메뉴 건너뛰기




Volumn 444, Issue 3, 2012, Pages 503-514

The AMPK-related kinase SIK2 is regulated by cAMP via phosphorylation at Ser 358 in adipocytes

Author keywords

14 3 3; 3T3 l1 adipocyte; cAMP; Insulin; Phosphorylation; Salt induced kinase (SIK)

Indexed keywords

5 [2 [[2 (3 CHLOROPHENYL) 2 HYDROXYETHYL]AMINO]PROPYL] 1,3 BENZODIOXOLE 2,2 DICARBOXYLIC ACID; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; FORSKOLIN; HEMAGGLUTININ; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; SALT INDUCIBLE KINASE 2; SERINE; UNCLASSIFIED DRUG;

EID: 84862237698     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111932     Document Type: Article
Times cited : (55)

References (39)
  • 1
    • 63849210402 scopus 로고    scopus 로고
    • The regulation and function of mammalian AMPK-related kinases
    • Bright, N. J., Thornton, C. and Carling, D. (2009) The regulation and function of mammalian AMPK-related kinases. Acta Physiol. 196, 15-26
    • (2009) Acta Physiol. , vol.196 , pp. 15-26
    • Bright, N.J.1    Thornton, C.2    Carling, D.3
  • 2
    • 40149106453 scopus 로고    scopus 로고
    • SIK2 can be activated by deprivation of nutrition and it inhibits expression of lipogenic genes in adipocytes
    • DOI 10.1038/oby.2007.98, PII OBY200798
    • Du, J., Chen, Q., Takemori, H. and Xu, H. (2008) SIK2 can be activated by deprivation of nutrition and it inhibits expression of lipogenic genes in adipocytes. Obesity 16, 531-538 (Pubitemid 351328002)
    • (2008) Obesity , vol.16 , Issue.3 , pp. 531-538
    • Du, J.1    Chen, Q.2    Takemori, H.3    Xu, H.4
  • 4
    • 0034710814 scopus 로고    scopus 로고
    • The new serine-threonine kinase, Qik, is a target of the Qin oncogene
    • Xia, Y., Zhang, Z., Kruse, U., Vogt, P. K. and Li, J. (2000) The new serine-threonine kinase, Qik, is a target of the Qin oncogene. Biochem. Biophys. Res. Commun. 276, 564-570
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 564-570
    • Xia, Y.1    Zhang, Z.2    Kruse, U.3    Vogt, P.K.4    Li, J.5
  • 5
    • 0034527427 scopus 로고    scopus 로고
    • SIK (salt-inducible kinase): Regulation of ACTH-mediated steroidogenic gene expression and nuclear/cytosol re-distribution
    • Lin, X., Takemori, H., Doi, J., Katoh, Y. and Okamoto, M. (2000) SIK (salt-inducible kinase): regulation of ACTH-mediated steroidogenic gene expression and nuclear/cytosol redistribution. Endocr. Res. 26, 995-1002 (Pubitemid 32053132)
    • (2000) Endocrine Research , vol.26 , Issue.4 , pp. 995-1002
    • Lin, X.-Z.1    Takemori, H.2    Doi, J.3    Katoh, Y.4    Okamoto, M.5
  • 6
    • 0037013197 scopus 로고    scopus 로고
    • Salt-inducible kinase represses cAMP-dependent protein kinase-mediated activation of human cholesterol side chain cleavage cytochrome P450 promoter through the CREB basic leucine zipper domain
    • DOI 10.1074/jbc.M109365200
    • Doi, J., Takemori, H., Lin, X. Z., Horike, N., Katoh, Y. and Okamoto, M. (2002) Salt-inducible kinase represses cAMP-dependent protein kinase-mediated activation of human cholesterol side chain cleavage cytochrome P450 promoter through the CREB basic leucine zipper domain. J. Biol. Chem. 277, 15629-15637 (Pubitemid 34967834)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15629-15637
    • Doi, J.1    Takemori, H.2    Lin, X.-Z.3    Horike, N.4    Katoh, Y.5    Okamoto, M.6
  • 7
    • 0036829519 scopus 로고    scopus 로고
    • ACTH-induced nucleocytoplasmic translocation of salt-inducible kinase: Implication in the protein kinase A-activated gene transcription in mouse adrenocortical tumor cells
    • DOI 10.1074/jbc.M204602200
    • Takemori, H., Katoh, Y., Horike, N., Doi, J. and Okamoto, M. (2002) ACTH-induced nucleocytoplasmic translocation of salt-inducible kinase. Implication in the protein kinase A-activated gene transcription in mouse adrenocortical tumor cells. J. Biol. Chem. 277, 42334-42343 (Pubitemid 35257554)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 42334-42343
    • Takemori, H.1    Katoh, Y.2    Horike, N.3    Doi, J.4    Okamoto, M.5
  • 11
    • 34548831102 scopus 로고    scopus 로고
    • Insulin modulates gluconeogenesis by inhibition of the coactivator TORC2
    • DOI 10.1038/nature06128, PII NATURE06128
    • Dentin, R., Liu, Y., Koo, S. H., Hedrick, S., Vargas, T., Heredia, J., Yates, III, J. and Montminy, M. (2007) Insulin modulates gluconeogenesis by inhibition of the coactivator TORC2. Nature 449, 366-369 (Pubitemid 47443476)
    • (2007) Nature , vol.449 , Issue.7160 , pp. 366-369
    • Dentin, R.1    Liu, Y.2    Koo, S.-H.3    Hedrick, S.4    Vargas, T.5    Heredia, J.6    Yates III, J.7    Montminy, M.8
  • 13
    • 0036940765 scopus 로고    scopus 로고
    • Identification of the nuclear localization domain of salt-inducible kinase
    • DOI 10.1081/ERC-120016802
    • Katoh, Y., Takemori, H., Doi, J. and Okamoto, M. (2002) Identification of the nuclear localization domain of salt-inducible kinase. Endocr. Res. 28, 315-318 (Pubitemid 36042480)
    • (2002) Endocrine Research , vol.28 , Issue.4 , pp. 315-318
    • Katoh, Y.1    Takemori, H.2    Doi, J.3    Okamoto, M.4
  • 14
    • 8644226763 scopus 로고    scopus 로고
    • Salt-inducible kinase-1 represses cAMP response element-binding protein activity both in the nucleus and in the cytoplasm
    • DOI 10.1111/j.1432-1033.2004.04372.x
    • Katoh, Y., Takemori, H., Min, L., Muraoka, M., Doi, J., Horike, N. and Okamoto, M. (2004) Salt-inducible kinase-1 represses cAMP response element-binding protein activity both in the nucleus and in the cytoplasm. Eur. J. Biochem. 271, 4307-4319 (Pubitemid 39506760)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.21 , pp. 4307-4319
    • Katoh, Y.1    Takemori, H.2    Min, L.3    Muraoka, H.4    Doi, J.5    Horike, N.6    Okamoto, M.7
  • 17
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher, Y., Perret, S. and Kamen, A. (2002) High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 30, E9
    • (2002) Nucleic Acids Res. , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 18
    • 0028942747 scopus 로고
    • Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I
    • Dale, S., Wilson, W. A., Edelman, A. M. and Hardie, D. G. (1995) Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Lett. 361, 191-195
    • (1995) FEBS Lett. , vol.361 , pp. 191-195
    • Dale, S.1    Wilson, W.A.2    Edelman, A.M.3    Hardie, D.G.4
  • 22
    • 33644674733 scopus 로고    scopus 로고
    • Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer
    • DOI 10.1074/mcp.M500210-MCP200
    • Williamson, B. L., Marchese, J. and Morrice, N. A. (2006) Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer. Mol. Cell. Proteomics 5, 337-346 (Pubitemid 43329311)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.2 , pp. 337-346
    • Williamson, B.L.1    Marchese, J.2    Morrice, N.A.3
  • 23
    • 34548453703 scopus 로고    scopus 로고
    • Characterization of a protein kinase B inhibitor in vitro and in insulin-treated liver cells
    • DOI 10.2337/db07-0343
    • Logie, L., Ruiz-Alcaraz, A. J., Keane, M., Woods, Y. L., Bain, J., Marquez, R., Alessi, D. R. and Sutherland, C. (2007) Characterization of a protein kinase B inhibitor in vitro and in insulin-treated liver cells. Diabetes 56, 2218-2227 (Pubitemid 47358228)
    • (2007) Diabetes , vol.56 , Issue.9 , pp. 2218-2227
    • Logie, L.1    Ruiz-Alcaraz, A.J.2    Keane, M.3    Woods, Y.L.4    Bain, J.5    Marquez, R.6    Alessi, D.R.7    Sutherland, C.8
  • 24
    • 2342486073 scopus 로고    scopus 로고
    • Salt-inducible kinase (SIK) isoforms: Their involvement in steroidogenesis and adipogenesis
    • DOI 10.1016/j.mce.2003.10.016, PII S0303720703003873
    • Katoh, Y., Takemori, H., Horike, N., Doi, J., Muraoka, M., Min, L. and Okamoto, M. (2004) Salt-inducible kinase (SIK) isoforms: their involvement in steroidogenesis and adipogenesis. Mol. Cell. Endocrinol. 217, 109-112 (Pubitemid 38596635)
    • (2004) Molecular and Cellular Endocrinology , vol.217 , Issue.1-2 , pp. 109-112
    • Katoh, Y.1    Takemori, H.2    Horike, N.3    Doi, J.4    Muraoka, M.5    Min, L.6    Okamoto, M.7
  • 25
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh, C. (2004) Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem. J. 381, 329-342
    • (2004) Biochem. J. , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 26
    • 33750457625 scopus 로고    scopus 로고
    • Regulation of the polarity kinases PAR-1/MARK by 14-3-3 interaction and phosphorylation
    • DOI 10.1242/jcs.03097
    • Goransson, O., Deak, M., Wullschleger, S., Morrice, N. A., Prescott, A. R. and Alessi, D. R. (2006) Regulation of the polarity kinases PAR-1/MARK by 14-3-3 interaction and phosphorylation. J. Cell Sci. 119, 4059-4070 (Pubitemid 44650878)
    • (2006) Journal of Cell Science , vol.119 , Issue.19 , pp. 4059-4070
    • Goransson, O.1    Deak, M.2    Wullschleger, S.3    Morrice, N.A.4    Prescott, A.R.5    Alessi, D.R.6
  • 28
    • 0344081177 scopus 로고    scopus 로고
    • Minireview: The AMP-activated protein kinase cascade: The key sensor of cellular energy status
    • Hardie, D. G. (2003) Minireview: the AMP-activated protein kinase cascade: the key sensor of cellular energy status. Endocrinology 144, 5179-5183
    • (2003) Endocrinology , vol.144 , pp. 5179-5183
    • Hardie, D.G.1
  • 29
    • 34147152841 scopus 로고    scopus 로고
    • Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
    • DOI 10.1042/BJ20061520
    • Sanders, M. J., Grondin, P. O., Hegarty, B. D., Snowden, M. A. and Carling, D. (2007) Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade. Biochem. J. 403, 139-148 (Pubitemid 46569875)
    • (2007) Biochemical Journal , vol.403 , Issue.1 , pp. 139-148
    • Sanders, M.J.1    Grondin, P.O.2    Hegarty, B.D.3    Snowden, M.A.4    Carling, D.5
  • 33
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase
    • DOI 10.1016/j.cmet.2005.05.009, PII S155041310500166X
    • Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G. and Hardie, D. G. (2005) Calmodulin-dependent protein kinase kinase-β is an alternative upstream kinase for AMP-activated protein kinase. Cell Metab. 2, 9-19 (Pubitemid 43239821)
    • (2005) Cell Metabolism , vol.2 , Issue.1 , pp. 9-19
    • Hawley, S.A.1    Pan, D.A.2    Mustard, K.J.3    Ross, L.4    Bain, J.5    Edelman, A.M.6    Frenguelli, B.G.7    Hardie, D.G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.