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Volumn 5, Issue 6, 2006, Pages 1045-1053

Interdomain conformational changes in Akt activation revealed by chemical cross-linking and tandem mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE B;

EID: 33745610132     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M600026-MCP200     Document Type: Article
Times cited : (46)

References (34)
  • 1
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signalling: A hard Akt to follow
    • Brazil, D. P., and Hemmings, B. A. (2001) Ten years of protein kinase B signalling: A hard Akt to follow. Trends Biochem. Sci. 26, 657-664
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 2
    • 0034845958 scopus 로고    scopus 로고
    • PKB/Akt: A key mediator of cell proliferation, survival and insulin responses?
    • Lawlor, M. A., and Alessi, D. R. (2001) PKB/Akt: A key mediator of cell proliferation, survival and insulin responses? J. Cell Sci. 114, 2903-2910
    • (2001) J. Cell Sci. , vol.114 , pp. 2903-2910
    • Lawlor, M.A.1    Alessi, D.R.2
  • 3
    • 0001582482 scopus 로고
    • Molecular cloning of the Akt oncogene and its human homologues Akt1 and Akt2: Amplification of Akt1 in a primary human gastric adenocarcinoma
    • Staal, S. P. (1987) Molecular cloning of the Akt oncogene and its human homologues Akt1 and Akt2: Amplification of Akt1 in a primary human gastric adenocarcinoma. Proc. Natl. Acad. Sci. U. S. A. 84, 5034-5037
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 5034-5037
    • Staal, S.P.1
  • 4
    • 0026095665 scopus 로고
    • A retroviral oncogene, Akt, encoding a serine-threonine kinase containing an SH2-like region
    • Bellacosa, A., Testa, J. R., Staal, S. P., and Tsichlis, P. N. (1991) A retroviral oncogene, Akt, encoding a serine-threonine kinase containing an SH2-like region. Science 254, 274-277
    • (1991) Science , vol.254 , pp. 274-277
    • Bellacosa, A.1    Testa, J.R.2    Staal, S.P.3    Tsichlis, P.N.4
  • 5
    • 0031913246 scopus 로고    scopus 로고
    • Mechanism of activation and function of protein kinase B
    • Alessi, D. R., and Cohen, P. (1998) Mechanism of activation and function of protein kinase B. Curr. Opin. Genet. Dev. 8, 55-62
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 55-62
    • Alessi, D.R.1    Cohen, P.2
  • 6
    • 0037162293 scopus 로고    scopus 로고
    • High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol (3,4,5)-trisphosphate
    • Thomas, C., C., Deak, M., Alessi, D. R., and van Aalten, D. M. F. (2002) High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol (3,4,5)-trisphosphate. Curr. Biol. 12, 1256-1262
    • (2002) Curr. Biol. , vol.12 , pp. 1256-1262
    • Thomas, C.C.1    Deak, M.2    Alessi, D.R.3    van Aalten, D.M.F.4
  • 10
    • 0033594403 scopus 로고    scopus 로고
    • Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction
    • Watton, S. J., and Downward, J. (1999) Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction. Curr. Biol. 9, 433-436
    • (1999) Curr. Biol. , vol.9 , pp. 433-436
    • Watton, S.J.1    Downward, J.2
  • 11
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • Yang, J., Cron, P., Thompson, V., Good, V. M., Hess, D., Hemmings, B. A., and Barford, D. (2002) Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol. Cell 9, 1227-1240
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 12
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta, S. R., Brunet, A., and Greenberg, M. E. (1999) Cellular survival: a play in three Akts. Genes Dev. 13, 2905-2927
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 13
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R., Dudek, H., Tao, X. Masters, S. Fu, Haian, Gotoh, Y., and Greenberg, M. E. (1997) Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.Fu.4    Haian Gotoh, Y.5    Greenberg, M.E.6
  • 14
    • 0242468741 scopus 로고    scopus 로고
    • Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change
    • Milburn, C. C., Deak, M., Kelly, S. M., Price, S. M., Alessi, D. R., and van Aalten, D. M. F. (2003) Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. Biochem. J. 375, 531-538
    • (2003) Biochem. J. , vol.375 , pp. 531-538
    • Milburn, C.C.1    Deak, M.2    Kelly, S.M.3    Price, S.M.4    Alessi, D.R.5    van Aalten, D.M.F.6
  • 16
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • Yang, J., Cron, P., Good, V. M., Thompson, V., Hemmings, B. A., and Barford, D. (2002) Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat. Struct. Biol. 12, 940-944
    • (2002) Nat. Struct. Biol. , vol.12 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 17
    • 1242263882 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt): Interaction with inositol phosphates
    • Auguin, D., Barthe, P., Auge-Senegas, M., Stern, M., Noguchi, M., and Roumestand, C. (2004) Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt): interaction with inositol phosphates. J. Biomol. NMR 28, 137-155
    • (2004) J. Biomol. NMR , vol.28 , pp. 137-155
    • Auguin, D.1    Barthe, P.2    Auge-Senegas, M.3    Stern, M.4    Noguchi, M.5    Roumestand, C.6
  • 18
    • 0038630916 scopus 로고    scopus 로고
    • Monitoring conformational changes of proteins in cells by fluorescence lifetime imaging microscopy
    • Calleja, V., Ameer-beg, S. M., Vojnovic, B., Woscholski, R., Downward, J., and Larijani, B. (2003) Monitoring conformational changes of proteins in cells by fluorescence lifetime imaging microscopy. Biochem. J. 372, 33-40
    • (2003) Biochem. J. , vol.372 , pp. 33-40
    • Calleja, V.1    Ameer-beg, S.M.2    Vojnovic, B.3    Woscholski, R.4    Downward, J.5    Larijani, B.6
  • 19
    • 0034705128 scopus 로고    scopus 로고
    • High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
    • Young, M. M., Tang, N., Hempel, J. C., Oshiro, C. M., Taylor, E. W., Kuntz, I. D., Gilson, B. W., and Dollinger, G. (2000) High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 97, 5802-5806
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5802-5806
    • Young, M.M.1    Tang, N.2    Hempel, J.C.3    Oshiro, C.M.4    Taylor, E.W.5    Kuntz, I.D.6    Gilson, B.W.7    Dollinger, G.8
  • 20
    • 2242437182 scopus 로고    scopus 로고
    • Characterization of an antagonist interleukin-6 dimer by stable isotope labeling, cross-linking, and mass spectrometry
    • Taverner, T., Hall, N. E., Ohair, R. A. J., and Simpson, R. J. (2002) Characterization of an antagonist interleukin-6 dimer by stable isotope labeling, cross-linking, and mass spectrometry. J. Biol. Chem. 277, 46487-46492
    • (2002) J. Biol. Chem. , vol.277 , pp. 46487-46492
    • Taverner, T.1    Hall, N.E.2    Ohair, R.A.J.3    Simpson, R.J.4
  • 21
    • 0042349690 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for protein structural modeling
    • Back, J. W., de Jong, L., Muijsers, A. O., and Koster, C. G. (2003) Chemical cross-linking and mass spectrometry for protein structural modeling. J. Mol. Biol. 331, 303-313
    • (2003) J. Mol. Biol. , vol.331 , pp. 303-313
    • Back, J.W.1    de Jong, L.2    Muijsers, A.O.3    Koster, C.G.4
  • 22
    • 18844423484 scopus 로고    scopus 로고
    • Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry
    • Huang, B. X., Dass, C., and Kim, H.-Y. (2005) Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry. Biochem. J. 387, 695-702
    • (2005) Biochem. J. , vol.387 , pp. 695-702
    • Huang, B.X.1    Dass, C.2    Kim, H.-Y.3
  • 23
    • 14344258702 scopus 로고    scopus 로고
    • A three-dimensional molecular model of lipid-free apolipoprotein A-1 determined by cross-linking/mass spectrometry and sequence threading
    • Silva, R. A. G., Hilliard, G. M., Fang, J., Macha, S., and Davidson, W. S. (2005) A three-dimensional molecular model of lipid-free apolipoprotein A-1 determined by cross-linking/mass spectrometry and sequence threading. Biochemistry 44, 2759-2769
    • (2005) Biochemistry , vol.44 , pp. 2759-2769
    • Silva, R.A.G.1    Hilliard, G.M.2    Fang, J.3    Macha, S.4    Davidson, W.S.5
  • 24
    • 0033837787 scopus 로고    scopus 로고
    • Chemical cross-linking with thiol-cleavable reagents combined with differential mass spectrometric peptide mapping - A novel approach to assess intermolecular protein contacts
    • Bennett, K. L., Kussmann, M., Bjork, P., Godzwon, M., Mikkelsen, M., Sorensen, P., and Roepstorff, P. (2000) Chemical cross-linking with thiol-cleavable reagents combined with differential mass spectrometric peptide mapping - a novel approach to assess intermolecular protein contacts. Protein Sci. 9, 1503-1518
    • (2000) Protein Sci. , vol.9 , pp. 1503-1518
    • Bennett, K.L.1    Kussmann, M.2    Bjork, P.3    Godzwon, M.4    Mikkelsen, M.5    Sorensen, P.6    Roepstorff, P.7
  • 25
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz, A. (2003) Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J. Mass Spectrom. 38, 1225-1237
    • (2003) J. Mass Spectrom. , vol.38 , pp. 1225-1237
    • Sinz, A.1
  • 26
    • 2442500478 scopus 로고    scopus 로고
    • Cross-linking phosphatidylinositol-specific phospholipase C traps two activating phosphatidylcholine molecules on the enzyme
    • Zhang, X., Wehbi, H., and Roberts, M. F. (2004) Cross-linking phosphatidylinositol-specific phospholipase C traps two activating phosphatidylcholine molecules on the enzyme. J. Biol. Chem. 279, 20490-20500
    • (2004) J. Biol. Chem. , vol.279 , pp. 20490-20500
    • Zhang, X.1    Wehbi, H.2    Roberts, M.F.3
  • 28
    • 9344221072 scopus 로고    scopus 로고
    • Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry
    • Chu, F., Shan, S., Moustakas, D. T., Alber, F., Egea, P. F., Stroud, R. M., Walter, P., and Burlingame, A. L. (2004) Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 101, 16454-16459
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16454-16459
    • Chu, F.1    Shan, S.2    Moustakas, D.T.3    Alber, F.4    Egea, P.F.5    Stroud, R.M.6    Walter, P.7    Burlingame, A.L.8
  • 29
    • 3242772209 scopus 로고    scopus 로고
    • Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry
    • Huang, B. X., Dass, C., and Kim, H.-Y. (2004) Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry. J. Am. Soc. Mass Spectrom. 15, 1237-1247
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1237-1247
    • Huang, B.X.1    Dass, C.2    Kim, H.-Y.3
  • 30
  • 32
    • 0942279701 scopus 로고    scopus 로고
    • Substrate preference in phosphatidylserine biosynthesis for docosahexaenoic acid containing species
    • Kim, H.-Y, Bigelow, J., and Kevala, J. H. (2004) Substrate preference in phosphatidylserine biosynthesis for docosahexaenoic acid containing species. Biochemistry 43, 1030-1036
    • (2004) Biochemistry , vol.43 , pp. 1030-1036
    • Kim, H.-Y.1    Bigelow, J.2    Kevala, J.H.3
  • 33
    • 0031127305 scopus 로고    scopus 로고
    • Characterization ofa3-phosphoinositide-dependent protein kinase which phosphorylates protein kinase Bα
    • Alessi, D. R., James, S. R., Downes, C. P., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., and Cohen, P. (1997) Characterization ofa3-phosphoinositide-dependent protein kinase which phosphorylates protein kinase Bα. Curr. Biol. 7, 261-269
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.J.5    Reese, C.B.6    Cohen, P.7
  • 34
    • 0041846956 scopus 로고    scopus 로고
    • MS2assign, automated assignment and nomenclature of tandem mass spectrometry of chemically cross-linked peptides
    • Schilling, B., Row, R. H., Gilbon, B. W., Guo, X., and Yong, M. M. (2003) MS2assign, automated assignment and nomenclature of tandem mass spectrometry of chemically cross-linked peptides. J. Am. Soc. Mass Spectrom. 14, 834-850
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 834-850
    • Schilling, B.1    Row, R.H.2    Gilbon, B.W.3    Guo, X.4    Yong, M.M.5


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