메뉴 건너뛰기




Volumn 287, Issue 3, 2012, Pages 2221-2236

Yeast lipin 1 orthologue Pah1p regulates vacuole homeostasis and membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTATION; DEPHOSPHORYLATIONS; DIACYLGLYCEROL; LATE ENDOSOMES; MEMBRANE FUSION; METABOLIC PATHWAYS; PHOSPHATASE ACTIVITY; PHOSPHATIDIC ACIDS; PHOSPHATIDYLINOSITOL 3 PHOSPHATES; PHOSPHATIDYLINOSITOL 3-KINASE; PROTEIN SORTING; VACUOLE FUSION; WILD TYPES;

EID: 84862909319     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.317420     Document Type: Article
Times cited : (79)

References (77)
  • 1
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • DOI 10.1146/annurev.biochem.68.1.863
    • Jahn, R., and Südhof, T. C. (1999) Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911, (Pubitemid 29449211)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 2
    • 11244258475 scopus 로고    scopus 로고
    • Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
    • DOI 10.1083/jcb.200409068
    • Fratti, R. A., Jun, Y., Merz, A. J., Margolis, N., and Wickner, W. (2004) Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles. J. Cell Biol. 167, 1087-1098 (Pubitemid 40066624)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 1087-1098
    • Fratti, R.A.1    Jun, Y.2    Merz, A.J.3    Margolis, N.4    Wickner, W.5    Wickner, B.6
  • 3
    • 11144240474 scopus 로고    scopus 로고
    • Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion
    • DOI 10.1074/jbc.M411363200
    • Jun, Y., Fratti, R. A., and Wickner, W. (2004) Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion. J. Biol. Chem. 279, 53186-53195 (Pubitemid 40051821)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53186-53195
    • Jun, Y.1    Fratti, R.A.2    Wickner, W.3
  • 4
    • 0035423116 scopus 로고    scopus 로고
    • Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion
    • DOI 10.1093/emboj/20.15.4035
    • Kato, M., and Wickner, W. (2001) Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion. EMBO J. 20, 4035-4040 (Pubitemid 32751820)
    • (2001) EMBO Journal , vol.20 , Issue.15 , pp. 4035-4040
    • Kato, M.1    Wickner, W.2
  • 5
    • 0036544561 scopus 로고    scopus 로고
    • A cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion
    • DOI 10.1083/jcb.200112098
    • Boeddinghaus, C., Merz, A. J., Laage, R., and Ungermann, C. (2002)Acycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion. J. Cell Biol. 157, 79-89 (Pubitemid 34847831)
    • (2002) Journal of Cell Biology , vol.157 , Issue.1 , pp. 79-89
    • Boeddinghaus, C.1    Merz, A.J.2    Laage, R.3    Ungermann, C.4
  • 6
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles
    • DOI 10.1016/S0092-8674(00)81084-3
    • Mayer, A., Wickner, W., and Haas, A. (1996) Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94 (Pubitemid 26116809)
    • (1996) Cell , vol.85 , Issue.1 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 7
    • 0028788311 scopus 로고
    • The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance
    • Haas, A., Scheglmann, D., Lazar, T., Gallwitz, D., and Wickner, W. (1995) The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance. EMBO J. 14, 5258-5270
    • (1995) EMBO J. , vol.14 , pp. 5258-5270
    • Haas, A.1    Scheglmann, D.2    Lazar, T.3    Gallwitz, D.4    Wickner, W.5
  • 8
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • DOI 10.1083/jcb.136.2.307
    • Mayer, A., and Wickner, W. (1997) Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J. Cell Biol. 136, 307-317 (Pubitemid 27063081)
    • (1997) Journal of Cell Biology , vol.136 , Issue.2 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 9
    • 33646128965 scopus 로고    scopus 로고
    • Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
    • Stroupe, C., Collins, K. M., Fratti, R. A., and Wickner, W. (2006) Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J. 25, 1579-1589
    • (2006) EMBO J. , vol.25 , pp. 1579-1589
    • Stroupe, C.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4
  • 10
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann, C., Sato, K., and Wickner, W. (1998) Defining the functions of trans-SNARE pairs. Nature 396, 543-558
    • (1998) Nature , vol.396 , pp. 543-558
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 11
    • 1642539980 scopus 로고    scopus 로고
    • 2+ efflux from the yeast vacuole lumen
    • 2+ efflux from the yeast vacuole lumen. J. Cell Biol. 164, 195-206
    • (2004) J. Cell Biol. , vol.164 , pp. 195-206
    • Merz, A.J.1    Wickner, W.2
  • 12
    • 0036180245 scopus 로고    scopus 로고
    • Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
    • DOI 10.1016/S0092-8674(02)00632-3
    • Wang, L., Seeley, E. S., Wickner, W., and Merz, A. J. (2002) Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell 108, 357-369 (Pubitemid 34178400)
    • (2002) Cell , vol.108 , Issue.3 , pp. 357-369
    • Wang, L.1    Seeley, E.S.2    Wickner, W.3    Merz, A.J.4
  • 13
    • 0037415612 scopus 로고    scopus 로고
    • Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion
    • DOI 10.1083/jcb.200209095
    • Wang, L., Merz, A. J., Collins, K. M., and Wickner, W. (2003) Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J. Cell Biol. 160, 365-374 (Pubitemid 36182727)
    • (2003) Journal of Cell Biology , vol.160 , Issue.3 , pp. 365-374
    • Wang, L.1    Merz, A.J.2    Collins, K.M.3    Wickner, W.4
  • 14
    • 0034019904 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulates two steps of homotypic vacuole fusion
    • Mayer, A., Scheglmann, D., Dove, S., Glatz, A., Wickner, W., and Haas, A. (2000) Phosphatidylinositol 4,5-bisphosphate regulates two steps of homotypic vacuole fusion. Mol. Biol. Cell 11, 807-817 (Pubitemid 30159303)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.3 , pp. 807-817
    • Mayer, A.1    Scheglmann, D.2    Dove, S.3    Glatz, A.4    Wickner, W.5    Haas, A.6
  • 15
    • 70350433273 scopus 로고    scopus 로고
    • Complex lipid requirements for SNARE- And SNARE chaperone-dependent membrane fusion
    • Mima, J., and Wickner, W. (2009) Complex lipid requirements for SNARE- and SNARE chaperone-dependent membrane fusion. J. Biol. Chem. 284, 27114-27122
    • (2009) J. Biol. Chem. , vol.284 , pp. 27114-27122
    • Mima, J.1    Wickner, W.2
  • 18
    • 1642390110 scopus 로고    scopus 로고
    • Genetic Evidence of a Role for Membrane Lipid Composition in the Regulation of Soluble NEM-Sensitive Factor Receptor Function in Saccharomyces cerevisiae
    • DOI 10.1534/genetics.166.1.89
    • Coluccio, A., Malzone, M., and Neiman, A. M. (2004) Genetic evidence of a role for membrane lipid composition in the regulation of soluble NEM-sensitive factor receptor function in Saccharomyces cerevisiae. Genetics 166, 89-97 (Pubitemid 38364705)
    • (2004) Genetics , vol.166 , Issue.1 , pp. 89-97
    • Coluccio, A.1    Malzone, M.2    Neiman, A.M.3
  • 19
    • 35348819374 scopus 로고    scopus 로고
    • In vitro fusion catalyzed by the sporulation-specific t-sNARE light-chain Spo20p is stimulated by phosphatidic acid
    • DOI 10.1111/j.1600-0854.2007.00628.x
    • Liu, S., Wilson, K. A., Rice-Stitt, T., Neiman, A. M., and McNew, J. A. (2007) In vitro fusion catalyzed by the sporulation-specific t-SNARE light-chain Spo20p is stimulated by phosphatidic acid. Traffic 8, 1630-1643 (Pubitemid 47578366)
    • (2007) Traffic , vol.8 , Issue.11 , pp. 1630-1643
    • Liu, S.1    Wilson, K.A.2    Rice-stitt, T.3    Neiman, A.M.4    Mcnew, J.A.5
  • 20
    • 33750526473 scopus 로고    scopus 로고
    • A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis
    • DOI 10.1038/ncb1487, PII NCB1487
    • Choi, S. Y., Huang, P., Jenkins, G. M., Chan, D. C., Schiller, J., and Frohman, M. A. (2006) A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis. Nat. Cell Biol. 8, 1255-1262 (Pubitemid 44660590)
    • (2006) Nature Cell Biology , vol.8 , Issue.11 , pp. 1255-1262
    • Choi, S.-Y.1    Huang, P.2    Jenkins, G.M.3    Chan, D.C.4    Schiller, J.5    Frohman, M.A.6
  • 23
    • 0035971250 scopus 로고    scopus 로고
    • Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc
    • Han, G. S., Johnston, C. N., Chen, X., Athenstaedt, K., Daum, G., and Carman, G. M. (2001) Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc. J. Biol. Chem. 276, 10126-10133
    • (2001) J. Biol. Chem. , vol.276 , pp. 10126-10133
    • Han, G.S.1    Johnston, C.N.2    Chen, X.3    Athenstaedt, K.4    Daum, G.5    Carman, G.M.6
  • 25
    • 0035163850 scopus 로고    scopus 로고
    • Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin
    • DOI 10.1038/83685
    • Péterfy, M., Phan, J., Xu, P., and Reue, K. (2001) Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin. Nat. Genet. 27, 121-124 (Pubitemid 32044532)
    • (2001) Nature Genetics , vol.27 , Issue.1 , pp. 121-124
    • Peterfy, M.1    Phan, J.2    Xu, P.3    Reue, K.4
  • 27
    • 38049010121 scopus 로고    scopus 로고
    • Association of Lipin 1 gene polymorphisms with measures of energy and glucose metabolism
    • Loos, R. J., Rankinen, T., Pérusse, L., Tremblay, A., Després, J. P., and Bouchard, C. (2007) Association of Lipin 1 gene polymorphisms with measures of energy and glucose metabolism. Obesity 15, 2723-2732
    • (2007) Obesity , vol.15 , pp. 2723-2732
    • Loos, R.J.1    Rankinen, T.2    Pérusse, L.3    Tremblay, A.4    Després, J.P.5    Bouchard, C.6
  • 28
    • 15944375261 scopus 로고    scopus 로고
    • Lipin, a lipodystrophy and obesity gene
    • DOI 10.1016/j.cmet.2004.12.002, PII S1550413104000087
    • Phan, J., and Reue, K. (2005) Lipin, a lipodystrophy and obesity gene. Cell Metab. 1, 73-83 (Pubitemid 43960586)
    • (2005) Cell Metabolism , vol.1 , Issue.1 , pp. 73-83
    • Phan, J.1    Reue, K.2
  • 29
    • 59149106049 scopus 로고    scopus 로고
    • Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis
    • Carman, G. M., and Han, G. S. (2009) Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis. J. Biol. Chem. 284, 2593-2597
    • (2009) J. Biol. Chem. , vol.284 , pp. 2593-2597
    • Carman, G.M.1    Han, G.S.2
  • 30
    • 78651385378 scopus 로고    scopus 로고
    • Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae. Identification of Ser-602, Thr-723, and Ser-744 as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase
    • Choi, H. S., Su, W. M., Morgan, J. M., Han, G. S., Xu, Z., Karanasios, E., Siniossoglou, S., and Carman, G. M. (2011) Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae. Identification of Ser-602, Thr-723, and Ser-744 as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase. J. Biol. Chem. 286, 1486-1498
    • (2011) J. Biol. Chem. , vol.286 , pp. 1486-1498
    • Choi, H.S.1    Su, W.M.2    Morgan, J.M.3    Han, G.S.4    Xu, Z.5    Karanasios, E.6    Siniossoglou, S.7    Carman, G.M.8
  • 31
    • 21244480972 scopus 로고    scopus 로고
    • The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
    • DOI 10.1038/sj.emboj.7600672
    • Santos-Rosa, H., Leung, J., Grimsey, N., Peak-Chew, S., and Siniossoglou, S. (2005) The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J. 24, 1931-1941 (Pubitemid 40896165)
    • (2005) EMBO Journal , vol.24 , Issue.11 , pp. 1931-1941
    • Santos-Rosa, H.1    Leung, J.2    Grimsey, N.3    Peak-Chew, S.4    Siniossoglou, S.5
  • 33
    • 78049319504 scopus 로고    scopus 로고
    • Aphosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase
    • Karanasios, E., Han, G. S., Xu, Z., Carman, G. M., and Siniossoglou, S. (2010)Aphosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase. Proc. Natl. Acad. Sci. U.S.A. 107, 17539-17544
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17539-17544
    • Karanasios, E.1    Han, G.S.2    Xu, Z.3    Carman, G.M.4    Siniossoglou, S.5
  • 36
    • 0030968878 scopus 로고    scopus 로고
    • Homotypic vacuolar fusion mediated by t- and v-SNAREs
    • DOI 10.1038/387199a0
    • Nichols, B. J., Ungermann, C., Pelham, H. R., Wickner, W. T., and Haas, A. (1997) Homotypic vacuolar fusion mediated by t- and v-SNAREs. Nature 387, 199-202 (Pubitemid 27209437)
    • (1997) Nature , vol.387 , Issue.6629 , pp. 199-202
    • Nichols, B.J.1    Ungermann, C.2    Pelham, H.R.B.3    Wickner, W.T.4    Haas, A.5
  • 40
    • 34250327976 scopus 로고    scopus 로고
    • Distinct targeting and fusion functions of the PX and SNARE domains of yeast vacuolar Vam7p
    • DOI 10.1074/jbc.M700584200
    • Fratti, R. A., and Wickner, W. (2007) Distinct targeting and fusion functions of the Phox homology and SNARE domains of yeast vacuolar Vam7p. J. Biol. Chem. 282, 13133-13138 (Pubitemid 47100619)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 13133-13138
    • Fratti, R.A.1    Wickner, W.2
  • 41
    • 34447524098 scopus 로고    scopus 로고
    • Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification
    • DOI 10.1074/jbc.M700971200
    • Fratti, R. A., Collins, K. M., Hickey, C. M., and Wickner, W. (2007) Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. J. Biol. Chem. 282, 14861-14867 (Pubitemid 47093360)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 14861-14867
    • Fratti, R.A.1    Collins, K.M.2    Hickey, C.M.3    Wickner, W.4
  • 42
    • 0020338057 scopus 로고
    • PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae
    • Jones, E. W., Zubenko, G. S., and Parker, R. R. (1982) PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. Genetics 102, 665-677
    • (1982) Genetics , vol.102 , pp. 665-677
    • Jones, E.W.1    Zubenko, G.S.2    Parker, R.R.3
  • 43
    • 0028333056 scopus 로고
    • G-protein ligands inhibit in vitro reactions of vacuole inheritance
    • DOI 10.1083/jcb.126.1.87
    • Haas, A., Conradt, B., and Wickner, W. (1994) G-protein ligands inhibit in vitro reactions of vacuole inheritance. J. Cell Biol. 126, 87-97 (Pubitemid 24214931)
    • (1994) Journal of Cell Biology , vol.126 , Issue.1 , pp. 87-97
    • Haas, A.1    Conradt, B.2    Wickner, W.3
  • 45
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • DOI 10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U
    • Longtine, M. S., McKenzie, A., 3rd, Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J. R. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961 (Pubitemid 28328001)
    • (1998) Yeast , vol.14 , Issue.10 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 46
    • 37549018969 scopus 로고    scopus 로고
    • The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity
    • Han, G. S., Siniossoglou, S., and Carman, G. M. (2007) The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity. J. Biol. Chem. 282, 37026-37035
    • (2007) J. Biol. Chem. , vol.282 , pp. 37026-37035
    • Han, G.S.1    Siniossoglou, S.2    Carman, G.M.3
  • 47
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • DOI 10.1002/(SICI)1097-0061(199910)15:14<1541::AID-YEA476>3.0.CO;2- K
    • Goldstein, A. L., and McCusker, J. H. (1999) Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast 15, 1541-1553 (Pubitemid 29472165)
    • (1999) Yeast , vol.15 , Issue.14 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 48
    • 0031818471 scopus 로고    scopus 로고
    • Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe
    • DOI 10.1002/(SICI)1097-0061(199807)14:10<943::AID-YEA292>3.0.CO;2-Y
    • Bähler, J.,Wu, J. Q., Longtine, M. S., Shah, N. G., McKenzie, A., 3rd, Steever, A. B., Wach, A., Philippsen, P., and Pringle, J. R. (1998) Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe. Yeast 14, 943-951 (Pubitemid 28328000)
    • (1998) Yeast , vol.14 , Issue.10 , pp. 943-951
    • Bahler, J.1    Wu, J.-Q.2    Longtine, M.S.3    Shah, N.G.4    McKenzie III, A.5    Steever, A.B.6    Wach, A.7    Philippsen, P.8    Pringle, J.R.9
  • 49
    • 77956912124 scopus 로고    scopus 로고
    • + exchanger Nhx1p regulates the initiation of Saccharomyces cerevisiae vacuole fusion
    • + exchanger Nhx1p regulates the initiation of Saccharomyces cerevisiae vacuole fusion. J. Cell Sci. 123, 3266-3275
    • (2010) J. Cell Sci. , vol.123 , pp. 3266-3275
    • Qiu, Q.S.1    Fratti, R.A.2
  • 51
    • 0034189787 scopus 로고    scopus 로고
    • A novel pathway for transport and metabolism of a fluorescent phosphatidic acid analog in yeast
    • Trotter, P. J. (2000) A novel pathway for transport and metabolism of a fluorescent phosphatidic acid analog in yeast. Traffic 1, 425-434
    • (2000) Traffic , vol.1 , pp. 425-434
    • Trotter, P.J.1
  • 52
    • 0025894167 scopus 로고
    • Phosphatidate phosphatase from Saccharomyces cerevisiae: Isolation of 45- and 104-kDa forms of the enzyme that are differentially regulated by inositol
    • Morlock, K. R., McLaughlin, J. J., Lin, Y. P., and Carman, G. M. (1991) Phosphatidate phosphatase from Saccharomyces cerevisiae. Isolation of 45- and 104-kDa forms of the enzyme that are differentially regulated by inositol. J. Biol. Chem. 266, 3586-3593 (Pubitemid 21909253)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.6 , pp. 3586-3593
    • Morlock, K.R.1    McLaughlin, J.J.2    Lin, Y.-P.3    Carman, G.M.4
  • 53
    • 0021078203 scopus 로고
    • Propranolol-induced inhibition of rat brain cytoplasmic phosphatidate phosphohydrolase
    • DOI 10.1007/BF00964158
    • Pappu, A. S., and Hauser, G. (1983) Propranolol-induced inhibition of rat brain cytoplasmic phosphatidate phosphohydrolase. Neurochem. Res. 8, 1565-1575 (Pubitemid 14157628)
    • (1983) Neurochemical Research , vol.8 , Issue.12 , pp. 1565-1575
    • Pappu, A.S.1    Hauser, G.2
  • 54
    • 77951979740 scopus 로고    scopus 로고
    • Characterization of the human LPIN1-encoded phosphatidate phosphatase isoforms
    • Han, G. S., and Carman, G. M. (2010) Characterization of the human LPIN1-encoded phosphatidate phosphatase isoforms. J. Biol. Chem. 285, 14628-14638
    • (2010) J. Biol. Chem. , vol.285 , pp. 14628-14638
    • Han, G.S.1    Carman, G.M.2
  • 55
    • 29144520288 scopus 로고    scopus 로고
    • Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusion
    • DOI 10.1083/jcb.200510018
    • Reese, C., and Mayer, A. (2005) Transition from hemifusion to pore opening is rate-limiting for vacuole membrane fusion. J. Cell Biol. 171, 981-990 (Pubitemid 41815830)
    • (2005) Journal of Cell Biology , vol.171 , Issue.6 , pp. 981-990
    • Reese, C.1    Mayer, A.2
  • 56
    • 22944485726 scopus 로고    scopus 로고
    • Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion
    • DOI 10.1038/nature03722
    • Reese, C., Heise, F., and Mayer, A. (2005) Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion. Nature 436, 410-414 (Pubitemid 41059052)
    • (2005) Nature , vol.436 , Issue.7049 , pp. 410-414
    • Reese, C.1    Heise, F.2    Mayer, A.3
  • 57
    • 0346147032 scopus 로고    scopus 로고
    • Detection of apoptotic cells using a synthetic fluorescent sensor for membrane surfaces that contain phosphatidylserine
    • DOI 10.1038/sj.cdd.4401315
    • Koulov, A. V., Stucker, K. A., Lakshmi, C., Robinson, J. P., and Smith, B. D. (2003) Detection of apoptotic cells using a synthetic fluorescent sensor for membrane surfaces that contain phosphatidylserine. Cell Death Differ. 10, 1357-1359 (Pubitemid 37536740)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.12 , pp. 1357-1359
    • Koulov, A.V.1    Stucker, K.A.2    Lakshmi, C.3    Robinson, J.P.4    Smith, B.D.5
  • 58
    • 20044377804 scopus 로고    scopus 로고
    • Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion
    • DOI 10.1038/sj.emboj.7600658
    • Collins, K. M., Thorngren, N. L., Fratti, R. A., and Wickner, W. T. (2005) Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J. 24, 1775-1786 (Pubitemid 40769497)
    • (2005) EMBO Journal , vol.24 , Issue.10 , pp. 1775-1786
    • Collins, K.M.1    Thorngren, N.L.2    Fratti, R.A.3    Wickner, W.T.4
  • 59
    • 0035886714 scopus 로고    scopus 로고
    • Rho1p and Cdc42p act after Ypt7p to regulate vacuole docking
    • DOI 10.1093/emboj/20.20.5650
    • Eitzen, G., Thorngren, N., and Wickner, W. (2001) Rho1p and Cdc42p act after Ypt7p to regulate vacuole docking. EMBO J. 20, 5650-5656 (Pubitemid 33010042)
    • (2001) EMBO Journal , vol.20 , Issue.20 , pp. 5650-5656
    • Eitzen, G.1    Thorngren, N.2    Wickner, W.3
  • 60
    • 0035937773 scopus 로고    scopus 로고
    • Differential binding of traffic-related proteins to phosphatidic acid- Or phosphatidylinositol 4,5-bisphosphate-coupled affinity reagents
    • Manifava, M., Thuring, J. W., Lim, Z. Y., Packman, L., Holmes, A. B., and Ktistakis, N. T. (2001) Differential binding of traffic-related proteins to phosphatidic acid- or phosphatidylinositol 4,5-bisphosphate-coupled affinity reagents. J. Biol. Chem. 276, 8987-8994
    • (2001) J. Biol. Chem. , vol.276 , pp. 8987-8994
    • Manifava, M.1    Thuring, J.W.2    Lim, Z.Y.3    Packman, L.4    Holmes, A.B.5    Ktistakis, N.T.6
  • 61
    • 3542999933 scopus 로고    scopus 로고
    • A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion
    • DOI 10.1038/sj.emboj.7600286
    • Thorngren, N., Collins, K. M., Fratti, R. A., Wickner, W., and Merz, A. J. (2004) A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion. EMBO J. 23, 2765-2776 (Pubitemid 39013549)
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2765-2776
    • Thorngren, N.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4    Merz, A.J.5
  • 62
    • 77956799413 scopus 로고    scopus 로고
    • The interactivities with lipid membranes differentially characterize selective and nonselective beta1-blockers
    • Mizogami, M., Takakura, K., and Tsuchiya, H. (2010) The interactivities with lipid membranes differentially characterize selective and nonselective beta1-blockers. Eur. J. Anaesthesiol. 27, 829-834
    • (2010) Eur. J. Anaesthesiol. , vol.27 , pp. 829-834
    • Mizogami, M.1    Takakura, K.2    Tsuchiya, H.3
  • 63
    • 33751080603 scopus 로고    scopus 로고
    • Reversible, cooperative reactions of yeast vacuole docking
    • DOI 10.1038/sj.emboj.7601413, PII 7601413
    • Jun, Y., Thorngren, N., Starai, V. J., Fratti, R. A., Collins, K., and Wickner, W. (2006) Reversible, cooperative reactions of yeast vacuole docking. EMBO J. 25, 5260-5269 (Pubitemid 44764136)
    • (2006) EMBO Journal , vol.25 , Issue.22 , pp. 5260-5269
    • Jun, Y.1    Thorngren, N.2    Starai, V.J.3    Fratti, R.A.4    Collins, K.5    Wickner, W.6
  • 64
    • 67749120188 scopus 로고    scopus 로고
    • Helical extension of the neuronal SNARE complex into the membrane
    • Stein, A., Weber, G., Wahl, M. C., and Jahn, R. (2009) Helical extension of the neuronal SNARE complex into the membrane. Nature 460, 525-528
    • (2009) Nature , vol.460 , pp. 525-528
    • Stein, A.1    Weber, G.2    Wahl, M.C.3    Jahn, R.4
  • 65
    • 34247568898 scopus 로고    scopus 로고
    • The CORVET Tethering Complex Interacts with the Yeast Rab5 Homolog Vps21 and Is Involved in Endo-Lysosomal Biogenesis
    • DOI 10.1016/j.devcel.2007.03.006, PII S1534580707001062
    • Peplowska, K., Markgraf, D. F., Ostrowicz, C. W., Bange, G., and Ungermann, C. (2007) The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev. Cell 12, 739-750 (Pubitemid 46667746)
    • (2007) Developmental Cell , vol.12 , Issue.5 , pp. 739-750
    • Peplowska, K.1    Markgraf, D.F.2    Ostrowicz, C.W.3    Bange, G.4    Ungermann, C.5
  • 66
    • 77951918362 scopus 로고    scopus 로고
    • Identification of the switch in early-to-late endosome transition
    • Poteryaev, D., Datta, S., Ackema, K., Zerial, M., and Spang, A. (2010) Identification of the switch in early-to-late endosome transition. Cell 141, 497-508
    • (2010) Cell , vol.141 , pp. 497-508
    • Poteryaev, D.1    Datta, S.2    Ackema, K.3    Zerial, M.4    Spang, A.5
  • 67
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • DOI 10.1016/j.cell.2005.06.043, PII S0092867405006975
    • Rink, J., Ghigo, E., Kalaidzidis, Y., and Zerial, M. (2005) Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735-749 (Pubitemid 41242638)
    • (2005) Cell , vol.122 , Issue.5 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 68
    • 70149084564 scopus 로고    scopus 로고
    • A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway
    • Rivera-Molina, F. E., and Novick, P. J. (2009) A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway. Proc. Natl. Acad. Sci. U.S.A. 106, 14408-14413
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14408-14413
    • Rivera-Molina, F.E.1    Novick, P.J.2
  • 70
    • 0034735539 scopus 로고    scopus 로고
    • New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
    • Wurmser, A. E., Sato, T. K., and Emr, S. D. (2000) New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J. Cell Biol. 151, 551-562
    • (2000) J. Cell Biol. , vol.151 , pp. 551-562
    • Wurmser, A.E.1    Sato, T.K.2    Emr, S.D.3
  • 71
    • 77950460749 scopus 로고    scopus 로고
    • Identification of two evolutionarily conserved genes regulating processing of engulfed apoptotic cells
    • Kinchen, J. M., and Ravichandran, K. S. (2010) Identification of two evolutionarily conserved genes regulating processing of engulfed apoptotic cells. Nature 464, 778-782
    • (2010) Nature , vol.464 , pp. 778-782
    • Kinchen, J.M.1    Ravichandran, K.S.2
  • 72
    • 0033202945 scopus 로고    scopus 로고
    • Rab5 regulates motility of early endosomes on microtubules
    • Nielsen, E., Severin, F., Backer, J. M., Hyman, A. A., and Zerial, M. (1999) Rab5 regulates motility of early endosomes on microtubules. Nat. Cell Biol. 1, 376-382 (Pubitemid 129493581)
    • (1999) Nature Cell Biology , vol.1 , Issue.6 , pp. 376-382
    • Nielsen, E.1    Severin, F.2    Backer, J.M.3    Hyman, A.A.4    Zerial, M.5
  • 73
    • 33845286562 scopus 로고    scopus 로고
    • G protein signaling in yeast: New components, new connections, new compartments
    • DOI 10.1126/science.1134041
    • Slessareva, J. E., and Dohlman, H. G. (2006) G protein signaling in yeast. New components, new connections, new compartments. Science 314, 1412-1413 (Pubitemid 44871938)
    • (2006) Science , vol.314 , Issue.5804 , pp. 1412-1413
    • Slessareva, J.E.1    Dohlman, H.G.2
  • 74
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase y sorting in Saccharomyces cerevisiae
    • Kihara, A., Noda, T., Ishihara, N., and Ohsumi, Y. (2001) Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J. Cell Biol. 152, 519-530 (Pubitemid 34280235)
    • (2001) Journal of Cell Biology , vol.153 , Issue.3 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 76
    • 77953608974 scopus 로고    scopus 로고
    • HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion
    • Xu, H., Jun, Y., Thompson, J., Yates, J., and Wickner, W. (2010) HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion. EMBO J. 29, 1948-1960
    • (2010) EMBO J. , vol.29 , pp. 1948-1960
    • Xu, H.1    Jun, Y.2    Thompson, J.3    Yates, J.4    Wickner, W.5
  • 77
    • 78649821097 scopus 로고    scopus 로고
    • Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly
    • Xu, H., and Wickner, W. (2010) Phosphoinositides function asymmetrically for membrane fusion, promoting tethering and 3Q-SNARE subcomplex assembly. J. Biol. Chem. 285, 39359-39365
    • (2010) J. Biol. Chem. , vol.285 , pp. 39359-39365
    • Xu, H.1    Wickner, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.