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Volumn 384, Issue 3, 2004, Pages 477-488

Exploitation of KESTREL to identify NDRG family members as physiological substrates for SGK1 and GSK3

Author keywords

Glycogen synthase kinase 3 (GSK3); N myc down stream regulated gene (NDRG); p53; Phosphorylation; Serum and glucocorticoid induced kinase 1 (SGK1)

Indexed keywords

CELLS; ELECTROPHORESIS; GENES; LIVING SYSTEMS STUDIES; MUSCLE; SUBSTRATES;

EID: 19944408613     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041057     Document Type: Article
Times cited : (288)

References (52)
  • 1
    • 0035856598 scopus 로고    scopus 로고
    • Regulation and physiological roles of serum- and glucocorticoid-induced protein kinase isoforms
    • Lang, F. and Cohen, P. (2001) Regulation and physiological roles of serum- and glucocorticoid-induced protein kinase isoforms. Science STKE 2001 (108), RE17
    • (2001) Science STKE , Issue.108
    • Lang, F.1    Cohen, P.2
  • 2
    • 0037234487 scopus 로고    scopus 로고
    • Stimulus-dependent regulation of serum and glucocorticoid-induced protein kinase (SGK) transcription, sub-cellular location and enzymatic activity
    • Firestone, G. L., Giampaolo, J. R. and O'Keeffe, B. A. (2003) Stimulus-dependent regulation of serum and glucocorticoid-induced protein kinase (SGK) transcription, sub-cellular location and enzymatic activity. Cell. Physiol. Biochem. 13, 1-12
    • (2003) Cell. Physiol. Biochem. , vol.13 , pp. 1-12
    • Firestone, G.L.1    Giampaolo, J.R.2    O'Keeffe, B.A.3
  • 3
    • 0042967831 scopus 로고    scopus 로고
    • In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation
    • Collins, B. J., Deak, M., Arthur, J. S. C., Armit, L. J. and Alessi, D. R. (2003) In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation. EMBO J. 22, 4202-4211
    • (2003) EMBO J. , vol.22 , pp. 4202-4211
    • Collins, B.J.1    Deak, M.2    Arthur, J.S.C.3    Armit, L.J.4    Alessi, D.R.5
  • 4
    • 0030590875 scopus 로고    scopus 로고
    • Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP-K1 and p70 S6 kinase
    • Alessi, D. R., Caudwell, F. B., Andjelkovic, M., Hemmings, B. A. and Cohen, P. (1996) Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP-K1 and p70 S6 kinase. FEBS Lett. 399, 333-338
    • (1996) FEBS Lett. , vol.399 , pp. 333-338
    • Alessi, D.R.1    Caudwell, F.B.2    Andjelkovic, M.3    Hemmings, B.A.4    Cohen, P.5
  • 5
    • 0033560707 scopus 로고    scopus 로고
    • Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2
    • Kobayashi, T. and Cohen, P. (1999) Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2. Biochem. J. 339, 319-328
    • (1999) Biochem. J. , vol.339 , pp. 319-328
    • Kobayashi, T.1    Cohen, P.2
  • 6
    • 0033151832 scopus 로고    scopus 로고
    • Serum and glucocorticoid-inducible kinase (SGK) is atarget of the P1 3-kinase-stimulated signaling pathway
    • Park, J., Leong, M. L., Buse, P., Maiyar, A. C., Firestone, G. L. and Hemmings, B. A. (1999) Serum and glucocorticoid-inducible kinase (SGK) is atarget of the P1 3-kinase-stimulated signaling pathway. EMBO J. 18, 3024-3033
    • (1999) EMBO J. , vol.18 , pp. 3024-3033
    • Park, J.1    Leong, M.L.2    Buse, P.3    Maiyar, A.C.4    Firestone, G.L.5    Hemmings, B.A.6
  • 7
    • 0035135841 scopus 로고    scopus 로고
    • Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (F0X03a)
    • Brunet, A., Park, J., Tran, H., Hu, L. S., Hemmings, B. A. and Greenberg, M. E. (2001) Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (F0X03a). Mol. Cell. Biol. 21, 952-965
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 952-965
    • Brunet, A.1    Park, J.2    Tran, H.3    Hu, L.S.4    Hemmings, B.A.5    Greenberg, M.E.6
  • 8
    • 1542781732 scopus 로고    scopus 로고
    • Isoform-specific regulation of insulin-dependent glucose uptake by Akt/protein kinase B
    • Bae, S. S., Cho, H., Mu, J. and Birnbaum, M. J. (2003) Isoform-specific regulation of insulin-dependent glucose uptake by Akt/protein kinase B. J. Biol. Chem. 278, 49530-49536
    • (2003) J. Biol. Chem. , vol.278 , pp. 49530-49536
    • Bae, S.S.1    Cho, H.2    Mu, J.3    Birnbaum, M.J.4
  • 10
    • 0037236662 scopus 로고    scopus 로고
    • Regulation of ion channels by the serum and glucocorticoid-inducible kinase; implications for transport, excitability and cell proliferation
    • Lang, F., Henke, G., Embark, H. M., Waldegger, S., Palmada, M., Bohmer, C. and Vallon, V. (2003) Regulation of ion channels by the serum and glucocorticoid-inducible kinase; implications for transport, excitability and cell proliferation. Cell. Physiol. Biochem. 13, 41-50
    • (2003) Cell. Physiol. Biochem. , vol.13 , pp. 41-50
    • Lang, F.1    Henke, G.2    Embark, H.M.3    Waldegger, S.4    Palmada, M.5    Bohmer, C.6    Vallon, V.7
  • 13
    • 0033571416 scopus 로고    scopus 로고
    • Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced kinase
    • Kobayashi, T., Deak, M., Morrice, N. and Cohen, P. (1999) Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced kinase. Biochem. J. 344, 189-197
    • (1999) Biochem. J. , vol.344 , pp. 189-197
    • Kobayashi, T.1    Deak, M.2    Morrice, N.3    Cohen, P.4
  • 14
    • 0028875925 scopus 로고
    • Comparison of the specifcities of p70 S6 kinase and MAPKAP kinase-1 identifies a relatively specific substrate for p70 S6 kinase: The N-terminal kinase domain of MAPKAP-K1 is essential for peptide phosphorylation
    • Leighton, I. A., Dalby, K. N., Caudwell, F. B., Cohen, P. T. W. and Cohen, P. (1995) Comparison of the specifcities of p70 S6 kinase and MAPKAP kinase-1 identifies a relatively specific substrate for p70 S6 kinase: the N-terminal kinase domain of MAPKAP-K1 is essential for peptide phosphorylation. FEBS Lett. 375, 289-293
    • (1995) FEBS Lett. , vol.375 , pp. 289-293
    • Leighton, I.A.1    Dalby, K.N.2    Caudwell, F.B.3    Cohen, P.T.W.4    Cohen, P.5
  • 15
    • 0035881737 scopus 로고    scopus 로고
    • A novel method to identity protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38a
    • Knebel, A., Morrice, N. and Cohen, P. (2001) A novel method to identity protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38a. EMBO J. 20, 4360-4369
    • (2001) EMBO J. , vol.20 , pp. 4360-4369
    • Knebel, A.1    Morrice, N.2    Cohen, P.3
  • 16
    • 10944250433 scopus 로고    scopus 로고
    • Identification of filamin C as a new physiological substrate of PKBα using KESTREL
    • Murray, J. T., Campbell, D. G., Peggie, M., Alfonso, M. and Cohen, P. (2004) Identification of filamin C as a new physiological substrate of PKBα using KESTREL. Biochem. J. 384, 489-494
    • (2004) Biochem. J. , vol.384 , pp. 489-494
    • Murray, J.T.1    Campbell, D.G.2    Peggie, M.3    Alfonso, M.4    Cohen, P.5
  • 17
    • 0029782176 scopus 로고    scopus 로고
    • Purification and cloning of SAPKK3, the major activator of RK/p38 in stress and cytokine-stimulated monocytes and epithelial cells
    • Cuenda, A., Alonso, G., Morrice, N., Jones, M., Meier, R., Cohen, P. and Nebreda, A. R. (1996) Purification and cloning of SAPKK3, the major activator of RK/p38 in stress and cytokine-stimulated monocytes and epithelial cells. EMBO J. 15, 4156-4164
    • (1996) EMBO J. , vol.15 , pp. 4156-4164
    • Cuenda, A.1    Alonso, G.2    Morrice, N.3    Jones, M.4    Meier, R.5    Cohen, P.6    Nebreda, A.R.7
  • 18
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M. and Cohen, P. (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 19
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • Bain, J., McLauchlan, H., Elliott, M. and Cohen, P. (2003) The specificities of protein kinase inhibitors: an update. Biochem. J. 371, 199-204
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 20
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross, D. A., Alessi, D. R., Cohen, P., Andjelkovich, M. and Hemmings, B. A. (1995) Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature (London) 378, 785-789
    • (1995) Nature (London) , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 21
    • 10944227566 scopus 로고    scopus 로고
    • (2002) Inhibitors of glycogen synthase kinase 3. U.S. Pat. 6,417,185
    • Goff, D. A., Harrison, D. S., Nuss, J. M., Ring, D. B. and Zhou, X. A. (2002) Inhibitors of glycogen synthase kinase 3. U.S. Pat. 6,417,185
    • Goff, D.A.1    Harrison, D.S.2    Nuss, J.M.3    Ring, D.B.4    Zhou, X.A.5
  • 23
    • 0012059894 scopus 로고    scopus 로고
    • Identification of protein phosphorylation sites by a combination of mass spectrometry and solid phase Edman sequencing
    • Campbell, D. G. and Morrice, N. (2002) Identification of protein phosphorylation sites by a combination of mass spectrometry and solid phase Edman sequencing. J. Biomol. Techn. 13, 119-130
    • (2002) J. Biomol. Techn. , vol.13 , pp. 119-130
    • Campbell, D.G.1    Morrice, N.2
  • 25
    • 0035307347 scopus 로고    scopus 로고
    • Characterization of the human NDRG gene family: A newly identified member, NDRG4, is specifically expressed in brain and heart
    • Zhou, R. H., Kokame, K., Tsukamoto, Y., Yutani, C., Kato, H. and Miyata, T (2001) Characterization of the human NDRG gene family: a newly identified member, NDRG4, is specifically expressed in brain and heart. Genomics 73, 86-97
    • (2001) Genomics , vol.73 , pp. 86-97
    • Zhou, R.H.1    Kokame, K.2    Tsukamoto, Y.3    Yutani, C.4    Kato, H.5    Miyata, T.6
  • 26
    • 0036184953 scopus 로고    scopus 로고
    • Characterization and expression of three novel differentiation-related genes belonging to the human NDRG gene family
    • Qu, X., Zhai, Y., Wei, H., Zhang, C., Xing, G., Yu, Y. and He, F. (2002) Characterization and expression of three novel differentiation-related genes belonging to the human NDRG gene family. Mol. Cell. Biochem. 229, 35-44
    • (2002) Mol. Cell. Biochem. , vol.229 , pp. 35-44
    • Qu, X.1    Zhai, Y.2    Wei, H.3    Zhang, C.4    Xing, G.5    Yu, Y.6    He, F.7
  • 27
    • 0023656594 scopus 로고
    • Formation of protein kinase recognition sites by covalent modification of the substrate; molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase-3
    • Fiol, C. J., Mahrenholz, A. M., Wang, Y., Roeske, R. W. and Roach, P. J. (1987) Formation of protein kinase recognition sites by covalent modification of the substrate; molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase-3. J. Biol. Chem. 262, 14042-14048
    • (1987) J. Biol. Chem. , vol.262 , pp. 14042-14048
    • Fiol, C.J.1    Mahrenholz, A.M.2    Wang, Y.3    Roeske, R.W.4    Roach, P.J.5
  • 28
    • 0037339766 scopus 로고    scopus 로고
    • Selective glycogen synthase kinase 3 inhibitors potentiate insulin activation of glucose transport and utilization in vitro and in vivo
    • Ring, D. B., Johnson, K. W., Henricksen, E. J., Nuss, J. M., Goff, D., Kinnick, T. R., Ma, S. T., Reeder, J. W., Samuels, I., Slabiak, T et al. (2003) Selective glycogen synthase kinase 3 inhibitors potentiate insulin activation of glucose transport and utilization in vitro and in vivo. Diabetes 52, 588-595
    • (2003) Diabetes , vol.52 , pp. 588-595
    • Ring, D.B.1    Johnson, K.W.2    Henricksen, E.J.3    Nuss, J.M.4    Goff, D.5    Kinnick, T.R.6    Ma, S.T.7    Reeder, J.W.8    Samuels, I.9    Slabiak, T.10
  • 33
    • 0041524094 scopus 로고    scopus 로고
    • A reinvestigation of the multisite phosphorylation of the transcription factor c-Jun
    • Morton, S., Davis, R. J., McLaren, A. and Cohen, P. (2003) A reinvestigation of the multisite phosphorylation of the transcription factor c-Jun. EMBO J. 22, 3876-3886
    • (2003) EMBO J. , vol.22 , pp. 3876-3886
    • Morton, S.1    Davis, R.J.2    McLaren, A.3    Cohen, P.4
  • 34
    • 3042635178 scopus 로고    scopus 로고
    • GSK3 inhibitors: Development and potential for the treatment of disease
    • Cohen, P. and Goedert, M. (2004) GSK3 inhibitors: development and potential for the treatment of disease. Nat. Rev. Drug Discov. 3, 479-487
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 479-487
    • Cohen, P.1    Goedert, M.2
  • 35
    • 0034969088 scopus 로고    scopus 로고
    • A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation
    • Frame, S., Cohen, P. and Biondi, R. M. (2001) A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation. Mol. Cell 7, 1321-1327
    • (2001) Mol. Cell , vol.7 , pp. 1321-1327
    • Frame, S.1    Cohen, P.2    Biondi, R.M.3
  • 36
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase-3β: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • Dajani, R., Fraser, E., Roe, S. M., Young, N., Good, V., Dale, T. C. and Pearl, L. H. (2001) Crystal structure of glycogen synthase kinase-3β: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 105, 721-732
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Young, N.4    Good, V.5    Dale, T.C.6    Pearl, L.H.7
  • 37
    • 0029860742 scopus 로고    scopus 로고
    • Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis
    • Kokame, K., Kato, H. and Miyata, T. (1996) Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. J. Biol. Chem. 271, 29659-29665
    • (1996) J. Biol. Chem. , vol.271 , pp. 29659-29665
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 38
    • 0032877460 scopus 로고    scopus 로고
    • Nickel-induced transformation shifts the balance between HIF-1 and p53 transcription factors
    • Salnikow, K., An, W. G., Melillo, G., Blagosklonny, M. V. and Costa, M. (1999) Nickel-induced transformation shifts the balance between HIF-1 and p53 transcription factors. Carcinogenesis 20, 1819-1823
    • (1999) Carcinogenesis , vol.20 , pp. 1819-1823
    • Salnikow, K.1    An, W.G.2    Melillo, G.3    Blagosklonny, M.V.4    Costa, M.5
  • 40
    • 0032188908 scopus 로고    scopus 로고
    • Inhibition of tumour cell growth by RTP/rit42 and its responsiveness to p53 and DNA damage
    • Kurdistani, S. K., Arizti, P., Reimer, C. L., Sugrue, M. M., Aaronson, S. A. and Lee, S. W. (1998) Inhibition of tumour cell growth by RTP/rit42 and its responsiveness to p53 and DNA damage. Cancer Res. 58, 4439-4444
    • (1998) Cancer Res. , vol.58 , pp. 4439-4444
    • Kurdistani, S.K.1    Arizti, P.2    Reimer, C.L.3    Sugrue, M.M.4    Aaronson, S.A.5    Lee, S.W.6
  • 41
    • 0033057980 scopus 로고    scopus 로고
    • Differential expression of the RTP/Drg1/Ndr1 gene product in proliferating and growth-arrested cells
    • Piquemal, D., Joulia, D., Balaguer, P., Basset, A., Marti, J. and Commes, T. (1999) Differential expression of the RTP/Drg1/Ndr1 gene product in proliferating and growth-arrested cells. Biochim. Biophys. Acta 1450, 364-373
    • (1999) Biochim. Biophys. Acta , vol.1450 , pp. 364-373
    • Piquemal, D.1    Joulia, D.2    Balaguer, P.3    Basset, A.4    Marti, J.5    Commes, T.6
  • 42
    • 0033006387 scopus 로고    scopus 로고
    • N-myc-dependent repression of Ndr1, a gene identified by direct subtraction of whole mouse embryo cDNAs between wild type and N-Myc mutant
    • Shimono, A., Okuda, T. and Kondoh, H. (1999) N-myc-dependent repression of Ndr1, a gene identified by direct subtraction of whole mouse embryo cDNAs between wild type and N-Myc mutant. Mech. Dev. 83, 39-52
    • (1999) Mech. Dev. , vol.83 , pp. 39-52
    • Shimono, A.1    Okuda, T.2    Kondoh, H.3
  • 45
    • 0033972140 scopus 로고    scopus 로고
    • Drg-1 as a differentiation-related, putative metastatic suppressor gene in human colon cancer
    • Guan, R. J., Ford, H. L., Fu, Y., Li, Y., Shaw, L. M. and Pardee, A. B. (2000) Drg-1 as a differentiation-related, putative metastatic suppressor gene in human colon cancer. Cancer Res. 60, 749-755
    • (2000) Cancer Res. , vol.60 , pp. 749-755
    • Guan, R.J.1    Ford, H.L.2    Fu, Y.3    Li, Y.4    Shaw, L.M.5    Pardee, A.B.6
  • 50
    • 0036524611 scopus 로고    scopus 로고
    • Molecular cell biology of Charcot-Marie-Tooth disease
    • Berger, P., Young, P. and Suter, U. (2002) Molecular cell biology of Charcot-Marie-Tooth disease. Neurogenetics 4, 1-15
    • (2002) Neurogenetics , vol.4 , pp. 1-15
    • Berger, P.1    Young, P.2    Suter, U.3
  • 51
    • 1942422199 scopus 로고    scopus 로고
    • Ndrg1-deficient mice exhibit a progressive demyelinating disorder of the peripheral nerves
    • Okuda, T., Higashi, Y., Kokame, K., Tanaka, C., Kondoh, H. and Miyata, T. (2004) Ndrg1-deficient mice exhibit a progressive demyelinating disorder of the peripheral nerves. Mol. Cell. Biol. 24, 3949-3956
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3949-3956
    • Okuda, T.1    Higashi, Y.2    Kokame, K.3    Tanaka, C.4    Kondoh, H.5    Miyata, T.6


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