메뉴 건너뛰기




Volumn 95, Issue 2, 1998, Pages 287-295

A putative protein serine/threonine phosphatase from Plasmodium falciparum contains a large N-terminal extension and five unique inserts in the catalytic domain

Author keywords

Chromosome; Gametocyte; Malaria; mRNA; Plasmodium falciparum; Protein serine threonine phosphatase

Indexed keywords

MESSENGER RNA; PROTEIN SERINE THREONINE KINASE;

EID: 0032531315     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(98)00106-6     Document Type: Article
Times cited : (37)

References (29)
  • 1
    • 0028035122 scopus 로고
    • Staurosporine inhibits invasion of erythrocytes by malarial merozoites
    • [1] Ward GE, Fujioka H, Aikawa M, Miller LH. Staurosporine inhibits invasion of erythrocytes by malarial merozoites. Exp Parasitol 1994;79:480-7.
    • (1994) Exp Parasitol , vol.79 , pp. 480-487
    • Ward, G.E.1    Fujioka, H.2    Aikawa, M.3    Miller, L.H.4
  • 2
    • 0022965175 scopus 로고
    • Control of malarial invasion by phosphorylation of the host cell membrane cytoskeleton
    • [2] Rangachari K, Dluzewski A, Wilson RJM, Gratzer WB. Control of malarial invasion by phosphorylation of the host cell membrane cytoskeleton. Nature 1986;324:364-5.
    • (1986) Nature , vol.324 , pp. 364-365
    • Rangachari, K.1    Dluzewski, A.2    Wilson, R.J.M.3    Gratzer, W.B.4
  • 3
    • 0023667518 scopus 로고
    • The relationship of phosphorylation of membrane proteins with the osmotic fragility and filterability of Plasmodium berghei-infected mouse erythrocytes
    • [3] Yuthavong Y, Limpaiboon T. The relationship of phosphorylation of membrane proteins with the osmotic fragility and filterability of Plasmodium berghei-infected mouse erythrocytes. Biochim Biophys Acta 1987;929:278-87.
    • (1987) Biochim Biophys Acta , vol.929 , pp. 278-287
    • Yuthavong, Y.1    Limpaiboon, T.2
  • 4
    • 0028988027 scopus 로고
    • Pfcrk-1, a developmentally regulated cdc2-related protein kinase of Plasmodium falciparum
    • [4] Doerig C, Doerig C, Horrocks P, et al. Pfcrk-1, a developmentally regulated cdc2-related protein kinase of Plasmodium falciparum. Mol Biochem Parasitol 1995;70:167-74.
    • (1995) Mol Biochem Parasitol , vol.70 , pp. 167-174
    • Doerig, C.1    Doerig, C.2    Horrocks, P.3
  • 5
    • 0029927806 scopus 로고    scopus 로고
    • PfKIN, an SNF1 type protein kinase of Plasmodium falciparum predominantly expressed in gametocytes
    • [5] Bracchi V, Langsley G, Thelu J, Eling W, Ambroise-Thomas P. PfKIN, an SNF1 type protein kinase of Plasmodium falciparum predominantly expressed in gametocytes. Mol Biochem Parasitol 1996;76:299-303.
    • (1996) Mol Biochem Parasitol , vol.76 , pp. 299-303
    • Bracchi, V.1    Langsley, G.2    Thelu, J.3    Eling, W.4    Ambroise-Thomas, P.5
  • 6
    • 0029862051 scopus 로고    scopus 로고
    • Pfmrk, a MO15-related protein kinase from Plasmodium falciparum: Gene cloning, sequence, stage-specific expression and chromosome localization
    • [6] Li JL, Robson KJH, Chen JL, Targett GAT, Baker DA. Pfmrk, a MO15-related protein kinase from Plasmodium falciparum: gene cloning, sequence, stage-specific expression and chromosome localization. Eur J Biochem 1996;241:805-13.
    • (1996) Eur J Biochem , vol.241 , pp. 805-813
    • Li, J.L.1    Robson, K.J.H.2    Chen, J.L.3    Targett, G.A.T.4    Baker, D.A.5
  • 7
    • 0029943490 scopus 로고    scopus 로고
    • Stage-specific expression of a Plasmodium falciparum protein related to the eukaryotic mitogen-activated protein kinases
    • [7] Lin DT, Goldman ND, Syin C. Stage-specific expression of a Plasmodium falciparum protein related to the eukaryotic mitogen-activated protein kinases. Mol Biochem Parasitol 1996;78:67-77.
    • (1996) Mol Biochem Parasitol , vol.78 , pp. 67-77
    • Lin, D.T.1    Goldman, N.D.2    Syin, C.3
  • 8
    • 0030771216 scopus 로고    scopus 로고
    • Protein phosphatase β, a putative type-2A protein phosphatase from the human malaria parasite Plasmodium falciparum
    • [8] Li JL, Baker DA. Protein phosphatase β, a putative type-2A protein phosphatase from the human malaria parasite Plasmodium falciparum. Eur J Biochem 1997;249:98-106.
    • (1997) Eur J Biochem , vol.249 , pp. 98-106
    • Li, J.L.1    Baker, D.A.2
  • 9
    • 0025313882 scopus 로고
    • Protein serine/threonine phosphatases: An expanding family
    • [9] Cohen PTW, Brewis ND, Hughes V, Mann DJ. Protein serine/threonine phosphatases: an expanding family. FEBS Lett 1990;268:355-9.
    • (1990) FEBS Lett , vol.268 , pp. 355-359
    • Cohen, P.T.W.1    Brewis, N.D.2    Hughes, V.3    Mann, D.J.4
  • 10
    • 0028053053 scopus 로고
    • Conservation analysis and structure prediction of the protein serine/threonine phosphatases
    • [10] Barton GJ, Cohen PTW, Barford D. Conservation analysis and structure prediction of the protein serine/threonine phosphatases. Eur J Biochem 1994;220:225-37.
    • (1994) Eur J Biochem , vol.220 , pp. 225-237
    • Barton, G.J.1    Cohen, P.T.W.2    Barford, D.3
  • 11
    • 0028298882 scopus 로고
    • A mutant of protein phosphatase-1 that exhibits altered toxin sensitivity
    • [11] Zhang Z, Zhao S, Long F, et al. A mutant of protein phosphatase-1 that exhibits altered toxin sensitivity. J Biol Chem 1994;269:16997-7000.
    • (1994) J Biol Chem , vol.269 , pp. 16997-17000
    • Zhang, Z.1    Zhao, S.2    Long, F.3
  • 12
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of serine/threonine phosphatase-1
    • [12] Goldberg J, Huang H, Kwon Y, Greengard P, Nairn AC, Kuriyan J. Three-dimensional structure of the catalytic subunit of serine/threonine phosphatase-1. Nature 1995;376:745-53.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.2    Kwon, Y.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 13
    • 0027139838 scopus 로고
    • PPQ, a novel protein phosphatase containing a Ser+Asn-rich amino terminal domain, is involved in the regulation of protein synthesis
    • [13] Chen MX, Chen YH, Cohen PTW. PPQ, a novel protein phosphatase containing a Ser+Asn-rich amino terminal domain, is involved in the regulation of protein synthesis. Eur J Biochem 1993;218:689-99.
    • (1993) Eur J Biochem , vol.218 , pp. 689-699
    • Chen, M.X.1    Chen, Y.H.2    Cohen, P.T.W.3
  • 14
    • 0026753631 scopus 로고
    • Molecular cloning and analysis of a yeast protein phosphatase with an unusual amino-terminal region
    • [14] Posas F, Casamayor A, Morral N, Arino J. Molecular cloning and analysis of a yeast protein phosphatase with an unusual amino-terminal region. J Biol Chem 1992;267:11734-40.
    • (1992) J Biol Chem , vol.267 , pp. 11734-11740
    • Posas, F.1    Casamayor, A.2    Morral, N.3    Arino, J.4
  • 15
    • 0027181530 scopus 로고
    • Both isoforms of protein phosphatase Z are essential for the maintenance of cell size and integrity in Saccharomyces cerevisiae in response to osmotic stress
    • [15] Hughes V, Muller A, Stark MJR, Cohen PTW. Both isoforms of protein phosphatase Z are essential for the maintenance of cell size and integrity in Saccharomyces cerevisiae in response to osmotic stress. Eur J Biochem 1993;216:269-79.
    • (1993) Eur J Biochem , vol.216 , pp. 269-279
    • Hughes, V.1    Muller, A.2    Stark, M.J.R.3    Cohen, P.T.W.4
  • 16
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • [16] Kennelly PJ, Krebs EG. Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 1991;266:15555-8.
    • (1991) J Biol Chem , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 17
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • [17] Wera S, Hemmings BA. Serine/threonine protein phosphatases. Biochem J 1995;311:17-29.
    • (1995) Biochem J , vol.311 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 18
    • 0026724733 scopus 로고
    • Drosophila retinal degeneration C (rdgC) encodes a novel serine/ threonine protein phosphatase
    • [18] Steele FR, Washburn T, Rieger R, O'Tousa JE. Drosophila retinal degeneration C (rdgC) encodes a novel serine/ threonine protein phosphatase. Cell 1992;69:669-76.
    • (1992) Cell , vol.69 , pp. 669-676
    • Steele, F.R.1    Washburn, T.2    Rieger, R.3    O'Tousa, J.E.4
  • 19
    • 0031915128 scopus 로고    scopus 로고
    • Molecular cloning expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)
    • [19] Huang X, Honkanen RE. Molecular cloning expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC). J Biol Chem 1998;273:1462-8.
    • (1998) J Biol Chem , vol.273 , pp. 1462-1468
    • Huang, X.1    Honkanen, R.E.2
  • 20
    • 0025647113 scopus 로고
    • Saccharomyces cerevisiae protein-phosphatase 2A performs an essential cellular function and is encoded by two genes
    • [20] Sneddon AA, Cohen PT, Stark MJ. Saccharomyces cerevisiae protein-phosphatase 2A performs an essential cellular function and is encoded by two genes. EMBO J 1990;9:4339-46.
    • (1990) EMBO J , vol.9 , pp. 4339-4346
    • Sneddon, A.A.1    Cohen, P.T.2    Stark, M.J.3
  • 21
    • 0025809351 scopus 로고
    • The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B
    • [21] Liu Y, Ishii S, Tokai M, et al. The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B. Mol Gen Genet 1991;227:52-9.
    • (1991) Mol Gen Genet , vol.227 , pp. 52-59
    • Liu, Y.1    Ishii, S.2    Tokai, M.3
  • 22
    • 0025913953 scopus 로고
    • Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase
    • [22] Cyert MS, Kunisawa R, Kaim D, Thorner J. Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase. Proc Natl Acad Sci USA 1991;88:7376-80.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7376-7380
    • Cyert, M.S.1    Kunisawa, R.2    Kaim, D.3    Thorner, J.4
  • 23
    • 0028133445 scopus 로고
    • A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus
    • [23] Chen MX, McPartlin AE, Brown L, Chen YH, Barker HM, Cohen PTW. A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus. EMBO J 1994;13:4278-90.
    • (1994) EMBO J , vol.13 , pp. 4278-4290
    • Chen, M.X.1    McPartlin, A.E.2    Brown, L.3    Chen, Y.H.4    Barker, H.M.5    Cohen, P.T.W.6
  • 24
    • 0026681136 scopus 로고
    • Twine, a cdc25 homologue that functions in the male and female germline of Drosophila
    • [24] Alphey L, Jimemez J, White-Cooper H, Dawson I, Nurse P, Glover DM. Twine, a cdc25 homologue that functions in the male and female germline of Drosophila. Cell 1992;69:977-88.
    • (1992) Cell , vol.69 , pp. 977-988
    • Alphey, L.1    Jimemez, J.2    White-Cooper, H.3    Dawson, I.4    Nurse, P.5    Glover, D.M.6
  • 25
    • 0026555258 scopus 로고
    • Molecular cloning of a calmodulin-dependent phosphatase from murine testis: Identification of a developmentally expressed nonneural isoenzyme
    • [25] Muramatsu T, Giri PR, Higuchi S, Kincaid RL. Molecular cloning of a calmodulin-dependent phosphatase from murine testis: identification of a developmentally expressed nonneural isoenzyme. Proc Natl Acad Sci USA 1992;89:529-33.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 529-533
    • Muramatsu, T.1    Giri, P.R.2    Higuchi, S.3    Kincaid, R.L.4
  • 26
    • 0028809939 scopus 로고
    • Drosophila PPY, a novel male specific protein serine/ threonine phosphatase localised in somatic cells of the testis
    • [26] Armstrong CG, Mann DJ, Berndt N, Cohen PTW. Drosophila PPY, a novel male specific protein serine/ threonine phosphatase localised in somatic cells of the testis. J Cell Sci 1995;108:3367-75.
    • (1995) J Cell Sci , vol.108 , pp. 3367-3375
    • Armstrong, C.G.1    Mann, D.J.2    Berndt, N.3    Cohen, P.T.W.4
  • 27
    • 0029294569 scopus 로고
    • A novel arabidopsis type 1 protein phosphatase is highly expressed in male and female tissues and functionally complements a conditional cell cycle mutant of Aspergillus
    • [27] Arundhati A, Feiler H, Traas J, Zhang H, Lunness PA, Doonan JH. A novel Arabidopsis type 1 protein phosphatase is highly expressed in male and female tissues and functionally complements a conditional cell cycle mutant of Aspergillus. Plant J 1995;7:823-34.
    • (1995) Plant J , vol.7 , pp. 823-834
    • Arundhati, A.1    Feiler, H.2    Traas, J.3    Zhang, H.4    Lunness, P.A.5    Doonan, J.H.6
  • 29
    • 0027368938 scopus 로고
    • Use of pharmacological agents to implicate a role for phosphoinositide hydrolysis products in malaria gamete formation
    • [29] Ogwan'g R, Mwangi J, Gachihi G, Nwachukwu A, Roberts CR, Martin SK. Use of pharmacological agents to implicate a role for phosphoinositide hydrolysis products in malaria gamete formation. Biochem Pharmacol 1993;46:1601-6.
    • (1993) Biochem Pharmacol , vol.46 , pp. 1601-1606
    • Ogwan'g, R.1    Mwangi, J.2    Gachihi, G.3    Nwachukwu, A.4    Roberts, C.R.5    Martin, S.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.