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Volumn 53, Issue 3, 2012, Pages 522-528

Fluorescence spectroscopy measures yeast PAH1 -encoded phosphatidate phosphatase interaction with liposome membranes

Author keywords

Liposomes; Phospholipid; Triacylglycerol; Yeast

Indexed keywords

CASEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; FUNGAL ENZYME; LIPOSOME; PHOSPHATIDATE PHOSPHATASE; PHOSPHATIDATE PHOSPHATASE PAH1; PHOSPHATIDYLCHOLINE; PROTEIN KINASE C; UNCLASSIFIED DRUG;

EID: 84863229917     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M022798     Document Type: Article
Times cited : (27)

References (43)
  • 1
    • 59149106049 scopus 로고    scopus 로고
    • Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis
    • Carman, G. M., and G-S. Han. 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
  • 2
    • 0000456009 scopus 로고
    • The enzymatic dephosphorylation of phosphatidic acids
    • Smith, S. W., S. B. Weiss, and E. P. Kennedy. 1957. The enzymatic dephosphorylation of phosphatidic acids. J. Biol. Chem. 228: 915-922.
    • (1957) J. Biol. Chem. , vol.228 , pp. 915-922
    • Smith, S.W.1    Weiss, S.B.2    Kennedy, E.P.3
  • 3
    • 33646920976 scopus 로고    scopus 로고
    • 2+-dependent phosphatidate phosphatase enzyme
    • DOI 10.1074/jbc.M600425200
    • Han, G-S., W-I. Wu, and G. M. Carman. 2006. The Saccharomyces cerevisiae lipin homolog is a Mg 2+ -dependent phosphatidate phosphatase enzyme. J. Biol. Chem. 281:9210-9218. (Pubitemid 43864636)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9210-9218
    • Han, G.-S.1    Wu, W.-I.2    Carman, G.M.3
  • 4
    • 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., J. Phan, P. Xu, and K. Reue. 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
  • 5
    • 15944375261 scopus 로고    scopus 로고
    • Lipin, a lipodystrophy and obesity gene
    • DOI 10.1016/j.cmet.2004.12.002, PII S1550413104000087
    • Phan, J., and K. Reue. 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
  • 6
    • 33947542353 scopus 로고    scopus 로고
    • Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns
    • DOI 10.1074/jbc.M610745200
    • Donkor, J., M. Sariahmetoglu, J. Dewald, D. N. Brindley, and K. Reue. 2007. Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns. J. Biol. Chem. 282: 3450-3457. (Pubitemid 47084457)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 3450-3457
    • Donkor, J.1    Sariahmetoglu, M.2    Dewald, J.3    Brindley, D.N.4    Reue, K.5
  • 7
    • 37549018969 scopus 로고    scopus 로고
    • The cellular functions of the yeast lipin homolog Pah1p are dependent on its phosphatidate phosphatase activity
    • Han, G. S., S. Siniossoglou, and G. M. Carman. 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
  • 8
    • 79959457450 scopus 로고    scopus 로고
    • Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae
    • Carman, G. M., and G-S. Han. 2011. Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae. Annu. Rev. Biochem. 80: 859-883.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 859-883
    • Carman, G.M.1    Han, G.-S.2
  • 9
    • 38049110718 scopus 로고    scopus 로고
    • Phosphatidic acid plays a central role in the transcriptional regulation of glycerophospholipid synthesis in Saccharomyces cerevisiae
    • Carman, G. M., and S. A. Henry. 2007. Phosphatidic acid plays a central role in the transcriptional regulation of glycerophospholipid synthesis in Saccharomyces cerevisiae. J. Biol. Chem. 282: 37293-37297.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37293-37297
    • Carman, G.M.1    Henry, S.A.2
  • 10
    • 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., J. Leung, N. Grimsey, S. Peak-Chew, and S. Siniossoglou. 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
  • 12
    • 80051695513 scopus 로고    scopus 로고
    • Phosphatidate phosphatase activity plays a key role in protection against fatty acid-induced toxicity in yeast
    • Fakas, S., Y. Qiu, J. L. Dixon, G. S. Han, K. V. Ruggles, J. Garbarino, S. L. Sturley, and G. M. Carman. 2011. Phosphatidate phosphatase activity plays a key role in protection against fatty acid-induced toxicity in yeast. J. Biol. Chem. 286:29074-29085.
    • (2011) J. Biol. Chem. , vol.286 , pp. 29074-29085
    • Fakas, S.1    Qiu, Y.2    Dixon, J.L.3    Han, G.S.4    Ruggles, K.V.5    Garbarino, J.6    Sturley, S.L.7    Carman, G.M.8
  • 13
    • 0025951848 scopus 로고
    • Characterization of the peripheral neuropathy in neonatal and adult mice that are homozygous for the fatty liver dystrophy (fld) mutation
    • Langner, C. A., E. H. Birkenmeier, K. A. Roth, R. T. Bronson, and J. I. Gordon. 1991. Characterization of the peripheral neuropathy in neonatal and adult mice that are homozygous for the fatty liver dystrophy (fld) mutation. J. Biol. Chem. 266:11955-11964. (Pubitemid 21907042)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.18 , pp. 11955-11964
    • Langner, C.A.1    Birkenmeier, E.H.2    Roth, K.A.3    Bronson, R.T.4    Gordon, J.I.5
  • 14
    • 0024399652 scopus 로고
    • The fatty liver dystrophy (fld) mutation. A new mutant mouse with a developmental abnormality in triglyceride metabolism and associated tissue-specific defects in lipoprotein lipase and hepatic lipase activities
    • Langner, C. A., E. H. Birkenmeier, O. Ben-Zeev, M. C. Schotz, H. O. Sweet, M. T. Davisson, and J. I. Gordon. 1989. The fatty liver dystrophy (fld) mutation. A new mutant mouse with a developmental abnormality in triglyceride metabolism and associated tissue-specific defects in lipoprotein lipase and hepatic lipase activities. J. Biol. Chem. 264:7994-8003. (Pubitemid 19137280)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.14 , pp. 7994-8003
    • Langner, C.A.1    Birkenmeier, E.H.2    Ben-Zeev, O.3    Schotz, M.C.4    Sweet, H.O.5    Davisson, M.T.6    Gordon, J.I.7
  • 17
    • 36849000320 scopus 로고    scopus 로고
    • Genetic factors in type 2 diabetes: all in the (Lipin) family
    • DOI 10.2337/db07-1288
    • Reue, K., and J. Donkor. 2007. Genetic factors in type 2 diabetes: all in the (lipin) family. Diabetes. 56:2842-2843. (Pubitemid 350223615)
    • (2007) Diabetes , vol.56 , Issue.12 , pp. 2842-2843
    • Reue, K.1    Donkor, J.2
  • 18
    • 59649088176 scopus 로고    scopus 로고
    • Multiple roles for lipins/phosphatidate phosphatase enzymes in lipid metabolism
    • Reue, K., and D. N. Brindley. 2008. Multiple roles for lipins/phosphatidate phosphatase enzymes in lipid metabolism. J. Lipid Res. 49:2493-2503.
    • (2008) J. Lipid Res. , vol.49 , pp. 2493-2503
    • Reue, K.1    Brindley, D.N.2
  • 19
    • 84863494132 scopus 로고    scopus 로고
    • Lipin proteins and metabolic homeostasis
    • Reue, K., and J. R. Dwyer. 2009. Lipin proteins and metabolic homeostasis. J. Lipid Res. 50(Suppl):S109-S114.
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Reue, K.1    Dwyer, J.R.2
  • 20
    • 70350399460 scopus 로고    scopus 로고
    • A conserved serine residue is required for the phosphatidate phosphatase activity but not transcriptional coactivator functions of lipin-1 and lipin-2
    • Donkor, J., P. Zhang, S. Wong, L. O'Loughlin, J. Dewald, B. P. Kok, D. N. Brindley, and K. Reue. 2009. A conserved serine residue is required for the phosphatidate phosphatase activity but not transcriptional coactivator functions of lipin-1 and lipin-2. J. Biol. Chem. 284:29968-29978.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29968-29978
    • Donkor, J.1    Zhang, P.2    Wong, S.3    O'Loughlin, L.4    Dewald, J.5    Kok, B.P.6    Brindley, D.N.7    Reue, K.8
  • 21
    • 0021566523 scopus 로고
    • Intracellular translocation of phosphatidate phosphohydrolase and its possible role in the control of glycerolipid synthesis
    • Brindley, D. N. 1984. Intracellular translocation of phosphatidate phosphohydrolase and its possible role in the control of glycerolipid synthesis. Prog. Lipid Res. 23:115-133.
    • (1984) Prog. Lipid Res. , vol.23 , pp. 115-133
    • Brindley, D.N.1
  • 22
    • 33846975789 scopus 로고    scopus 로고
    • Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1
    • DOI 10.1074/jbc.M609537200
    • Harris, T. E., T. A. Huffman, A. Chi, J. Shabanowitz, D. F. Hunt, A. Kumar, and J. C. Lawrence, Jr. 2007. Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, Lipin 1. J. Biol. Chem. 282:277-286. (Pubitemid 47076630)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.1 , pp. 277-286
    • Harris, T.E.1    Huffman, T.A.2    Chi, A.3    Shabanowitz, J.4    Hunt, D.F.5    Kumar, A.6    Lawrence Jr., J.C.7
  • 23
    • 78049319504 scopus 로고    scopus 로고
    • A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase
    • Karanasios, E., G-S. Han, Z. Xu, G. M. Carman, and S. Siniossoglou. 2010. A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase. Proc. Natl. Acad. Sci. USA. 107:17539-17544.
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 17539-17544
    • Karanasios, E.1    Han, G.-S.2    Xu, Z.3    Carman, G.M.4    Siniossoglou, S.5
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227: 680-685.
    • (1970) Nature. , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0021010421 scopus 로고
    • Immunochemical identification of membrane proteins after sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Haid, A., and M. Suissa. 1983. Immunochemical identification of membrane proteins after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Methods Enzymol. 96:192-205.
    • (1983) Methods Enzymol. , vol.96 , pp. 192-205
    • Haid, A.1    Suissa, M.2
  • 29
    • 0014713811 scopus 로고
    • Etude des conversions mitotiques au niveau du gene ad-9 de schizosaccharomyces pombe
    • Adondi, G., and H. Heslot. 1970. Etude des conversions mitotiques au niveau du gene ad-9 de schizosaccharomyces pombe. Mutat. Res. 9:41-58.
    • (1970) Mutat. Res. , vol.9 , pp. 41-58
    • Adondi, G.1    Heslot, H.2
  • 30
    • 77951979740 scopus 로고    scopus 로고
    • Characterization of the human LPIN1-encoded phosphatidate phosphatase isoforms
    • Han, G-S., and G. M. Carman. 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
  • 31
    • 0018349895 scopus 로고
    • The behavior of oxonol dyes in phospholipid dispersions
    • Bashford, C. L., B. Chance, J. C. Smith, and T. Yoshida. 1979. The behavior of oxonol dyes in phospholipid dispersions. Biophys. J. 25: 63-85. (Pubitemid 9107847)
    • (1979) Biophysical Journal , vol.25 , Issue.1 , pp. 63-85
    • Bashford, C.L.1    Chance, B.2    Smith, J.C.3    Yoshida, T.4
  • 32
    • 0030725122 scopus 로고    scopus 로고
    • Interaction of the delta-endotoxin CytA from Bacillus thuringiensis var. israelensis with lipid membranes
    • DOI 10.1021/bi9702389
    • Butko, P., F. Huang, M. Pusztai-Carey, and W. K. Surewicz. 1997. Interaction of the delta-endotoxin CytA from Bacillus thuringiensis var. israelensis with lipid membranes. Biochemistry. 36: 12862-12868. (Pubitemid 27465397)
    • (1997) Biochemistry , vol.36 , Issue.42 , pp. 12862-12868
    • Butko, P.1    Huang, F.2    Pusztai-Carey, M.3    Surewicz, W.K.4
  • 33
    • 0034663233 scopus 로고    scopus 로고
    • Membrane binding of MARCKS-related protein studied by tryptophan fluorescence spectroscopy
    • DOI 10.1006/abbi.2000.1925
    • Schmitz, A. A., A. Ulrich, and G. Vergeres. 2000. Membrane binding of MARCKS-related protein studied by tryptophan fluorescence spectroscopy. Arch. Biochem. Biophys. 380:380-386. (Pubitemid 30659110)
    • (2000) Archives of Biochemistry and Biophysics , vol.380 , Issue.2 , pp. 380-386
    • Schmitz, A.A.P.1    Ulrich, A.2    Vergeres, G.3
  • 34
    • 0025813301 scopus 로고
    • Phosphatidate phosphatase from yeast
    • Carman, G. M., and Y-P. Lin. 1991. Phosphatidate phosphatase from yeast. Methods Enzymol. 197:548-553.
    • (1991) Methods Enzymol. , vol.197 , pp. 548-553
    • Carman, G.M.1    Lin, Y.-P.2
  • 35
    • 0025162158 scopus 로고
    • Kinetic analysis of yeast phosphatidate phosphatase toward Triton X-100/phosphatidate mixed micelles
    • Lin, Y-P., and G. M. Carman. 1990. Kinetic analysis of yeast phosphatidate phosphatase toward Triton X-100/phosphatidate mixed micelles. J. Biol. Chem. 265:166-170.
    • (1990) J. Biol. Chem. , vol.265 , pp. 166-170
    • Lin, Y.-P.1    Carman, G.M.2
  • 36
    • 0032581014 scopus 로고    scopus 로고
    • Conformation and lipid binding properties of four peptides derived from the membrane-binding domain of CTP:Phosphocholine cytidylyltransferase
    • DOI 10.1021/bi980340l
    • Johnson, J. E., N. M. Rao, S. W. Hui, and R. B. Cornell. 1998. Conformation and lipid binding properties of four peptides derived from the membrane-binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry. 37:9509-9519. (Pubitemid 28307707)
    • (1998) Biochemistry , vol.37 , Issue.26 , pp. 9509-9519
    • Johnson, J.E.1    Rao, N.M.2    Hui, S.-W.3    Cornell, R.B.4
  • 37
    • 43949121778 scopus 로고    scopus 로고
    • Optical anisotropy of supported lipid structures probed by waveguide spectroscopy and its application to study of supported lipid bilayer formation kinetics
    • DOI 10.1021/ac800027s
    • Mashaghi, A., M. Swann, J. Popplewell, M. Textor, and E. Reimhult. 2008. Optical anisotropy of supported lipid structures probed by waveguide spectroscopy and Its application to study of supported lipid bilayer formation kinetics. Anal. Chem. 80: 3666-3676. (Pubitemid 351705866)
    • (2008) Analytical Chemistry , vol.80 , Issue.10 , pp. 3666-3676
    • Mashaghi, A.1    Swann, M.2    Popplewell, J.3    Textor, M.4    Reimhult, E.5
  • 38
    • 5344228352 scopus 로고    scopus 로고
    • 2 action on vesicles and supported planar bilayers using a quartz crystal microbalance with dissipation
    • DOI 10.1016/j.jcis.2004.06.083, PII S0021979704006149
    • Justesen, P. H., T. Kristensen, T. Ebdrup, and D. Otzen. 2004. Investigating porcine pancreatic phospholipase A2 action on vesicles and supported planar bilayers using a quartz crystal microbalance with dissipation. J. Colloid Interface Sci. 279: 399-409. (Pubitemid 39349437)
    • (2004) Journal of Colloid and Interface Science , vol.279 , Issue.2 , pp. 399-409
    • Justesen, P.H.1    Kristensen, T.2    Ebdrup, T.3    Otzen, D.4
  • 39
    • 33746728985 scopus 로고    scopus 로고
    • Surface plasmon resonance in protein-membrane interactions
    • DOI 10.1016/j.chemphyslip.2006.02.010, PII S0009308406000326
    • Besenicar, M., P. Macek, J. H. Lakey, and G. Anderluh. 2006. Surface plasmon resonance in protein-membrane interactions. Chem. Phys. Lipids. 141:169-178. (Pubitemid 44250813)
    • (2006) Chemistry and Physics of Lipids , vol.141 , Issue.1-2 , pp. 169-178
    • Besenicar, M.1    Macek, P.2    Lakey, J.H.3    Anderluh, G.4
  • 40
    • 0034792514 scopus 로고    scopus 로고
    • Determination of strength and specificity of membrane-bound G protein-phospholipase C association using fluorescence spectroscopy
    • Scarlata, S. 2002. Determination of strength and specificity of membrane-bound G protein-phospholipase C association using fluorescence spectroscopy. Methods Enzymol. 345:306-327.
    • (2002) Methods Enzymol. , vol.345 , pp. 306-327
    • Scarlata, S.1
  • 42
    • 0141919746 scopus 로고    scopus 로고
    • Lipid-induced conformational switch in the membrane binding domain of CTP:phosphocholine cytidylyltransferase: A circular dichroism study
    • DOI 10.1021/bi035234k
    • Taneva, S., J. E. Johnson, and R. B. Cornell. 2003. Lipid-induced conformational switch in the membrane binding domain of CTP:phosphocholine cytidylyltransferase: a circular dichroism study. Biochemistry. 42:11768-11776. (Pubitemid 37243638)
    • (2003) Biochemistry , vol.42 , Issue.40 , pp. 11768-11776
    • Taneva, S.1    Johnson, J.E.2    Cornell, R.B.3
  • 43
    • 0027765632 scopus 로고
    • Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles
    • Casals, C., E. Miguel, and J. Perez-Gil. 1993. Tryptophan fluorescence study on the interaction of pulmonary surfactant protein A with phospholipid vesicles. Biochem. J. 296:585-593. (Pubitemid 24008172)
    • (1993) Biochemical Journal , vol.296 , Issue.3 , pp. 585-593
    • Casals, C.1    Miguel, E.2    Perez-Gil, J.3


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