메뉴 건너뛰기




Volumn 288, Issue 37, 2013, Pages 26822-26833

Phosphorylation regulates myo-inositol-3-phosphate synthase a novel regulatory mechanism of inositol biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN DISORDERS; REGULATORY MECHANISM; SYNTHASES;

EID: 84884182719     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.479121     Document Type: Article
Times cited : (38)

References (42)
  • 1
    • 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
  • 3
    • 33747375103 scopus 로고    scopus 로고
    • Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae
    • Gaspar, M. L., Aregullin, M. A., Jesch, S. A., and Henry, S. A. (2006) Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae. J. Biol. Chem. 281, 22773-22785
    • (2006) J. Biol. Chem. , vol.281 , pp. 22773-22785
    • Gaspar, M.L.1    Aregullin, M.A.2    Jesch, S.A.3    Henry, S.A.4
  • 4
    • 0026074320 scopus 로고
    • Role of organic osmolytes in adaptation of renal cells to high osmolality
    • Garcia-Perez, A., and Burg, M. B. (1991) Role of organic osmolytes in adaptation of renal cells to high osmolality. J. Membr. Biol. 119, 1-13
    • (1991) J. Membr. Biol. , vol.119 , pp. 1-13
    • Garcia-Perez, A.1    Burg, M.B.2
  • 5
    • 0033588069 scopus 로고    scopus 로고
    • Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1- phosphate synthase enzyme
    • Bachhawat, N., and Mande, S. C. (1999) Identification of the INO1 gene of Mycobacterium tuberculosis H37Rv reveals a novel class of inositol-1- phosphate synthase enzyme. J. Mol. Biol. 291, 531-536
    • (1999) J. Mol. Biol. , vol.291 , pp. 531-536
    • Bachhawat, N.1    Mande, S.C.2
  • 6
    • 0034634004 scopus 로고    scopus 로고
    • Inositol-1-phosphate synthase from Archaeoglobus fulgidus is a class II aldolase
    • Chen, L., Zhou, C., Yang, H., and Roberts, M. F. (2000) Inositol-1-phosphate synthase from Archaeoglobus fulgidus is a class II aldolase. Biochemistry 39, 12415-12423
    • (2000) Biochemistry , vol.39 , pp. 12415-12423
    • Chen, L.1    Zhou, C.2    Yang, H.3    Roberts, M.F.4
  • 7
    • 0032951376 scopus 로고    scopus 로고
    • L-myo-Inositol 1-phosphate synthase from Entamoeba histolytica
    • Lohia, A., Hait, N. C., and Majumder, A. L. (1999) L-myo-Inositol 1-phosphate synthase from Entamoeba histolytica. Mol. Biochem. Parasitol. 98, 67-79
    • (1999) Mol. Biochem. Parasitol. , vol.98 , pp. 67-79
    • Lohia, A.1    Hait, N.C.2    Majumder, A.L.3
  • 8
    • 0001703224 scopus 로고
    • The isolation and characterization of D-glucose 6-phosphate cycloaldolase (NAD-dependent) from acer pseudoplatanus L. Cell cultures. Its occurrence in plants
    • Loewus, M. W., and Loewus, F. (1971) The isolation and characterization of D-glucose 6-phosphate cycloaldolase (NAD-dependent) from Acer pseudoplatanus L. cell cultures. Its occurrence in plants. Plant Physiol. 48, 255-260
    • (1971) Plant Physiol. , vol.48 , pp. 255-260
    • Loewus, M.W.1    Loewus, F.2
  • 9
    • 0024212931 scopus 로고
    • L-myo-Inositol-1-phosphate synthase from mammalian brain. Partial purification and characterisation of the fetal and adult enzyme
    • Adhikari, J., and Majumder, A. L. (1988) L-myo-Inositol-1-phosphate synthase from mammalian brain. Partial purification and characterisation of the fetal and adult enzyme. Indian J. Biochem. Biophys. 25, 408-412
    • (1988) Indian J. Biochem. Biophys. , vol.25 , pp. 408-412
    • Adhikari, J.1    Majumder, A.L.2
  • 10
    • 0019332962 scopus 로고
    • Purification, structure, and catalytic properties of L-myo-Inositol-1- phosphate synthase from rat testis
    • Maeda, T., and Eisenberg, F., Jr. (1980) Purification, structure, and catalytic properties of L-myo-Inositol-1-phosphate synthase from rat testis. J. Biol. Chem. 255, 8458-8464
    • (1980) J. Biol. Chem. , vol.255 , pp. 8458-8464
    • Maeda, T.1    Eisenberg Jr., F.2
  • 11
    • 0024494204 scopus 로고
    • Biosynthesis of inositol in yeast. Primary structure of myo-inositol-1-phosphate synthase (EC 5.5.1.4) and functional analysis of its structural gene, the INO1 locus
    • Dean-Johnson, M., and Henry, S. A. (1989) Biosynthesis of inositol in yeast. Primary structure of myo-inositol-1-phosphate synthase (EC 5.5.1.4) and functional analysis of its structural gene, the INO1 locus. J. Biol. Chem. 264, 1274-1283
    • (1989) J. Biol. Chem. , vol.264 , pp. 1274-1283
    • Dean-Johnson, M.1    Henry, S.A.2
  • 12
    • 0041662062 scopus 로고    scopus 로고
    • CDNA cloning and gene expression analysis of human myo-inositol 1-phosphate synthase
    • Guan, G., Dai, P., and Shechter, I. (2003) cDNA cloning and gene expression analysis of human myo-inositol 1-phosphate synthase. Arch. Biochem. Biophys. 417, 251-259
    • (2003) Arch. Biochem. Biophys. , vol.417 , pp. 251-259
    • Guan, G.1    Dai, P.2    Shechter, I.3
  • 13
    • 66149137994 scopus 로고    scopus 로고
    • Identification of myo-inositol-3-phosphate synthase isoforms. Characterization, expression, and putative role of a 16-kDaγc isoform
    • Seelan, R. S., Lakshmanan, J., Casanova, M. F., and Parthasarathy, R. N. (2009) Identification of myo-inositol-3-phosphate synthase isoforms. Characterization, expression, and putative role of a 16-kDaγc isoform. J. Biol. Chem. 284, 9443-9457
    • (2009) J. Biol. Chem. , vol.284 , pp. 9443-9457
    • Seelan, R.S.1    Lakshmanan, J.2    Casanova, M.F.3    Parthasarathy, R.N.4
  • 14
    • 82955169487 scopus 로고    scopus 로고
    • Crystal structure of a trapped catalytic intermediate suggests that forced atomic proximity drives the catalysis of mIPS
    • Neelon, K., Roberts, M. F., and Stec, B. (2011) Crystal structure of a trapped catalytic intermediate suggests that forced atomic proximity drives the catalysis of mIPS. Biophys. J. 101, 2816-2824
    • (2011) Biophys. J. , vol.101 , pp. 2816-2824
    • Neelon, K.1    Roberts, M.F.2    Stec, B.3
  • 15
    • 39049184513 scopus 로고    scopus 로고
    • The structure and mechanism of myoinositol- 1-phosphate synthase
    • Geiger, J. H., and Jin, X. (2006) The structure and mechanism of myoinositol- 1-phosphate synthase. Subcell. Biochem. 39, 157-180
    • (2006) Subcell. Biochem. , vol.39 , pp. 157-180
    • Geiger, J.H.1    Jin, X.2
  • 16
    • 0038793610 scopus 로고    scopus 로고
    • Structures of NAD+- and NADH-bound 1-L-myo-Inositol 1-phosphate synthase
    • Jin, X., and Geiger, J. H. (2003) Structures of NAD+- and NADH-bound 1-L-myo-Inositol 1-phosphate synthase. Acta Crystallogr. D Biol. Crystallogr. 59, 1154-1164
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 1154-1164
    • Jin, X.1    Geiger, J.H.2
  • 17
    • 0037088612 scopus 로고    scopus 로고
    • The crystal structure and mechanism of 1-L-myo-inositol-1-phosphate synthase
    • Stein, A. J., and Geiger, J. H. (2002) The crystal structure and mechanism of 1-L-myo-inositol-1-phosphate synthase. J. Biol. Chem. 277, 9484-9491
    • (2002) J. Biol. Chem. , vol.277 , pp. 9484-9491
    • Stein, A.J.1    Geiger, J.H.2
  • 18
    • 0141682777 scopus 로고    scopus 로고
    • Diversification and evolution of L-myo-inositol 1-phosphate synthase
    • Majumder, A. L., Chatterjee, A., Ghosh Dastidar, K., and Majee, M. (2003) Diversification and evolution of L-myo-inositol 1-phosphate synthase. FEBS Lett. 553, 3-10
    • (2003) FEBS Lett. , vol.553 , pp. 3-10
    • Majumder, A.L.1    Chatterjee, A.2    Ghosh Dastidar, K.3    Majee, M.4
  • 19
    • 0032730257 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes
    • Carman, G. M., and Henry, S. A. (1999) Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes. Prog. Lipid Res. 38, 361-399
    • (1999) Prog. Lipid Res. , vol.38 , pp. 361-399
    • Carman, G.M.1    Henry, S.A.2
  • 20
    • 0029963923 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae
    • Greenberg, M. L., and Lopes, J. M. (1996) Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae. Microbiol. Rev. 60, 1-20
    • (1996) Microbiol. Rev. , vol.60 , pp. 1-20
    • Greenberg, M.L.1    Lopes, J.M.2
  • 21
    • 38549162457 scopus 로고    scopus 로고
    • Regulation of 1D-myo-inositol-3- phosphate synthase in yeast
    • Nunez, L. R., and Henry, S. A. (2006) Regulation of 1D-myo-inositol-3- phosphate synthase in yeast. Subcell. Biochem. 39, 135-156
    • (2006) Subcell. Biochem. , vol.39 , pp. 135-156
    • Nunez, L.R.1    Henry, S.A.2
  • 22
    • 84857424979 scopus 로고    scopus 로고
    • Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae
    • Henry, S. A., Kohlwein, S. D., and Carman, G. M. (2012) Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae. Genetics 190, 317-349
    • (2012) Genetics , vol.190 , pp. 317-349
    • Henry, S.A.1    Kohlwein, S.D.2    Carman, G.M.3
  • 23
    • 0026088571 scopus 로고
    • The OPI1 gene of Saccharomyces cerevisiae, a negative regulator of phospholipid biosynthesis, encodes a protein containing polyglutamine tracts and a leucine zipper
    • White, M. J., Hirsch, J. P., and Henry, S. A. (1991) The OPI1 gene of Saccharomyces cerevisiae, a negative regulator of phospholipid biosynthesis, encodes a protein containing polyglutamine tracts and a leucine zipper. J. Biol. Chem. 266, 863-872
    • (1991) J. Biol. Chem. , vol.266 , pp. 863-872
    • White, M.J.1    Hirsch, J.P.2    Henry, S.A.3
  • 24
    • 0016739154 scopus 로고
    • Inositol-requiring mutants of Saccharomyces cerevisiae
    • Culbertson, M. R., and Henry, S. A. (1975) Inositol-requiring mutants of Saccharomyces cerevisiae. Genetics 80, 23-40
    • (1975) Genetics , vol.80 , pp. 23-40
    • Culbertson, M.R.1    Henry, S.A.2
  • 25
    • 70350169737 scopus 로고    scopus 로고
    • Cellular consequences of inositol depletion
    • Deranieh, R. M., and Greenberg, M. L. (2009) Cellular consequences of inositol depletion. Biochem. Soc. Trans. 37, 1099-1103
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1099-1103
    • Deranieh, R.M.1    Greenberg, M.L.2
  • 26
    • 79551583348 scopus 로고    scopus 로고
    • Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling
    • Villa-Garc?á, M. J., Choi, M. S., Hinz, F. I., Gaspar, M. L., Jesch, S. A., and Henry, S. A. (2011) Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling. Mol. Genet. Genomics 285, 125-149
    • (2011) Mol. Genet. Genomics , vol.285 , pp. 125-149
    • Villa-Garcá, M.J.1    Choi, M.S.2    Hinz, F.I.3    Gaspar, M.L.4    Jesch, S.A.5    Henry, S.A.6
  • 27
    • 3342900250 scopus 로고    scopus 로고
    • Bipolar disorder
    • Belmaker, R. H. (2004) Bipolar disorder. N. Engl. J. Med. 351, 476-486
    • (2004) N. Engl. J. Med. , vol.351 , pp. 476-486
    • Belmaker, R.H.1
  • 28
    • 0032562547 scopus 로고    scopus 로고
    • Phosphatidylinositol and inositol involvement in Alzheimer amyloid-βfibril growth and arrest
    • McLaurin, J., Franklin, T., Chakrabartty, A., and Fraser, P. E. (1998) Phosphatidylinositol and inositol involvement in Alzheimer amyloid-βfibril growth and arrest. J. Mol. Biol. 278, 183-194
    • (1998) J. Mol. Biol. , vol.278 , pp. 183-194
    • McLaurin, J.1    Franklin, T.2    Chakrabartty, A.3    Fraser, P.E.4
  • 29
    • 0032502633 scopus 로고    scopus 로고
    • Alteration of myo-inositol monophosphatase in Alzheimer's disease brains
    • Shimohama, S., Tanino, H., Sumida, Y., Tsuda, J., and Fujimoto, S. (1998) Alteration of myo-inositol monophosphatase in Alzheimer's disease brains. Neuroscience Lett. 245, 159-162
    • (1998) Neuroscience Lett. , vol.245 , pp. 159-162
    • Shimohama, S.1    Tanino, H.2    Sumida, Y.3    Tsuda, J.4    Fujimoto, S.5
  • 30
    • 0025912111 scopus 로고
    • Lithium and the phosphoinositide cycle. An example of uncompetitive inhibition and its pharmacological consequences
    • Nahorski, S. R., Ragan, C. I., and Challiss, R. A. (1991) Lithium and the phosphoinositide cycle. An example of uncompetitive inhibition and its pharmacological consequences. Trends Pharmacol. Sci. 12, 297-303
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 297-303
    • Nahorski, S.R.1    Ragan, C.I.2    Challiss, R.A.3
  • 31
    • 2542422679 scopus 로고    scopus 로고
    • Human 1-D-myo-Inositol-3-phosphate synthase is functional in yeast
    • Ju, S., Shaltiel, G., Shamir, A., Agam, G., and Greenberg, M. L. (2004) Human 1-D-myo-Inositol-3-phosphate synthase is functional in yeast. J. Biol. Chem. 279, 21759-21765
    • (2004) J. Biol. Chem. , vol.279 , pp. 21759-21765
    • Ju, S.1    Shaltiel, G.2    Shamir, A.3    Agam, G.4    Greenberg, M.L.5
  • 33
    • 0035805569 scopus 로고    scopus 로고
    • Lithium and valproate decrease inositol mass and increase expression of the yeast INO1 and INO2 genes for inositol biosynthesis
    • Vaden, D. L., Ding, D., Peterson, B., and Greenberg, M. L. (2001) Lithium and valproate decrease inositol mass and increase expression of the yeast INO1 and INO2 genes for inositol biosynthesis. J. Biol. Chem. 276, 15466-15471
    • (2001) J. Biol. Chem. , vol.276 , pp. 15466-15471
    • Vaden, D.L.1    Ding, D.2    Peterson, B.3    Greenberg, M.L.4
  • 34
    • 34547127402 scopus 로고    scopus 로고
    • Phosphorylation of human CTP synthetase 1 by protein kinase C. Identification of Ser462 and Thr455 as major sites of phosphorylation
    • Chang, Y. F., Martin, S. S., Baldwin, E. P., and Carman, G. M. (2007) Phosphorylation of human CTP synthetase 1 by protein kinase C. Identification of Ser462 and Thr455 as major sites of phosphorylation. J. Biol. Chem. 282, 17613-17622
    • (2007) J. Biol. Chem. , vol.282 , pp. 17613-17622
    • Chang, Y.F.1    Martin, S.S.2    Baldwin, E.P.3    Carman, G.M.4
  • 35
    • 77951219665 scopus 로고    scopus 로고
    • Phosphorylation of yeast phosphatidylserine synthase by protein kinase A. Identification of Ser46 and Ser47 as major sites of phosphorylation
    • Choi, H. S., Han, G. S., and Carman, G. M. (2010) Phosphorylation of yeast phosphatidylserine synthase by protein kinase A. Identification of Ser46 and Ser47 as major sites of phosphorylation. J. Biol. Chem. 285, 11526-11536
    • (2010) J. Biol. Chem. , vol.285 , pp. 11526-11536
    • Choi, H.S.1    Han, G.S.2    Carman, G.M.3
  • 36
    • 78651385378 scopus 로고    scopus 로고
    • Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae. Identification of Ser602, Thr723, and Ser744 as the sites phosphorylated by CDC28 (CDK1)-encoded cyclindependent 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 Ser602, Thr723, and Ser744 as the sites phosphorylated by CDC28 (CDK1)-encoded cyclindependent 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
  • 37
    • 0014845123 scopus 로고
    • A colorimetric determination of inositol monophosphates as an assay for D-glucose 6-phosphate- 1L-myoinositol 1-phosphate cyclase
    • Barnett, J. E., Brice, R. E., and Corina, D. L. (1970) A colorimetric determination of inositol monophosphates as an assay for D-glucose 6-phosphate- 1L-myoinositol 1-phosphate cyclase. Biochem. J. 119, 183-186
    • (1970) Biochem. J. , vol.119 , pp. 183-186
    • Barnett, J.E.1    Brice, R.E.2    Corina, D.L.3
  • 38
    • 1842790985 scopus 로고    scopus 로고
    • The structure of the 1L-myoinositol- 1-phosphate synthase-NAD-2-deoxy-D- glucitol 6-(E)-vinylhomophosphonate complex demands a revision of the enzyme mechanism
    • Jin, X., Foley, K. M., and Geiger, J. H. (2004) The structure of the 1L-myoinositol- 1-phosphate synthase-NAD-2-deoxy-D-glucitol 6-(E)- vinylhomophosphonate complex demands a revision of the enzyme mechanism. J. Biol. Chem. 279, 13889-13895
    • (2004) J. Biol. Chem. , vol.279 , pp. 13889-13895
    • Jin, X.1    Foley, K.M.2    Geiger, J.H.3
  • 41
    • 0036118315 scopus 로고    scopus 로고
    • Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis
    • Norman, R. A., McAlister, M. S., Murray-Rust, J., Movahedzadeh, F., Stoker, N. G., and McDonald, N. Q. (2002) Crystal structure of inositol 1-phosphate synthase from Mycobacterium tuberculosis, a key enzyme in phosphatidylinositol synthesis. Structure 10, 393-402
    • (2002) Structure , vol.10 , pp. 393-402
    • Norman, R.A.1    McAlister, M.S.2    Murray-Rust, J.3    Movahedzadeh, F.4    Stoker, N.G.5    McDonald, N.Q.6
  • 42
    • 33846670518 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 is required for optimal de novo synthesis of inositol
    • Azab, A. N., He, Q., Ju, S., Li, G., and Greenberg, M. L. (2007) Glycogen synthase kinase-3 is required for optimal de novo synthesis of inositol. Mol. Microbiol. 63, 1248-1258
    • (2007) Mol. Microbiol. , vol.63 , pp. 1248-1258
    • Azab, A.N.1    He, Q.2    Ju, S.3    Li, G.4    Greenberg, M.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.