메뉴 건너뛰기




Volumn 14, Issue 10, 2012, Pages 825-830

Calcium dependent protein kinase 1 and calcium fluxes in the malaria parasite

Author keywords

Actomyosin motor complex; Alveoli; Calcium dependent protein kinase; Calcium release channels; Inner membrane complex; Malaria

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CALCIUM DEPENDENT PROTEIN KINASE 1; MYOSIN LIGHT CHAIN; PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN; PROTEIN INHIBITOR; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 84863818787     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2012.04.006     Document Type: Article
Times cited : (34)

References (63)
  • 1
    • 21744457120 scopus 로고    scopus 로고
    • Plants, symbiosis and parasites: a calcium signalling connection
    • Harper J.F., Harmon A. Plants, symbiosis and parasites: a calcium signalling connection. Nat. Rev. Mol. Cell Biol. 2005, 6:555-566.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 555-566
    • Harper, J.F.1    Harmon, A.2
  • 2
    • 33751021696 scopus 로고    scopus 로고
    • Purification and characterization of a calcium-dependent protein kinase from beetroot plasma membranes
    • Lino B., Carrillo-Rayas M.T., Chagolla A., Gonzalez de la Vara L.E. Purification and characterization of a calcium-dependent protein kinase from beetroot plasma membranes. Planta 2006, 225:255-268.
    • (2006) Planta , vol.225 , pp. 255-268
    • Lino, B.1    Carrillo-Rayas, M.T.2    Chagolla, A.3    Gonzalez de la Vara, L.E.4
  • 3
    • 77951217925 scopus 로고    scopus 로고
    • Tobacco calcium-dependent protein kinases are differentially phosphorylated in vivo as part of a kinase cascade that regulates stress response
    • Witte C.P., Keinath N., Dubiella U., Demouliere R., Seal A., Romeis T. Tobacco calcium-dependent protein kinases are differentially phosphorylated in vivo as part of a kinase cascade that regulates stress response. J. Biol. Chem. 2010, 285:9740-9748.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9740-9748
    • Witte, C.P.1    Keinath, N.2    Dubiella, U.3    Demouliere, R.4    Seal, A.5    Romeis, T.6
  • 8
    • 67649399023 scopus 로고    scopus 로고
    • Calcium-dependent signaling and kinases in apicomplexan parasites
    • Billker O., Lourido S., Sibley L.D. Calcium-dependent signaling and kinases in apicomplexan parasites. Cell Host Microbe 2009, 5:612-622.
    • (2009) Cell Host Microbe , vol.5 , pp. 612-622
    • Billker, O.1    Lourido, S.2    Sibley, L.D.3
  • 9
    • 9144258616 scopus 로고    scopus 로고
    • Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote
    • Ward P., Equinet L., Packer J., Doerig C. Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote. BMC Genomics 2004, 5:79.
    • (2004) BMC Genomics , vol.5 , pp. 79
    • Ward, P.1    Equinet, L.2    Packer, J.3    Doerig, C.4
  • 10
    • 80055105428 scopus 로고    scopus 로고
    • Structural and evolutionary divergence of eukaryotic protein kinases in Apicomplexa
    • Talevich E., Mirza A., Kannan N. Structural and evolutionary divergence of eukaryotic protein kinases in Apicomplexa. BMC Evol. Biol. 2011, 11:321.
    • (2011) BMC Evol. Biol. , vol.11 , pp. 321
    • Talevich, E.1    Mirza, A.2    Kannan, N.3
  • 11
    • 77958094517 scopus 로고    scopus 로고
    • The systematic functional analysis of Plasmodium protein kinases identifies essential regulators of mosquito transmission
    • Tewari R., Straschil U., Bateman A., Bohme U., Cherevach I., Gong P., Pain A., Billker O. The systematic functional analysis of Plasmodium protein kinases identifies essential regulators of mosquito transmission. Cell Host Microbe 2010, 8:377-387.
    • (2010) Cell Host Microbe , vol.8 , pp. 377-387
    • Tewari, R.1    Straschil, U.2    Bateman, A.3    Bohme, U.4    Cherevach, I.5    Gong, P.6    Pain, A.7    Billker, O.8
  • 13
    • 2342611064 scopus 로고    scopus 로고
    • Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite
    • Billker O., Dechamps S., Tewari R., Wenig G., Franke-Fayard B., Brinkmann V. Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite. Cell 2004, 117:503-514.
    • (2004) Cell , vol.117 , pp. 503-514
    • Billker, O.1    Dechamps, S.2    Tewari, R.3    Wenig, G.4    Franke-Fayard, B.5    Brinkmann, V.6
  • 15
    • 33645077874 scopus 로고    scopus 로고
    • A calcium-dependent protein kinase regulates Plasmodium ookinete access to the midgut epithelial cell
    • Ishino T., Orito Y., Chinzei Y., Yuda M. A calcium-dependent protein kinase regulates Plasmodium ookinete access to the midgut epithelial cell. Mol. Microbiol. 2006, 59:1175-1184.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1175-1184
    • Ishino, T.1    Orito, Y.2    Chinzei, Y.3    Yuda, M.4
  • 16
    • 33744482044 scopus 로고    scopus 로고
    • Plasmodium berghei calcium-dependent protein kinase 3 is required for ookinete gliding motility and mosquito midgut invasion
    • Siden-Kiamos I., Ecker A., Nyback S., Louis C., Sinden R.E., Billker O. Plasmodium berghei calcium-dependent protein kinase 3 is required for ookinete gliding motility and mosquito midgut invasion. Mol. Microbiol. 2006, 60:1355-1363.
    • (2006) Mol. Microbiol. , vol.60 , pp. 1355-1363
    • Siden-Kiamos, I.1    Ecker, A.2    Nyback, S.3    Louis, C.4    Sinden, R.E.5    Billker, O.6
  • 18
    • 2442528540 scopus 로고    scopus 로고
    • Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii
    • Gaskins E., Gilk S., DeVore N., Mann T., Ward G., Beckers C. Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii. J. Cell Biol. 2004, 165:383-393.
    • (2004) J. Cell Biol. , vol.165 , pp. 383-393
    • Gaskins, E.1    Gilk, S.2    DeVore, N.3    Mann, T.4    Ward, G.5    Beckers, C.6
  • 19
    • 33645306878 scopus 로고    scopus 로고
    • A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites
    • Baum J., Richard D., Healer J., Rug M., Krnajski Z., Gilberger T.W., Green J.L., Holder A.A., Cowman A.F. A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites. J. Biol. Chem. 2006, 281:5197-5208.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5197-5208
    • Baum, J.1    Richard, D.2    Healer, J.3    Rug, M.4    Krnajski, Z.5    Gilberger, T.W.6    Green, J.L.7    Holder, A.A.8    Cowman, A.F.9
  • 20
    • 7644221040 scopus 로고    scopus 로고
    • Export of Plasmodium falciparum calcium-dependent protein kinase 1 to the parasitophorous vacuole is dependent on three N-terminal membrane anchor motifs
    • Moskes C., Burghaus P.A., Wernli B., Sauder U., Durrenberger M., Kappes B. Export of Plasmodium falciparum calcium-dependent protein kinase 1 to the parasitophorous vacuole is dependent on three N-terminal membrane anchor motifs. Mol. Microbiol. 2004, 54:676-691.
    • (2004) Mol. Microbiol. , vol.54 , pp. 676-691
    • Moskes, C.1    Burghaus, P.A.2    Wernli, B.3    Sauder, U.4    Durrenberger, M.5    Kappes, B.6
  • 24
    • 80054901700 scopus 로고    scopus 로고
    • The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries
    • Treeck M., Sanders J.L., Elias J.E., Boothroyd J.C. The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries. Cell Host Microbe 2011, 10:410-419.
    • (2011) Cell Host Microbe , vol.10 , pp. 410-419
    • Treeck, M.1    Sanders, J.L.2    Elias, J.E.3    Boothroyd, J.C.4
  • 25
    • 33845292589 scopus 로고    scopus 로고
    • Raf kinase inhibitor protein affects activity of Plasmodium falciparum calcium-dependent protein kinase 1
    • Kugelstadt D., Winter D., Pluckhahn K., Lehmann W.D., Kappes B. Raf kinase inhibitor protein affects activity of Plasmodium falciparum calcium-dependent protein kinase 1. Mol. Biochem. Parasitol. 2007, 151:111-117.
    • (2007) Mol. Biochem. Parasitol. , vol.151 , pp. 111-117
    • Kugelstadt, D.1    Winter, D.2    Pluckhahn, K.3    Lehmann, W.D.4    Kappes, B.5
  • 26
    • 84859152006 scopus 로고    scopus 로고
    • Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development
    • Ridzuan M.A., Moon R.W., Knuepfer E., Black S., Holder A.A., Green J.L. Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development. PLoS One 2012, 7:e33845.
    • (2012) PLoS One , vol.7
    • Ridzuan, M.A.1    Moon, R.W.2    Knuepfer, E.3    Black, S.4    Holder, A.A.5    Green, J.L.6
  • 27
    • 67651004664 scopus 로고    scopus 로고
    • Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated Plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry
    • Winter D., Kugelstadt D., Seidler J., Kappes B., Lehmann W.D. Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated Plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry. Anal. Biochem. 2009, 393:41-47.
    • (2009) Anal. Biochem. , vol.393 , pp. 41-47
    • Winter, D.1    Kugelstadt, D.2    Seidler, J.3    Kappes, B.4    Lehmann, W.D.5
  • 28
    • 36348997151 scopus 로고    scopus 로고
    • A chemical-genetic approach to elucidate protein kinase function in planta
    • Bohmer M., Romeis T. A chemical-genetic approach to elucidate protein kinase function in planta. Plant Mol. Biol. 2007, 65:817-827.
    • (2007) Plant Mol. Biol. , vol.65 , pp. 817-827
    • Bohmer, M.1    Romeis, T.2
  • 29
    • 33748753548 scopus 로고    scopus 로고
    • PfPKB, a protein kinase B-like enzyme from Plasmodium falciparum: II. Identification of calcium/calmodulin as its upstream activator and dissection of a novel signaling pathway
    • Vaid A., Sharma P. PfPKB, a protein kinase B-like enzyme from Plasmodium falciparum: II. Identification of calcium/calmodulin as its upstream activator and dissection of a novel signaling pathway. J. Biol. Chem. 2006, 281:27126-27133.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27126-27133
    • Vaid, A.1    Sharma, P.2
  • 30
    • 41949086426 scopus 로고    scopus 로고
    • 2+/calmodulin-PfPKB signaling pathway in erythrocyte invasion by Plasmodium falciparum
    • 2+/calmodulin-PfPKB signaling pathway in erythrocyte invasion by Plasmodium falciparum. J. Biol. Chem. 2008, 283:5589-5597.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5589-5597
    • Vaid, A.1    Thomas, D.C.2    Sharma, P.3
  • 31
    • 59249083317 scopus 로고    scopus 로고
    • GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex
    • Gilk S.D., Gaskins E., Ward G.E., Beckers C.J. GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex. Eukaryot. Cell 2009, 8:190-196.
    • (2009) Eukaryot. Cell , vol.8 , pp. 190-196
    • Gilk, S.D.1    Gaskins, E.2    Ward, G.E.3    Beckers, C.J.4
  • 34
    • 0034788662 scopus 로고    scopus 로고
    • Calcium regulation in the intraerythrocytic malaria parasite Plasmodium falciparum
    • Alleva L.M., Kirk K. Calcium regulation in the intraerythrocytic malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 2001, 117:121-128.
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 121-128
    • Alleva, L.M.1    Kirk, K.2
  • 35
    • 77649263117 scopus 로고    scopus 로고
    • Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites
    • Singh S., Alam M.M., Pal-Bhowmick I., Brzostowski J.A., Chitnis C.E. Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites. PLoS Pathog. 2010, 6:e1000746.
    • (2010) PLoS Pathog. , vol.6
    • Singh, S.1    Alam, M.M.2    Pal-Bhowmick, I.3    Brzostowski, J.A.4    Chitnis, C.E.5
  • 36
    • 84863817173 scopus 로고    scopus 로고
    • Signaling mechanisms involved in apical organelle discharge during invasion of apicomplexan parasites
    • Singh S., Chitnis C.E. Signaling mechanisms involved in apical organelle discharge during invasion of apicomplexan parasites. Microbes Infect. 2012, 14:820-824.
    • (2012) Microbes Infect. , vol.14 , pp. 820-824
    • Singh, S.1    Chitnis, C.E.2
  • 37
    • 84863811575 scopus 로고    scopus 로고
    • Generation of second messengers in Plasmodium
    • Budu A., Garcia C.R. Generation of second messengers in Plasmodium. Microbes Infect. 2012, 14:787-795.
    • (2012) Microbes Infect. , vol.14 , pp. 787-795
    • Budu, A.1    Garcia, C.R.2
  • 38
    • 0033976150 scopus 로고    scopus 로고
    • Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases
    • Ponting C.P. Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases. Trends Biochem. Sci. 2000, 25:48-50.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 48-50
    • Ponting, C.P.1
  • 39
    • 84862591342 scopus 로고    scopus 로고
    • Calcium storage and function in apicomplexan parasites
    • Moreno S.N., Ayong L., Pace D.A. Calcium storage and function in apicomplexan parasites. Essays Biochem. 2011, 51:97-110.
    • (2011) Essays Biochem. , vol.51 , pp. 97-110
    • Moreno, S.N.1    Ayong, L.2    Pace, D.A.3
  • 41
    • 0033224351 scopus 로고    scopus 로고
    • Secretion of micronemal proteins is associated with toxoplasma invasion of host cells
    • Carruthers V.B., Giddings O.K., Sibley L.D. Secretion of micronemal proteins is associated with toxoplasma invasion of host cells. Cell. Microbiol. 1999, 1:225-235.
    • (1999) Cell. Microbiol. , vol.1 , pp. 225-235
    • Carruthers, V.B.1    Giddings, O.K.2    Sibley, L.D.3
  • 42
    • 0033485874 scopus 로고    scopus 로고
    • Calcium homeostasis and signaling in the blood-stage malaria parasite
    • Garcia C.R. Calcium homeostasis and signaling in the blood-stage malaria parasite. Parasitol. Today 1999, 15:488-491.
    • (1999) Parasitol. Today , vol.15 , pp. 488-491
    • Garcia, C.R.1
  • 43
    • 0032492553 scopus 로고    scopus 로고
    • 2+ release from chloroquine-sensitive and -insensitive intracellular stores in the intraerythrocytic stage of the malaria parasite P. chabaudi
    • 2+ release from chloroquine-sensitive and -insensitive intracellular stores in the intraerythrocytic stage of the malaria parasite P. chabaudi. Biochem. Biophys. Res. Commun. 1998, 245:155-160.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 155-160
    • Passos, A.P.1    Garcia, C.R.2
  • 46
    • 23044501275 scopus 로고    scopus 로고
    • Quantitative calcium measurements in subcellular compartments of Plasmodium falciparum-infected erythrocytes
    • Rohrbach P., Friedrich O., Hentschel J., Plattner H., Fink R.H., Lanzer M. Quantitative calcium measurements in subcellular compartments of Plasmodium falciparum-infected erythrocytes. J. Biol. Chem. 2005, 280:27960-27969.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27960-27969
    • Rohrbach, P.1    Friedrich, O.2    Hentschel, J.3    Plattner, H.4    Fink, R.H.5    Lanzer, M.6
  • 48
    • 79953129603 scopus 로고    scopus 로고
    • 2+ release from intracellular stores in the malaria parasite Plasmodium falciparum within infected red blood cells
    • 2+ release from intracellular stores in the malaria parasite Plasmodium falciparum within infected red blood cells. J. Biol. Chem. 2011, 286:5905-5912.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5905-5912
    • Alves, E.1    Bartlett, P.J.2    Garcia, C.R.3    Thomas, A.P.4
  • 53
    • 6444243291 scopus 로고    scopus 로고
    • Polyphosphate content and fine structure of acidocalcisomes of Plasmodium falciparum
    • Ruiz F.A., Luo S., Moreno S.N., Docampo R. Polyphosphate content and fine structure of acidocalcisomes of Plasmodium falciparum. Microsc. Microanal 2004, 10:563-567.
    • (2004) Microsc. Microanal , vol.10 , pp. 563-567
    • Ruiz, F.A.1    Luo, S.2    Moreno, S.N.3    Docampo, R.4
  • 55
    • 0344805645 scopus 로고    scopus 로고
    • Calcium signaling in a low calcium environment: how the intracellular malaria parasite solves the problem
    • Gazarini M.L., Thomas A.P., Pozzan T., Garcia C.R. Calcium signaling in a low calcium environment: how the intracellular malaria parasite solves the problem. J. Cell Biol. 2003, 161:103-110.
    • (2003) J. Cell Biol. , vol.161 , pp. 103-110
    • Gazarini, M.L.1    Thomas, A.P.2    Pozzan, T.3    Garcia, C.R.4
  • 56
    • 0030971213 scopus 로고    scopus 로고
    • Differential distribution of calcium stores in paramecium cells. Occurrence of a subplasmalemmal store with a calsequestrin-like protein
    • Plattner H., Habermann A., Kissmehl R., Klauke N., Majoul I., Soling H.D. Differential distribution of calcium stores in paramecium cells. Occurrence of a subplasmalemmal store with a calsequestrin-like protein. Eur. J. Cell Biol. 1997, 72:297-306.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 297-306
    • Plattner, H.1    Habermann, A.2    Kissmehl, R.3    Klauke, N.4    Majoul, I.5    Soling, H.D.6
  • 57
    • 0033781424 scopus 로고    scopus 로고
    • Calcium in ciliated protozoa: sources, regulation, and calcium-regulated cell functions
    • Plattner H., Klauke N. Calcium in ciliated protozoa: sources, regulation, and calcium-regulated cell functions. Int. Rev. Cytol. 2001, 201:115-208.
    • (2001) Int. Rev. Cytol. , vol.201 , pp. 115-208
    • Plattner, H.1    Klauke, N.2
  • 58
    • 80755159559 scopus 로고    scopus 로고
    • Calcium-release channels in paramecium. Genomic expansion, differential positioning and partial transcriptional elimination
    • Ladenburger E.M., Plattner H. Calcium-release channels in paramecium. Genomic expansion, differential positioning and partial transcriptional elimination. PLoS One 2011, 6:e27111.
    • (2011) PLoS One , vol.6
    • Ladenburger, E.M.1    Plattner, H.2
  • 60
    • 80054097452 scopus 로고    scopus 로고
    • Identification of intracellular and plasma membrane calcium channel homologues in pathogenic parasites
    • Prole D.L., Taylor C.W. Identification of intracellular and plasma membrane calcium channel homologues in pathogenic parasites. PLoS One 2011, 6:e26218.
    • (2011) PLoS One , vol.6
    • Prole, D.L.1    Taylor, C.W.2
  • 61
    • 70350410122 scopus 로고    scopus 로고
    • Membrane transport proteins of the malaria parasite
    • Martin R.E., Ginsburg H., Kirk K. Membrane transport proteins of the malaria parasite. Mol. Microbiol. 2009, 74:519-528.
    • (2009) Mol. Microbiol. , vol.74 , pp. 519-528
    • Martin, R.E.1    Ginsburg, H.2    Kirk, K.3
  • 62
    • 24144480800 scopus 로고    scopus 로고
    • The 'permeome' of the malaria parasite: an overview of the membrane transport proteins of Plasmodium falciparum
    • Martin R.E., Henry R.I., Abbey J.L., Clements J.D., Kirk K. The 'permeome' of the malaria parasite: an overview of the membrane transport proteins of Plasmodium falciparum. Genome Biol. 2005, 6:R26.
    • (2005) Genome Biol. , vol.6
    • Martin, R.E.1    Henry, R.I.2    Abbey, J.L.3    Clements, J.D.4    Kirk, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.