) Science , vol.269 , pp. 1580-1583
    • Skehel, P.A.1    Martin, K.C.2    Kandel, E.R.3    Bartsch, D.4
  • 63
    • 0032528227 scopus 로고    scopus 로고
    • Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): A broadly expressed protein that binds to VAMP
    • Weir M.L., Klip A., Trimble W.S. Identification of a human homologue of the vesicle-associated membrane protein (VAMP)-associated protein of 33 kDa (VAP-33): a broadly expressed protein that binds to VAMP. Biochem. J. 333:1998;247-251
    • (1998) Biochem. J. , vol.333 , pp. 247-251
    • Weir, M.L.1    Klip, A.2    Trimble, W.S.3
  • 64
    • 0031898053 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism
    • Kagiwada S., Hosaka K., Murata M., Nikawa J., Takatsuki A. The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin- associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism. J. Bacteriol. 180:1998;1700-1708
    • (1998) J. Bacteriol. , vol.180 , pp. 1700-1708
    • Kagiwada, S.1    Hosaka, K.2    Murata, M.3    Nikawa, J.4    Takatsuki, A.5
  • 65
    • 0037907626 scopus 로고    scopus 로고
    • Role of the yeast VAP homolog, Scs2p, in INO1 expression and phospholipid metabolism
    • Kagiwada S., Zen R. Role of the yeast VAP homolog, Scs2p, in INO1 expression and phospholipid metabolism. J. Biochem. (Tokyo). 133:2003;515-522
    • (2003) J. Biochem. (Tokyo) , vol.133 , pp. 515-522
    • Kagiwada, S.1    Zen, R.2
  • 66
    • 0036293678 scopus 로고    scopus 로고
    • Nir2, a human homolog of Drosophila melanogaster retinal degeneration B protein, is essential for cytokinesis
    • Litvak V., Tian D., Carmon S., Lev S. Nir2, a human homolog of Drosophila melanogaster retinal degeneration B protein, is essential for cytokinesis. Mol. Cell. Biol. 22:2002;5064-5075
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5064-5075
    • Litvak, V.1    Tian, D.2    Carmon, S.3    Lev, S.4
  • 67
    • 0036898535 scopus 로고    scopus 로고
    • Cytokinesis: Rho and formins are the ringleaders
    • Huckaba T.M., Pon L.A. Cytokinesis: rho and formins are the ringleaders. Curr. Biol. 12:2002;R813-R814
    • (2002) Curr. Biol. , vol.12
    • Huckaba, T.M.1    Pon, L.A.2
  • 69
    • 0035735822 scopus 로고    scopus 로고
    • The pebble GTP exchange factor and the control of cytokinesis
    • O'Keefe L., Somers W.G., Harley A., Saint R. The pebble GTP exchange factor and the control of cytokinesis. Cell Struct. Funct. 26:2001;619-626
    • (2001) Cell Struct. Funct. , vol.26 , pp. 619-626
    • O'Keefe, L.1    Somers, W.G.2    Harley, A.3    Saint, R.4
  • 72
    • 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., Fuller M.T. A phospholipid kinase regulates actin organization and intercellular bridge formation during germline cytokinesis. Development. 127:2000;2864-3855
    • (2000) Development , vol.127 , pp. 2864-3855
    • Brill, J.A.1    Hime, G.R.2    Scharer-Schuksz, M.3    Fuller, M.T.4
  • 73
    • 0031932924 scopus 로고    scopus 로고
    • Regulation of inositol lipid kinases by Rho and Rac
    • Ren X.D., Schwartz M.A. Regulation of inositol lipid kinases by Rho and Rac. Curr. Opin. Genet. Dev. 8:1998;63-67
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 63-67
    • Ren, X.D.1    Schwartz, M.A.2
  • 74
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias K.F., Cantley L.C., Carpenter C.L. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270:1995;17656-17659
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 75
    • 0030001638 scopus 로고    scopus 로고
    • Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
    • Ren X.D., Bokoch G.M., Traynor-Kaplan A., Jenkins G.H., Anderson R.A., Schwartz M.A. Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol. Biol. Cell. 7:1996;435-442
    • (1996) Mol. Biol. Cell , vol.7 , pp. 435-442
    • Ren, X.D.1    Bokoch, G.M.2    Traynor-Kaplan, A.3    Jenkins, G.H.4    Anderson, R.A.5    Schwartz, M.A.6
  • 76
    • 0034687212 scopus 로고    scopus 로고
    • Microtubules, membranes and cytokinesis
    • Straight A.F., Field C.M. Microtubules, membranes and cytokinesis. Curr. Biol. 10:2000;R760-R770
    • (2000) Curr. Biol. , vol.10
    • Straight, A.F.1    Field, C.M.2
  • 77
    • 0034575968 scopus 로고    scopus 로고
    • Membrane traffic and cytokinesis
    • O'Halloran T.J. Membrane traffic and cytokinesis. Traffic. 1:2000;921-926
    • (2000) Traffic , vol.1 , pp. 921-926
    • O'Halloran, T.J.1
  • 78
    • 0037155686 scopus 로고    scopus 로고
    • Fusion and fission: Membrane trafficking in animal cytokinesis
    • Finger F.P., White J.G. Fusion and fission: membrane trafficking in animal cytokinesis. Cell. 108:2002;727-730
    • (2002) Cell , vol.108 , pp. 727-730
    • Finger, F.P.1    White, J.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.