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Volumn 7, Issue 1, 2012, Pages

Human PAPS synthase isoforms are dynamically regulated enzymes with access to nucleus and cytoplasm

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE 3' PHOSPHATE 5' PHOSPHOSULFATE; ARGININE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; ISOENZYME; LEPTOMYCIN B; LYSINE; CELL RECEPTOR; ENHANCED GREEN FLUORESCENT PROTEIN; EXPORTIN 1 PROTEIN; GREEN FLUORESCENT PROTEIN; KARYOPHERIN; MULTIENZYME COMPLEX; MUTANT PROTEIN; PAPS SYNTHETASE; SULFATE ADENYLYLTRANSFERASE; UNSATURATED FATTY ACID;

EID: 84855385018     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0029559     Document Type: Article
Times cited : (32)

References (41)
  • 1
    • 0031136606 scopus 로고    scopus 로고
    • Sulfation and sulfotransferases 5: the importance of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation
    • Klaassen CD, Boles JW, (1997) Sulfation and sulfotransferases 5: the importance of 3′-phosphoadenosine 5′-phosphosulfate (PAPS) in the regulation of sulfation. FASEB J 11: 404-418.
    • (1997) FASEB J , vol.11 , pp. 404-418
    • Klaassen, C.D.1    Boles, J.W.2
  • 3
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: assembly of ligand binding sites in heparan sulfate
    • Esko JD, Selleck SB, (2002) Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 71: 435-471.
    • (2002) Annu Rev Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 4
    • 33645122881 scopus 로고    scopus 로고
    • Pharmacogenetics of human cytosolic sulfotransferases
    • Nowell S, Falany CN, (2006) Pharmacogenetics of human cytosolic sulfotransferases. Oncogene 25: 1673-1678.
    • (2006) Oncogene , vol.25 , pp. 1673-1678
    • Nowell, S.1    Falany, C.N.2
  • 5
    • 33746357573 scopus 로고    scopus 로고
    • Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment
    • Goettsch S, Badea RA, Mueller JW, Wotzlaw C, Schoelermann B, et al. (2006) Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment. J Mol Biol 361: 436-449.
    • (2006) J Mol Biol , vol.361 , pp. 436-449
    • Goettsch, S.1    Badea, R.A.2    Mueller, J.W.3    Wotzlaw, C.4    Schoelermann, B.5
  • 7
    • 33748905682 scopus 로고    scopus 로고
    • Characterization of proline-serine-rich carboxyl terminus in human sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic properties, and phosphorylation
    • He D, Falany CN, (2006) Characterization of proline-serine-rich carboxyl terminus in human sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic properties, and phosphorylation. Drug Metab Dispos 34: 1749-1755.
    • (2006) Drug Metab Dispos , vol.34 , pp. 1749-1755
    • He, D.1    Falany, C.N.2
  • 8
    • 0031946383 scopus 로고    scopus 로고
    • Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase
    • Girard JP, Baekkevold ES, Amalric F, (1998) Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J 12: 603-612.
    • (1998) FASEB J , vol.12 , pp. 603-612
    • Girard, J.P.1    Baekkevold, E.S.2    Amalric, F.3
  • 10
    • 14744300141 scopus 로고    scopus 로고
    • The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding
    • Harjes S, Bayer P, Scheidig AJ, (2005) The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding. J Mol Biol 347: 623-635.
    • (2005) J Mol Biol , vol.347 , pp. 623-635
    • Harjes, S.1    Bayer, P.2    Scheidig, A.J.3
  • 11
    • 33744951576 scopus 로고    scopus 로고
    • Essential roles of 3′-phosphoadenosine 5′-phosphosulfate synthase in embryonic and larval development of the nematode Caenorhabditis elegans
    • Dejima K, Seko A, Yamashita K, Gengyo-Ando K, Mitani S, et al. (2006) Essential roles of 3′-phosphoadenosine 5′-phosphosulfate synthase in embryonic and larval development of the nematode Caenorhabditis elegans. J Biol Chem 281: 11431-11440.
    • (2006) J Biol Chem , vol.281 , pp. 11431-11440
    • Dejima, K.1    Seko, A.2    Yamashita, K.3    Gengyo-Ando, K.4    Mitani, S.5
  • 12
    • 17344364658 scopus 로고    scopus 로고
    • Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse
    • ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, et al. (1998) Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse. Nat Genet 20: 157-162.
    • (1998) Nat Genet , vol.20 , pp. 157-162
    • ul Haque, M.F.1    King, L.M.2    Krakow, D.3    Cantor, R.M.4    Rusiniak, M.E.5
  • 13
    • 66249088642 scopus 로고    scopus 로고
    • Inactivating PAPSS2 mutations in a patient with premature pubarche
    • Noordam C, Dhir V, McNelis JC, Schlereth F, Hanley NA, et al. (2009) Inactivating PAPSS2 mutations in a patient with premature pubarche. N Engl J Med 360: 2310-2318.
    • (2009) N Engl J Med , vol.360 , pp. 2310-2318
    • Noordam, C.1    Dhir, V.2    McNelis, J.C.3    Schlereth, F.4    Hanley, N.A.5
  • 14
    • 84984578402 scopus 로고    scopus 로고
    • Evidence for association with hepatocellular carcinoma at the PAPSS1 locus on chromosome 4q25 in a family-based study
    • Shih WL, Yu MW, Chen PJ, Wu TW, Lin CL, et al. (2009) Evidence for association with hepatocellular carcinoma at the PAPSS1 locus on chromosome 4q25 in a family-based study. Eur J Hum Genet 17: 1250-1259.
    • (2009) Eur J Hum Genet , vol.17 , pp. 1250-1259
    • Shih, W.L.1    Yu, M.W.2    Chen, P.J.3    Wu, T.W.4    Lin, C.L.5
  • 15
    • 57149086286 scopus 로고    scopus 로고
    • The host cell sulfonation pathway contributes to retroviral infection at a step coincident with provirus establishment
    • Bruce JW, Ahlquist P, Young JA, (2008) The host cell sulfonation pathway contributes to retroviral infection at a step coincident with provirus establishment. PLoS Pathog 4: e1000207.
    • (2008) PLoS Pathog , vol.4
    • Bruce, J.W.1    Ahlquist, P.2    Young, J.A.3
  • 16
    • 65749085502 scopus 로고    scopus 로고
    • Chapter 7. Tyrosine sulfation of HIV-1 coreceptors and other chemokine receptors
    • Choe H, Farzan M, (2009) Chapter 7. Tyrosine sulfation of HIV-1 coreceptors and other chemokine receptors. Methods Enzymol 461: 147-170.
    • (2009) Methods Enzymol , vol.461 , pp. 147-170
    • Choe, H.1    Farzan, M.2
  • 17
    • 0033960622 scopus 로고    scopus 로고
    • Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells
    • Besset S, Vincourt JB, Amalric F, Girard JP, (2000) Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells. FASEB J 14: 345-354.
    • (2000) FASEB J , vol.14 , pp. 345-354
    • Besset, S.1    Vincourt, J.B.2    Amalric, F.3    Girard, J.P.4
  • 18
    • 77951880492 scopus 로고    scopus 로고
    • A heterodimer of human 3′-phospho-adenosine-5′-phosphosulphate (PAPS) synthases is a new sulphate activating complex
    • Grum D, van den Boom J, Neumann D, Matena A, Link NM, et al. (2010) A heterodimer of human 3′-phospho-adenosine-5′-phosphosulphate (PAPS) synthases is a new sulphate activating complex. Biochem Biophys Res Commun 395: 420-425.
    • (2010) Biochem Biophys Res Commun , vol.395 , pp. 420-425
    • Grum, D.1    van den Boom, J.2    Neumann, D.3    Matena, A.4    Link, N.M.5
  • 19
    • 78549264393 scopus 로고    scopus 로고
    • NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1
    • Guttler T, Madl T, Neumann P, Deichsel D, Corsini L, et al. (2010) NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Nat Struct Mol Biol 17: 1367-1376.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1367-1376
    • Guttler, T.1    Madl, T.2    Neumann, P.3    Deichsel, D.4    Corsini, L.5
  • 20
    • 0032528507 scopus 로고    scopus 로고
    • A novel system to quantitate nuclear-cytoplasmic flux in vivo: kinetics of signal-dependent nuclear protein export
    • Efthymiadis A, Dottorini T, Jans DA, (1998) A novel system to quantitate nuclear-cytoplasmic flux in vivo: kinetics of signal-dependent nuclear protein export. Arch Biochem Biophys 355: 254-261.
    • (1998) Arch Biochem Biophys , vol.355 , pp. 254-261
    • Efthymiadis, A.1    Dottorini, T.2    Jans, D.A.3
  • 22
    • 15244350737 scopus 로고    scopus 로고
    • Nuclear export is evolutionarily conserved in CVC paired-like homeobox proteins and influences protein stability, transcriptional activation, and extracellular secretion
    • Knauer SK, Carra G, Stauber RH, (2005) Nuclear export is evolutionarily conserved in CVC paired-like homeobox proteins and influences protein stability, transcriptional activation, and extracellular secretion. Mol Cell Biol 25: 2573-2582.
    • (2005) Mol Cell Biol , vol.25 , pp. 2573-2582
    • Knauer, S.K.1    Carra, G.2    Stauber, R.H.3
  • 23
    • 0037126617 scopus 로고    scopus 로고
    • A novel transferable nuclear export signal mediates CRM1-independent nucleocytoplasmic shuttling of the human cytomegalovirus transactivator protein pUL69
    • Lischka P, Rosorius O, Trommer E, Stamminger T, (2001) A novel transferable nuclear export signal mediates CRM1-independent nucleocytoplasmic shuttling of the human cytomegalovirus transactivator protein pUL69. EMBO J 20: 7271-7283.
    • (2001) EMBO J , vol.20 , pp. 7271-7283
    • Lischka, P.1    Rosorius, O.2    Trommer, E.3    Stamminger, T.4
  • 24
    • 0142211276 scopus 로고    scopus 로고
    • Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor
    • Saporita AJ, Zhang Q, Navai N, Dincer Z, Hahn J, et al. (2003) Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor. J Biol Chem 278: 41998-42005.
    • (2003) J Biol Chem , vol.278 , pp. 41998-42005
    • Saporita, A.J.1    Zhang, Q.2    Navai, N.3    Dincer, Z.4    Hahn, J.5
  • 25
    • 2342432165 scopus 로고    scopus 로고
    • Conserved nuclear export sequences in Schizosaccharomyces pombe Mex67 and human TAP function in mRNA export by direct nuclear pore interactions
    • Thakurta AG, Gopal G, Yoon JH, Saha T, Dhar R, (2004) Conserved nuclear export sequences in Schizosaccharomyces pombe Mex67 and human TAP function in mRNA export by direct nuclear pore interactions. J Biol Chem 279: 17434-17442.
    • (2004) J Biol Chem , vol.279 , pp. 17434-17442
    • Thakurta, A.G.1    Gopal, G.2    Yoon, J.H.3    Saha, T.4    Dhar, R.5
  • 26
    • 33749459704 scopus 로고    scopus 로고
    • Characterization of a novel transferable CRM-1-independent nuclear export signal in a herpesvirus tegument protein that shuttles between the nucleus and cytoplasm
    • Verhagen J, Donnelly M, Elliott G, (2006) Characterization of a novel transferable CRM-1-independent nuclear export signal in a herpesvirus tegument protein that shuttles between the nucleus and cytoplasm. J Virol 80: 10021-10035.
    • (2006) J Virol , vol.80 , pp. 10021-10035
    • Verhagen, J.1    Donnelly, M.2    Elliott, G.3
  • 27
    • 33845806444 scopus 로고    scopus 로고
    • Regulated nucleo-cytoplasmic shuttling of human aci-reductone dioxygenase (hADI1) and its potential role in mRNA processing
    • Gotoh I, Uekita T, Seiki M, (2007) Regulated nucleo-cytoplasmic shuttling of human aci-reductone dioxygenase (hADI1) and its potential role in mRNA processing. Genes Cells 12: 105-117.
    • (2007) Genes Cells , vol.12 , pp. 105-117
    • Gotoh, I.1    Uekita, T.2    Seiki, M.3
  • 28
    • 4444229456 scopus 로고    scopus 로고
    • Exportin 7 defines a novel general nuclear export pathway
    • Mingot JM, Bohnsack MT, Jakle U, Gorlich D, (2004) Exportin 7 defines a novel general nuclear export pathway. EMBO J 23: 3227-3236.
    • (2004) EMBO J , vol.23 , pp. 3227-3236
    • Mingot, J.M.1    Bohnsack, M.T.2    Jakle, U.3    Gorlich, D.4
  • 29
    • 44949122687 scopus 로고    scopus 로고
    • STRADalpha regulates LKB1 localization by blocking access to importin-alpha, and by association with Crm1 and exportin-7
    • Dorfman J, Macara IG, (2008) STRADalpha regulates LKB1 localization by blocking access to importin-alpha, and by association with Crm1 and exportin-7. Mol Biol Cell 19: 1614-1626.
    • (2008) Mol Biol Cell , vol.19 , pp. 1614-1626
    • Dorfman, J.1    Macara, I.G.2
  • 30
    • 33847203612 scopus 로고    scopus 로고
    • Elucidation of the active conformation of the APS-kinase domain of human PAPS synthetase 1
    • Sekulic N, Dietrich K, Paarmann I, Ort S, Konrad M, et al. (2007) Elucidation of the active conformation of the APS-kinase domain of human PAPS synthetase 1. J Mol Biol 367: 488-500.
    • (2007) J Mol Biol , vol.367 , pp. 488-500
    • Sekulic, N.1    Dietrich, K.2    Paarmann, I.3    Ort, S.4    Konrad, M.5
  • 31
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: definition, function, and interaction with importin alpha
    • Lange A, Mills RE, Lange CJ, Stewart M, Devine SE, et al. (2007) Classical nuclear localization signals: definition, function, and interaction with importin alpha. J Biol Chem 282: 5101-5105.
    • (2007) J Biol Chem , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5
  • 32
    • 58649104919 scopus 로고    scopus 로고
    • Six classes of nuclear localization signals specific to different binding grooves of importin alpha
    • Kosugi S, Hasebe M, Matsumura N, Takashima H, Miyamoto-Sato E, et al. (2009) Six classes of nuclear localization signals specific to different binding grooves of importin alpha. J Biol Chem 284: 478-485.
    • (2009) J Biol Chem , vol.284 , pp. 478-485
    • Kosugi, S.1    Hasebe, M.2    Matsumura, N.3    Takashima, H.4    Miyamoto-Sato, E.5
  • 33
    • 77958464695 scopus 로고    scopus 로고
    • An actin-regulated importin alpha/beta-dependent extended bipartite NLS directs nuclear import of MRTF-A
    • Pawlowski R, Rajakyla EK, Vartiainen MK, Treisman R, (2010) An actin-regulated importin alpha/beta-dependent extended bipartite NLS directs nuclear import of MRTF-A. EMBO J 29: 3448-3458.
    • (2010) EMBO J , vol.29 , pp. 3448-3458
    • Pawlowski, R.1    Rajakyla, E.K.2    Vartiainen, M.K.3    Treisman, R.4
  • 34
    • 35448936378 scopus 로고    scopus 로고
    • The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae
    • Kessler D, Papatheodorou P, Stratmann T, Dian EA, Hartmann-Fatu C, et al. (2007) The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae. BMC Biol 5: 37.
    • (2007) BMC Biol , vol.5 , pp. 37
    • Kessler, D.1    Papatheodorou, P.2    Stratmann, T.3    Dian, E.A.4    Hartmann-Fatu, C.5
  • 35
    • 77957862495 scopus 로고    scopus 로고
    • Cloning and functional characterization of the guinea pig apoptosis inhibitor protein Survivin
    • Habtemichael N, Wunsch D, Bier C, Tillmann S, Unruhe B, et al. (2010) Cloning and functional characterization of the guinea pig apoptosis inhibitor protein Survivin. Gene 469: 9-17.
    • (2010) Gene , vol.469 , pp. 9-17
    • Habtemichael, N.1    Wunsch, D.2    Bier, C.3    Tillmann, S.4    Unruhe, B.5
  • 36
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field
    • Krieger E, Koraimann G, Vriend G, (2002) Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field. Proteins 47: 393-402.
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 37
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C, (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


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