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Volumn 280, Issue 14, 2013, Pages 3220-3231

Thioredoxin h regulates calcium dependent protein kinases in plasma membranes

Author keywords

Arabidopsis thaliana; calcium signaling; plasma membrane; redox regulation; thioredoxin

Indexed keywords

CALCIUM DEPENDENT PROTEIN KINASE 21; CALPAIN; DSBA PROTEIN; HYDROGEN PEROXIDE; NEURONAL CALCIUM SENSOR; PHOSPHOINOSITIDE SPECIFIC PHOSPHOLIPASE 2; THIOREDOXIN; THIOREDOXIN H; UNCLASSIFIED DRUG;

EID: 84879976378     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12301     Document Type: Article
Times cited : (27)

References (44)
  • 1
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan BB, (1980) Role of light in the regulation of chloroplast enzymes. Annu Rev Plant Physiol 31, 341-374.
    • (1980) Annu Rev Plant Physiol , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 3
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan BB, &, Balmer Y, (2005) Redox regulation: a broadening horizon. Annu Rev Plant Biol 56, 187-220.
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 4
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Gene Initiative.
    • Arabidopsis Gene Initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408, 796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 5
    • 0036119804 scopus 로고    scopus 로고
    • Classification of plant thioredoxins by sequence similarity and intron position
    • Meyer Y, Vignols F, Reichheld JP, Sies H, &, Packer L, (2002) Classification of plant thioredoxins by sequence similarity and intron position. Methods Enzymol 347, 394-402.
    • (2002) Methods Enzymol , vol.347 , pp. 394-402
    • Meyer, Y.1    Vignols, F.2    Reichheld, J.P.3    Sies, H.4    Packer, L.5
  • 7
    • 0024110181 scopus 로고
    • An NADP/thioredoxin system in leaves: Purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach
    • Florencio FJ, Yee BC, Johnson TC, &, Buchanan BB, (1988) An NADP/thioredoxin system in leaves: purification and characterization of NADP-thioredoxin reductase and thioredoxin h from spinach. Arch Biochem Biophys 266, 496-507.
    • (1988) Arch Biochem Biophys , vol.266 , pp. 496-507
    • Florencio, F.J.1    Yee, B.C.2    Johnson, T.C.3    Buchanan, B.B.4
  • 8
    • 0142042960 scopus 로고    scopus 로고
    • Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves
    • Igamberdiev AU, &, Gardeström P, (2003) Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves. Biochim Biophys Acta 1606, 117-125.
    • (2003) Biochim Biophys Acta , vol.1606 , pp. 117-125
    • Igamberdiev, A.U.1    Gardeström, P.2
  • 9
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq L, Vignols F, Jacquot J-P, Chartier Y, &, Meyer Y, (1999) In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J Biol Chem 274, 19714-19722.
    • (1999) J Biol Chem , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Vignols, F.2    Jacquot, J.-P.3    Chartier, Y.4    Meyer, Y.5
  • 11
    • 0038662709 scopus 로고    scopus 로고
    • Thioredoxin and germinating barley: Targets and protein redox changes
    • Marx C, Wong J, &, Buchanan B, (2003) Thioredoxin and germinating barley: targets and protein redox changes. Planta 216, 454-460.
    • (2003) Planta , vol.216 , pp. 454-460
    • Marx, C.1    Wong, J.2    Buchanan, B.3
  • 14
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thioredoxin
    • Motohashi K, Kondoh A, Stumpp MT, &, Hisabori T, (2001) Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proc Natl Acad Sci USA 98, 11224-11229.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 15
    • 0035983609 scopus 로고    scopus 로고
    • Calcium signaling through protein kinases. The arabidopsis calcium-dependent protein kinase gene family
    • Cheng S-H, Willmann MR, &, Chen H-C, &, Sheen J, (2002) Calcium signaling through protein kinases. The arabidopsis calcium-dependent protein kinase gene family. Plant Physiol 129, 469-485.
    • (2002) Plant Physiol , vol.129 , pp. 469-485
    • Cheng, S.-H.1    Willmann, M.R.2    Chen, H.-C.3    Sheen, J.4
  • 19
    • 33748743864 scopus 로고    scopus 로고
    • Calcium-regulated phosphorylation of soybean serine acetyltransferase in response to oxidative stress
    • Liu F, Yoo B-C, &, Lee J-Y, Pan W, &, Harmon AC, (2006) Calcium-regulated phosphorylation of soybean serine acetyltransferase in response to oxidative stress. J Biol Chem 281, 27405-27415.
    • (2006) J Biol Chem , vol.281 , pp. 27405-27415
    • Liu, F.1    Yoo, B.-C.2    Lee, J.-Y.3    Pan, W.4    Harmon, A.C.5
  • 20
    • 34250728188 scopus 로고    scopus 로고
    • Calcium-dependent protein kinases regulate the production of reactive oxygen species by potato NADPH oxidase
    • Kobayashi M, Ohura I, Kawakita K, Yokota N, Fujiwara M, Shimamoto K, Doke N, &, Yoshioka H, (2007) Calcium-dependent protein kinases regulate the production of reactive oxygen species by potato NADPH oxidase. Plant Cell 19, 1065-1080.
    • (2007) Plant Cell , vol.19 , pp. 1065-1080
    • Kobayashi, M.1    Ohura, I.2    Kawakita, K.3    Yokota, N.4    Fujiwara, M.5    Shimamoto, K.6    Doke, N.7    Yoshioka, H.8
  • 21
    • 0030110747 scopus 로고    scopus 로고
    • Expression of three members of the calcium-dependent protein kinase gene family in Arabidopsis thaliana
    • Hong Y, Takano M, Liu C-M, Gasch A, &, Chye M-L, &, Chua N-H, (1996) Expression of three members of the calcium-dependent protein kinase gene family in Arabidopsis thaliana. Plant Mol Biol 30, 1259-1275.
    • (1996) Plant Mol Biol , vol.30 , pp. 1259-1275
    • Hong, Y.1    Takano, M.2    Liu, C.-M.3    Gasch, A.4    Chye, M.-L.5    Chua, N.-H.6
  • 22
    • 0032510705 scopus 로고    scopus 로고
    • Kinetic and calcium-binding properties of three calcium-dependent protein kinase isoenzymes from soybean
    • Lee JY, Yoo BC, &, Harmon AC, (1998) Kinetic and calcium-binding properties of three calcium-dependent protein kinase isoenzymes from soybean. Biochemistry 37, 6801-6809.
    • (1998) Biochemistry , vol.37 , pp. 6801-6809
    • Lee, J.Y.1    Yoo, B.C.2    Harmon, A.C.3
  • 23
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modeling
    • Arnold K, Bordoli L, Kopp J, &, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modeling. Bioinformatics 22, 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 24
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, &, Wüthrich K, (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14, 51-55.
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 25
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert LI, &, Jakob U, (2004) Protein thiol modifications visualized in vivo. PLoS Biol 2, e333.
    • (2004) PLoS Biol , vol.2
    • Leichert, L.I.1    Jakob, U.2
  • 26
    • 62549090194 scopus 로고    scopus 로고
    • A tobacco calcium-dependent protein kinase, CDPK1, regulates the transcription factor REPRESSION of SHOOT GROWTH in response to gibberellins
    • Ishida S, Yuasa T, Nakata M, &, Takahashi Y, (2008) A tobacco calcium-dependent protein kinase, CDPK1, regulates the transcription factor REPRESSION OF SHOOT GROWTH in response to gibberellins. Plant Cell 20, 3273-3288.
    • (2008) Plant Cell , vol.20 , pp. 3273-3288
    • Ishida, S.1    Yuasa, T.2    Nakata, M.3    Takahashi, Y.4
  • 29
    • 1942437463 scopus 로고    scopus 로고
    • Inverse regulation of rotation of F1-ATPase by the mutation at the regulatory region on the γ subunit of chloroplast ATP synthase
    • Ueoka-Nakanishi H, Nakanishi Y, Konno H, Motohashi K, Bald D, &, Hisabori T, (2004) Inverse regulation of rotation of F1-ATPase by the mutation at the regulatory region on the γ subunit of chloroplast ATP synthase. J Biol Chem 279, 16272-16277.
    • (2004) J Biol Chem , vol.279 , pp. 16272-16277
    • Ueoka-Nakanishi, H.1    Nakanishi, Y.2    Konno, H.3    Motohashi, K.4    Bald, D.5    Hisabori, T.6
  • 30
    • 0032560489 scopus 로고    scopus 로고
    • The structural basis for substrate recognition and control by protein kinases
    • Johnson LN, Lowe ED, Noble MEM, &, Owen DJ, (1998) The structural basis for substrate recognition and control by protein kinases. FEBS Lett 430, 1-11.
    • (1998) FEBS Lett , vol.430 , pp. 1-11
    • Johnson, L.N.1    Lowe, E.D.2    Noble, M.E.M.3    Owen, D.J.4
  • 31
    • 0028171293 scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79, 583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 32
    • 0037237973 scopus 로고    scopus 로고
    • Antioxidants, oxidative damage and oxygen deprivation stress
    • Blokhina O, Virolainen E, &, Fagerstedt KV, (2003) Antioxidants, oxidative damage and oxygen deprivation stress. Ann Bot 91, 179-194.
    • (2003) Ann Bot , vol.91 , pp. 179-194
    • Blokhina, O.1    Virolainen, E.2    Fagerstedt, K.V.3
  • 33
    • 0038826955 scopus 로고    scopus 로고
    • Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes
    • Mou Z, Fan W, &, Dong X, (2003) Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes. Cell 113, 935-944.
    • (2003) Cell , vol.113 , pp. 935-944
    • Mou, Z.1    Fan, W.2    Dong, X.3
  • 34
    • 0000520177 scopus 로고
    • A protocol for transient gene expression in Arabidopsis thaliana protoplasts isolated from cell-suspension cultures
    • Axelos M, Curie C, Mazzolini L, Bardet C, &, Lescure B, (1992) A protocol for transient gene expression in Arabidopsis thaliana protoplasts isolated from cell-suspension cultures. Plant Physiol Biochem 30, 123-128.
    • (1992) Plant Physiol Biochem , vol.30 , pp. 123-128
    • Axelos, M.1    Curie, C.2    Mazzolini, L.3    Bardet, C.4    Lescure, B.5
  • 35
    • 7044284712 scopus 로고    scopus 로고
    • Rapid response of Arabidopsis T87 cultured cells to cytokinin through His-to-Asp phosphorelay signal transduction
    • Yamada H, Koizumi N, Nakamichi N, Kiba T, Yamashino T, &, Mizuno T, (2004) Rapid response of Arabidopsis T87 cultured cells to cytokinin through His-to-Asp phosphorelay signal transduction. Biosci Biotech Biochem 68, 1966-1976.
    • (2004) Biosci Biotech Biochem , vol.68 , pp. 1966-1976
    • Yamada, H.1    Koizumi, N.2    Nakamichi, N.3    Kiba, T.4    Yamashino, T.5    Mizuno, T.6
  • 36
    • 0000592150 scopus 로고
    • Isolation and identification of plasma membrane from light-grown winter rye seedlings (Secale cereale L. cv Puma)
    • Uemura M, &, Yoshida S, (1983) Isolation and identification of plasma membrane from light-grown winter rye seedlings (Secale cereale L. cv Puma). Plant Physiol 73, 586-597.
    • (1983) Plant Physiol , vol.73 , pp. 586-597
    • Uemura, M.1    Yoshida, S.2
  • 37
    • 0041856169 scopus 로고    scopus 로고
    • Chloroplast cyclophilin is a target protein of thioredoxin: Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity
    • Motohashi K, Koyama F, Nakanishi Y, Ueoka-Nakanishi H, &, Hisabori T, (2003) Chloroplast cyclophilin is a target protein of thioredoxin: thiol modulation of the peptidyl-prolyl cis-trans isomerase activity. J Biol Chem 278, 31848-31852.
    • (2003) J Biol Chem , vol.278 , pp. 31848-31852
    • Motohashi, K.1    Koyama, F.2    Nakanishi, Y.3    Ueoka-Nakanishi, H.4    Hisabori, T.5
  • 38
    • 0242291099 scopus 로고    scopus 로고
    • Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins
    • Yu YQ, Gilar M, Lee PJ, Bouvier ESP, &, Gebler JC, (2003) Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins. Anal Chem 75, 6023-6028.
    • (2003) Anal Chem , vol.75 , pp. 6023-6028
    • Yu, Y.Q.1    Gilar, M.2    Lee, P.J.3    Bouvier, E.S.P.4    Gebler, J.C.5
  • 39
    • 1442325497 scopus 로고    scopus 로고
    • Acid-labile surfactant improves in-sodium dodecyl sulfate polyacrylamide gel protein digestion for matrix-assisted laser desorption/ionization mass spectrometric peptide mapping
    • Nomura E, Katsuta K, Ueda T, Toriyama M, Mori T, &, Inagaki N, (2004) Acid-labile surfactant improves in-sodium dodecyl sulfate polyacrylamide gel protein digestion for matrix-assisted laser desorption/ionization mass spectrometric peptide mapping. J Mass Spectrom 39, 202-207.
    • (2004) J Mass Spectrom , vol.39 , pp. 202-207
    • Nomura, E.1    Katsuta, K.2    Ueda, T.3    Toriyama, M.4    Mori, T.5    Inagaki, N.6
  • 40
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis
    • Rosenfeld J, Capdevielle J, Guillemot JC, &, Ferrara P, (1992) In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal Biochem 203, 173-179.
    • (1992) Anal Biochem , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 41
    • 3242734183 scopus 로고    scopus 로고
    • Improvement in the detection of low concentration protein digests on a MALDI TOF/TOF workstation by reducing α-cyano-4-hydroxycinnamic acid adduct ions
    • Zhu X, &, Papayannopoulos IA, (2003) Improvement in the detection of low concentration protein digests on a MALDI TOF/TOF workstation by reducing α-cyano-4-hydroxycinnamic acid adduct ions. J Biomol Tech 14, 298-307.
    • (2003) J Biomol Tech , vol.14 , pp. 298-307
    • Zhu, X.1    Papayannopoulos, I.A.2
  • 42
    • 0028247009 scopus 로고
    • Pseudosubstrate inhibition of CDPK, a protein kinase with a calmodulin-like domain
    • Harmon AC, Yoo B-C, &, McCaffery C, (1994) Pseudosubstrate inhibition of CDPK, a protein kinase with a calmodulin-like domain. Biochemistry 33, 7278-7287.
    • (1994) Biochemistry , vol.33 , pp. 7278-7287
    • Harmon, A.C.1    Yoo, B.-C.2    McCaffery, C.3
  • 43
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, &, Gordon J, (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76, 4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 44
    • 0742305352 scopus 로고    scopus 로고
    • The endoplasmic reticulum membrane is permeable to small molecules
    • Le Gall S, Neuhof A, &, Rapoport T, (2004) The endoplasmic reticulum membrane is permeable to small molecules. Mol Biol Cell 15, 447-455.
    • (2004) Mol Biol Cell , vol.15 , pp. 447-455
    • Le Gall, S.1    Neuhof, A.2    Rapoport, T.3


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