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Volumn 374, Issue 2, 2003, Pages 381-391

dDYRK2: A novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila

Author keywords

Development; Drosophila; Dual specificity kinase; Dual specificity tyrosine phosphorylation regulated kinase (DYRK); Minibrain

Indexed keywords

BIOLOGICAL MEMBRANES; ENZYME KINETICS; PROTEINS;

EID: 0042330069     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030500     Document Type: Article
Times cited : (37)

References (38)
  • 1
    • 0032603540 scopus 로고    scopus 로고
    • Structural and functional characteristics of Dyrk, a novel subfamily of protein kinases with dual specificity
    • Becker, W. and Joost, H. G. (1999) Structural and functional characteristics of Dyrk, a novel subfamily of protein kinases with dual specificity. Prog. Nucleic Acid Res. Mol. Biol. 62, 1-17
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.62 , pp. 1-17
    • Becker, W.1    Joost, H.G.2
  • 2
    • 0033590164 scopus 로고    scopus 로고
    • Distantly related cousins of MAP kinase: Biochemical properties and possible physiological functions
    • Miyata, Y. and Nishida, E. (1999) Distantly related cousins of MAP kinase: biochemical properties and possible physiological functions. Biochem. Biophys. Res. Commun. 266, 291-295
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 291-295
    • Miyata, Y.1    Nishida, E.2
  • 3
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human
    • Widmann, C., Gibson, S., Jarpe, M. B. and Johnson, G. L. (1999) Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 79, 143-180
    • (1999) Physiol. Rev. , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 4
    • 0034723403 scopus 로고    scopus 로고
    • Specificity determinants of substrate recognition by the protein kinase DYRK1A
    • Himpel, S., Tegge, W., Frank, R., Leder, S., Joost, H. G. and Becker, W. (2000) Specificity determinants of substrate recognition by the protein kinase DYRK1A. J. Biol. Chem. 275, 2431-2438
    • (2000) J. Biol. Chem. , vol.275 , pp. 2431-2438
    • Himpel, S.1    Tegge, W.2    Frank, R.3    Leder, S.4    Joost, H.G.5    Becker, W.6
  • 5
    • 0032475973 scopus 로고    scopus 로고
    • Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases
    • Becker, W., Weber, Y., Wetzel, K., Eirmbter, K., Tejedor, F. J. and Joost, H. G. (1998) Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases. J. Biol. Chem. 273, 25893-25902
    • (1998) J. Biol. Chem. , vol.273 , pp. 25893-25902
    • Becker, W.1    Weber, Y.2    Wetzel, K.3    Eirmbter, K.4    Tejedor, F.J.5    Joost, H.G.6
  • 6
    • 0024723687 scopus 로고
    • Loss of Ras activity in Saccharomyces cerevisiae is suppressed by disruptions of a new kinase gene, YAKI, whose product may act downstream of the cAMP-dependent protein kinase
    • Garrett, S. and Broach, J. (1989) Loss of Ras activity in Saccharomyces cerevisiae is suppressed by disruptions of a new kinase gene, YAKI, whose product may act downstream of the cAMP-dependent protein kinase. Genes Dev. 3, 1336-1348
    • (1989) Genes Dev. , vol.3 , pp. 1336-1348
    • Garrett, S.1    Broach, J.2
  • 7
    • 0025851170 scopus 로고
    • The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle
    • Garrett, S., Menold, M. M. and Broach, J. R. (1991) The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle. Mol. Cell. Biol. 11, 4045-4052
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4045-4052
    • Garrett, S.1    Menold, M.M.2    Broach, J.R.3
  • 8
    • 0032127462 scopus 로고    scopus 로고
    • Yeast PKA represses Msn2p/Msn4p-dependent gene expression to regulate growth, stress response and glycogen accumulation
    • Smith, A., Ward, M. P. and Garrett, S. (1998) Yeast PKA represses Msn2p/Msn4p-dependent gene expression to regulate growth, stress response and glycogen accumulation. EMBO J. 17, 3556-3564
    • (1998) EMBO J. , vol.17 , pp. 3556-3564
    • Smith, A.1    Ward, M.P.2    Garrett, S.3
  • 9
    • 0001019046 scopus 로고    scopus 로고
    • YakA, a protein kinase required for the transition from growth to development in Dictyostelium
    • Souza, G. M., Lu, S. and Kuspa, A. (1998) YakA, a protein kinase required for the transition from growth to development in Dictyostelium. Development 125, 2291-2302
    • (1998) Development , vol.125 , pp. 2291-2302
    • Souza, G.M.1    Lu, S.2    Kuspa, A.3
  • 10
    • 0040839027 scopus 로고    scopus 로고
    • Pom1p, a fission yeast protein kinase that provides positional information for both polarized growth and cytokinesis
    • Bahler, J. and Pringle, J. R. (1998) Pom1p, a fission yeast protein kinase that provides positional information for both polarized growth and cytokinesis. Genes Dev. 12, 1356-1370
    • (1998) Genes Dev. , vol.12 , pp. 1356-1370
    • Bahler, J.1    Pringle, J.R.2
  • 11
    • 0035283205 scopus 로고    scopus 로고
    • Fission yeast Pom1p kinase activity is cell cycle regulated and essential for cellular symmetry during growth and division
    • Bahler, J. and Nurse, P. (2001) Fission yeast Pom1p kinase activity is cell cycle regulated and essential for cellular symmetry during growth and division. EMBO J. 20, 1064-1073
    • (2001) EMBO J. , vol.20 , pp. 1064-1073
    • Bahler, J.1    Nurse, P.2
  • 13
    • 0033135902 scopus 로고    scopus 로고
    • Human minibrain homologue (MNBH/DYRK1): Characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome
    • Guimera, J., Casas, C., Estivill, X. and Pritchard, M. (1999) Human minibrain homologue (MNBH/DYRK1): characterization, alternative splicing, differential tissue expression, and overexpression in Down syndrome. Genomics 57, 407-418
    • (1999) Genomics , vol.57 , pp. 407-418
    • Guimera, J.1    Casas, C.2    Estivill, X.3    Pritchard, M.4
  • 17
    • 0035174668 scopus 로고    scopus 로고
    • A new expression cloning strategy for isolation of substrate-specific kinases by using phosphorylation site-specific antibody
    • Matsuo, R., Ochiai, W., Nakashima, K. and Taga, T. (2001) A new expression cloning strategy for isolation of substrate-specific kinases by using phosphorylation site-specific antibody. J. Immunol. Methods 247, 141-151
    • (2001) J. Immunol. Methods , vol.247 , pp. 141-151
    • Matsuo, R.1    Ochiai, W.2    Nakashima, K.3    Taga, T.4
  • 19
    • 0035873250 scopus 로고    scopus 로고
    • Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal
    • Moriya, H., Shimizu-Yoshida, Y., Omori, A., Iwashita, S., Katoh, M. and Sakai, A. (2001) Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal. Genes Dev. 15, 1217-1228
    • (2001) Genes Dev. , vol.15 , pp. 1217-1228
    • Moriya, H.1    Shimizu-Yoshida, Y.2    Omori, A.3    Iwashita, S.4    Katoh, M.5    Sakai, A.6
  • 20
    • 0037005887 scopus 로고    scopus 로고
    • Differing substrate specificities of members of the DYRK family of arginine-directed protein kinases
    • Campbell, L. E. and Proud, C. G. (2002) Differing substrate specificities of members of the DYRK family of arginine-directed protein kinases. FEBS Lett. 510, 31-36
    • (2002) FEBS Lett. , vol.510 , pp. 31-36
    • Campbell, L.E.1    Proud, C.G.2
  • 21
    • 0030022273 scopus 로고    scopus 로고
    • Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII
    • Kentrup, H., Becker, W., Heukelbach, J., Wilmes, A., Schurmann, A., Huppertz, C., Kainulainen, H. and Joost, H. G. (1996) Dyrk, a dual specificity protein kinase with unique structural features whose activity is dependent on tyrosine residues between subdomains VII and VIII. J. Biol. Chem. 271, 3488-3495
    • (1996) J. Biol. Chem. , vol.271 , pp. 3488-3495
    • Kentrup, H.1    Becker, W.2    Heukelbach, J.3    Wilmes, A.4    Schurmann, A.5    Huppertz, C.6    Kainulainen, H.7    Joost, H.G.8
  • 23
    • 0029960341 scopus 로고    scopus 로고
    • Effects of single P-element insertions on olfactory behavior in Drosophila melanogaster
    • Anholt, R. R., Lyman, R. F. and Mackay, T. F. (1996) Effects of single P-element insertions on olfactory behavior in Drosophila melanogaster. Genetics 143, 293-301
    • (1996) Genetics , vol.143 , pp. 293-301
    • Anholt, R.R.1    Lyman, R.F.2    Mackay, T.F.3
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0023691808 scopus 로고
    • Novel tyrosine kinase identified by phosphotyrosine antibody screening of cDNA libraries
    • Kornbluth, S., Paulson, K. E. and Hanafusa, H. (1988) Novel tyrosine kinase identified by phosphotyrosine antibody screening of cDNA libraries. Mol. Cell. Biol. 8, 5541-5544
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5541-5544
    • Kornbluth, S.1    Paulson, K.E.2    Hanafusa, H.3
  • 27
    • 0023664018 scopus 로고
    • Comparison of the consensus sequence flanking translational start sites in Drosophila and vertebrates
    • Cavener, D. R. (1987) Comparison of the consensus sequence flanking translational start sites in Drosophila and vertebrates. Nucleic Acids Res. 15, 1353-1361
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1353-1361
    • Cavener, D.R.1
  • 28
    • 0025832605 scopus 로고
    • Multiple components in an epidermal growth factor-stimulated protein kinase cascade: In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase
    • Ahn, N. G., Seger, R., Bratlien, R. L., Diltz, C. D., Tonks, N. K. and Krebs, E. G. (1991) Multiple components in an epidermal growth factor-stimulated protein kinase cascade: in vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase. J. Biol. Chem. 266, 4220-4227
    • (1991) J. Biol. Chem. , vol.266 , pp. 4220-4227
    • Ahn, N.G.1    Seger, R.2    Bratlien, R.L.3    Diltz, C.D.4    Tonks, N.K.5    Krebs, E.G.6
  • 30
    • 0027075932 scopus 로고
    • Extracellular signal-regulated kinases 2 autophosphorylates on a subset of peptides phosphorylated in intact cells in response to insulin and nerve growth factor: Analysis by peptide mapping
    • Robbins, D. J. and Cobb, M. H. (1992) Extracellular signal-regulated kinases 2 autophosphorylates on a subset of peptides phosphorylated in intact cells in response to insulin and nerve growth factor: analysis by peptide mapping. Mol. Biol. Cell 3, 299-308
    • (1992) Mol. Biol. Cell , vol.3 , pp. 299-308
    • Robbins, D.J.1    Cobb, M.H.2
  • 32
    • 0034235542 scopus 로고    scopus 로고
    • Mirk protein kinase is a mitogen-activated protein kinase substrate that mediates survival of colon cancer cells
    • Lee, K., Deng, X. and Friedman, E. (2000) Mirk protein kinase is a mitogen-activated protein kinase substrate that mediates survival of colon cancer cells. Cancer Res. 60, 3631-3637
    • (2000) Cancer Res. , vol.60 , pp. 3631-3637
    • Lee, K.1    Deng, X.2    Friedman, E.3
  • 33
    • 0034213189 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Yak1p protein kinase autophosphorylates on tyrosine residues and phosphorylates myelin basic protein on a C-terminal serine residue
    • Kassis, S., Melhuish, T., Annan, R. S., Chen, S. L., Lee, J. C., Livi, G. P. and Creasy, C. L. (2000) Saccharomyces cerevisiae Yak1p protein kinase autophosphorylates on tyrosine residues and phosphorylates myelin basic protein on a C-terminal serine residue. Biochem. J. 348, 263-272
    • (2000) Biochem. J. , vol.348 , pp. 263-272
    • Kassis, S.1    Melhuish, T.2    Annan, R.S.3    Chen, S.L.4    Lee, J.C.5    Livi, G.P.6    Creasy, C.L.7
  • 34
    • 0027475421 scopus 로고
    • Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation
    • Hughes, K., Nikolakaki, E., Plyte, S. E., Totty, N. F. and Woodgett, J. R. (1993) Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation. EMBO J. 12, 803-808
    • (1993) EMBO J. , vol.12 , pp. 803-808
    • Hughes, K.1    Nikolakaki, E.2    Plyte, S.E.3    Totty, N.F.4    Woodgett, J.R.5
  • 35
    • 0027932676 scopus 로고
    • Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: Determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis
    • Tokyo
    • Mansour, S. J., Resing, K. A., Candi, J. M., Hermann, A. S., Gloor, J. W., Herskind, K. R., Wartmann, M., Davis, R. J. and Ahn, N. G. (1994) Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis. J. Biochem. (Tokyo) 116, 304-314
    • (1994) J. Biochem. , vol.116 , pp. 304-314
    • Mansour, S.J.1    Resing, K.A.2    Candi, J.M.3    Hermann, A.S.4    Gloor, J.W.5    Herskind, K.R.6    Wartmann, M.7    Davis, R.J.8    Ahn, N.G.9
  • 36
    • 0035955696 scopus 로고    scopus 로고
    • Protein kinase Dyrk1 activates cAMP response element-binding protein during neuronal differentiation in hippocampal progenitor cells
    • Yang, E. J., Ahn, Y. S. and Chung, K. C. (2001) Protein kinase Dyrk1 activates cAMP response element-binding protein during neuronal differentiation in hippocampal progenitor cells. J. Biol. Chem. 276, 39819-39824
    • (2001) J. Biol. Chem. , vol.276 , pp. 39819-39824
    • Yang, E.J.1    Ahn, Y.S.2    Chung, K.C.3
  • 37
    • 0037067736 scopus 로고    scopus 로고
    • Mirk protein kinase is activated by MKK3 and functions as a transcriptional activator of HNF1α
    • Lim, S., Jin, K. and Friedman, E. (2002) Mirk protein kinase is activated by MKK3 and functions as a transcriptional activator of HNF1α. J. Biol. Chem. 277, 25040-25046
    • (2002) J. Biol. Chem. , vol.277 , pp. 25040-25046
    • Lim, S.1    Jin, K.2    Friedman, E.3


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