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Volumn 289, Issue 8, 2014, Pages 4723-4734

Characterization of the raptor/4E-BP1 interaction by chemical cross-linking coupled with mass spectrometry analysis

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL CROSS-LINKING; INTRAMOLECULAR CROSS-LINKS; MASS SPECTROMETRY ANALYSIS; N-TERMINALS; PROTEIN-PROTEIN INTERACTIONS;

EID: 84896706986     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.482067     Document Type: Article
Times cited : (17)

References (50)
  • 1
    • 70350418625 scopus 로고    scopus 로고
    • MTORsignaling at a glance
    • Laplante, M., and Sabatini, D. M. (2009)mTORsignaling at a glance. J. Cell Sci. 122, 3589-3594
    • (2009) J. Cell Sci. , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 2
    • 63749105226 scopus 로고    scopus 로고
    • MTOR and the control of whole body metabolism
    • Polak, P., and Hall, M. N. (2009) mTOR and the control of whole body metabolism. Curr. Opin. Cell Biol. 21, 209-218
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 209-218
    • Polak, P.1    Hall, M.N.2
  • 3
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger, S., Loewith, R., and Hall, M. N. (2006) TOR signaling in growth and metabolism. Cell 124, 471-484
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 6
    • 33845309430 scopus 로고    scopus 로고
    • Activation of the mTOR signaling pathway in renal clear cell carcinoma
    • Robb, V. A., Karbowniczek, M., Klein-Szanto, A. J., and Henske, E. P. (2007) Activation of the mTOR signaling pathway in renal clear cell carcinoma. J. Urol. 177, 346-352
    • (2007) J. Urol. , vol.177 , pp. 346-352
    • Robb, V.A.1    Karbowniczek, M.2    Klein-Szanto, A.J.3    Henske, E.P.4
  • 8
    • 77952243626 scopus 로고    scopus 로고
    • Single amino-acid changes that confer constitutive activation of mTOR are discovered in human cancer
    • Sato, T., Nakashima, A., Guo, L., Coffman, K., and Tamanoi, F. (2010) Single amino-acid changes that confer constitutive activation of mTOR are discovered in human cancer. Oncogene 29, 2746-2752
    • (2010) Oncogene , vol.29 , pp. 2746-2752
    • Sato, T.1    Nakashima, A.2    Guo, L.3    Coffman, K.4    Tamanoi, F.5
  • 9
    • 3242882820 scopus 로고    scopus 로고
    • PI 3-kinase related kinases. "Big" players in stressinduced signaling pathways
    • Abraham, R. T. (2004) PI 3-kinase related kinases. "Big" players in stressinduced signaling pathways. DNA Repair 3, 883-887
    • (2004) DNA Repair , vol.3 , pp. 883-887
    • Abraham, R.T.1
  • 10
    • 7944235758 scopus 로고    scopus 로고
    • Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive
    • Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Rüegg, M. A., Hall, A., and Hall, M. N. (2004) Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. 6, 1122-1128
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1122-1128
    • Jacinto, E.1    Loewith, R.2    Schmidt, A.3    Lin, S.4    Rüegg, M.A.5    Hall, A.6    Hall, M.N.7
  • 11
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and Raptorindependent pathway that regulates the cytoskeleton
    • Sarbassov, D. D., Ali, S. M., Kim, D. H., Guertin, D. A., Latek, R. R., Erdjument-Bromage, H., Tempst, P., and Sabatini, D. M. (2004) Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and Raptorindependent pathway that regulates the cytoskeleton. Curr. Biol. 14, 1296-1302
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 13
    • 77954296394 scopus 로고    scopus 로고
    • 4E-BP1 is a key effector of the oncogenic activation of the AKT and ERK signaling pathways that integrates their function in tumors
    • She, Q. B., Halilovic, E., Ye, Q., Zhen, W., Shirasawa, S., Sasazuki, T., Solit, D. B., and Rosen, N. (2010) 4E-BP1 is a key effector of the oncogenic activation of the AKT and ERK signaling pathways that integrates their function in tumors. Cancer Cell 18, 39-51
    • (2010) Cancer Cell , vol.18 , pp. 39-51
    • She, Q.B.1    Halilovic, E.2    Ye, Q.3    Zhen, W.4    Shirasawa, S.5    Sasazuki, T.6    Solit, D.B.7    Rosen, N.8
  • 14
    • 77649286736 scopus 로고    scopus 로고
    • Genetic dissection of the oncogenic mTOR pathway reveals druggable addiction to translational control via 4EBP1-eIF4E
    • Hsieh, A. C., Costa, M., Zollo, O., Davis, C., Feldman, M. E., Testa, J. R., Meyuhas, O., Shokat, K. M., and Ruggero, D. (2010) Genetic dissection of the oncogenic mTOR pathway reveals druggable addiction to translational control via 4EBP1-eIF4E. Cancer Cell 17, 249-261
    • (2010) Cancer Cell , vol.17 , pp. 249-261
    • Hsieh, A.C.1    Costa, M.2    Zollo, O.3    Davis, C.4    Feldman, M.E.5    Testa, J.R.6    Meyuhas, O.7    Shokat, K.M.8    Ruggero, D.9
  • 15
    • 0037178786 scopus 로고    scopus 로고
    • MTOR interacts with Raptor to form a nutrient-sensitive complex that signals to the cell growth machinery
    • Kim, D. H., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument-Bromage, H., Tempst, P., and Sabatini, D. M. (2002) mTOR interacts with Raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110, 163-175
    • (2002) Cell , vol.110 , pp. 163-175
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    King, J.E.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 17
    • 0037718389 scopus 로고    scopus 로고
    • TOS motif-mediated Raptor binding regulates 4E-BP1 multisite phosphorylation and function
    • Schalm, S. S., Fingar, D. C., Sabatini, D. M., and Blenis, J. (2003) TOS motif-mediated Raptor binding regulates 4E-BP1 multisite phosphorylation and function. Curr. Biol. 13, 797-806
    • (2003) Curr. Biol. , vol.13 , pp. 797-806
    • Schalm, S.S.1    Fingar, D.C.2    Sabatini, D.M.3    Blenis, J.4
  • 18
    • 33745263990 scopus 로고    scopus 로고
    • Different roles for the TOS and RAIP motifs of the translational regulator protein 4E-BP1 in the association with Raptor and phosphorylation by mTOR in the regulation of cell size
    • Eguchi, S., Tokunaga, C., Hidayat, S., Oshiro, N., Yoshino, K., Kikkawa, U., and Yonezawa, K. (2006) Different roles for the TOS and RAIP motifs of the translational regulator protein 4E-BP1 in the association with Raptor and phosphorylation by mTOR in the regulation of cell size. Genes Cells 11, 757-766
    • (2006) Genes Cells , vol.11 , pp. 757-766
    • Eguchi, S.1    Tokunaga, C.2    Hidayat, S.3    Oshiro, N.4    Yoshino, K.5    Kikkawa, U.6    Yonezawa, K.7
  • 19
    • 42449136578 scopus 로고    scopus 로고
    • Analysis of the regulatory motifs in eukaryotic initiation factor 4E binding protein 1
    • Lee, V. H., Healy, T., Fonseca, B. D., Hayashi, A., and Proud, C. G. (2008) Analysis of the regulatory motifs in eukaryotic initiation factor 4E binding protein 1. FEBS J. 275, 2185-2199
    • (2008) FEBS J. , vol.275 , pp. 2185-2199
    • Lee, V.H.1    Healy, T.2    Fonseca, B.D.3    Hayashi, A.4    Proud, C.G.5
  • 20
    • 84866062228 scopus 로고    scopus 로고
    • Evaluating protein interactions through cross-linking mass spectrometry
    • Tabb, D. L. (2012) Evaluating protein interactions through cross-linking mass spectrometry. Nat. Methods 9, 879-881
    • (2012) Nat. Methods , vol.9 , pp. 879-881
    • Tabb, D.L.1
  • 22
    • 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
    • 77950415030 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry as a low-resolution protein structure determination technique
    • Singh, P., Panchaud, A., and Goodlett, D. R. (2010) Chemical cross-linking and mass spectrometry as a low-resolution protein structure determination technique. Anal. Chem. 82, 2636-2642
    • (2010) Anal. Chem. , vol.82 , pp. 2636-2642
    • Singh, P.1    Panchaud, A.2    Goodlett, D.R.3
  • 27
    • 67649823420 scopus 로고    scopus 로고
    • Specific activation of mTORC1 by Rheb G-protein in vitro involves enhanced recruitment of its substrate protein
    • Sato, T., Nakashima, A., Guo, L., and Tamanoi, F. (2009) Specific activation of mTORC1 by Rheb G-protein in vitro involves enhanced recruitment of its substrate protein. J. Biol. Chem. 284, 12783-12791
    • (2009) J. Biol. Chem. , vol.284 , pp. 12783-12791
    • Sato, T.1    Nakashima, A.2    Guo, L.3    Tamanoi, F.4
  • 28
    • 0034690931 scopus 로고    scopus 로고
    • Use of mass spectrometry to study signaling pathways
    • Pandey, A., Andersen, J. S., and Mann, M. (2000) Use of mass spectrometry to study signaling pathways. Sci. STKE 2000, PL1
    • (2000) Sci. STKE , vol.2000
    • Pandey, A.1    Andersen, J.S.2    Mann, M.3
  • 29
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER. A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER. A unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 31
    • 84870371264 scopus 로고    scopus 로고
    • Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures
    • Bermejo, G. A., Clore, G. M., and Schwieters, C. D. (2012) Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures. Protein Sci. 21, 1824-1836
    • (2012) Protein Sci. , vol.21 , pp. 1824-1836
    • Bermejo, G.A.1    Clore, G.M.2    Schwieters, C.D.3
  • 32
    • 33749172207 scopus 로고    scopus 로고
    • A simple and reliable approach to docking protein-protein complexes from very sparse NOE-derived intermolecular distance restraints
    • Tang, C., and Clore, G. M. (2006) A simple and reliable approach to docking protein-protein complexes from very sparse NOE-derived intermolecular distance restraints. J. Biomol. NMR 36, 37-44
    • (2006) J. Biomol. NMR , vol.36 , pp. 37-44
    • Tang, C.1    Clore, G.M.2
  • 33
    • 34248513078 scopus 로고    scopus 로고
    • ZRANK. Reranking protein docking predictions with an optimized energy function
    • Pierce, B., and Weng, Z. (2007) ZRANK. Reranking protein docking predictions with an optimized energy function. Proteins 67, 1078-1086
    • (2007) Proteins , vol.67 , pp. 1078-1086
    • Pierce, B.1    Weng, Z.2
  • 36
    • 77953091045 scopus 로고    scopus 로고
    • Structure of the human mTOR complex i and its implications for rapamycin inhibition
    • Yip, C. K., Murata, K., Walz, T., Sabatini, D. M., and Kang, S. A. (2010) Structure of the human mTOR complex I and its implications for rapamycin inhibition. Mol. Cell 38, 768-774
    • (2010) Mol. Cell , vol.38 , pp. 768-774
    • Yip, C.K.1    Murata, K.2    Walz, T.3    Sabatini, D.M.4    Kang, S.A.5
  • 37
    • 27844576586 scopus 로고    scopus 로고
    • Structural basis for mRNA cap-binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, x-ray crystal structural, and molecular dynamics simulation methods
    • Tomoo, K., Matsushita, Y., Fujisaki, H., Abiko, F., Shen, X., Taniguchi, T., Miyagawa, H., Kitamura, K., Miura, K., and Ishida, T. (2005) Structural basis for mRNA cap-binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, x-ray crystal structural, and molecular dynamics simulation methods. Biochim. Biophys. Acta 1753, 191-208
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 191-208
    • Tomoo, K.1    Matsushita, Y.2    Fujisaki, H.3    Abiko, F.4    Shen, X.5    Taniguchi, T.6    Miyagawa, H.7    Kitamura, K.8    Miura, K.9    Ishida, T.10
  • 38
    • 34047174539 scopus 로고    scopus 로고
    • Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms
    • Rosettani, P., Knapp, S., Vismara, M. G., Rusconi, L., and Cameron, A. D. (2007) Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms. J. Mol. Biol. 368, 691-705
    • (2007) J. Mol. Biol. , vol.368 , pp. 691-705
    • Rosettani, P.1    Knapp, S.2    Vismara, M.G.3    Rusconi, L.4    Cameron, A.D.5
  • 39
    • 34547788872 scopus 로고    scopus 로고
    • Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives
    • Brown, C. J., McNae, I., Fischer, P. M., and Walkinshaw, M. D. (2007) Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives. J. Mol. Biol. 372, 7-15
    • (2007) J. Mol. Biol. , vol.372 , pp. 7-15
    • Brown, C.J.1    McNae, I.2    Fischer, P.M.3    Walkinshaw, M.D.4
  • 44
    • 0032577691 scopus 로고    scopus 로고
    • 4E-BP3, a new member of the eukaryotic initiation factor 4E-binding protein family
    • Poulin, F., Gingras, A. C., Olsen, H., Chevalier, S., and Sonenberg, N. (1998) 4E-BP3, a new member of the eukaryotic initiation factor 4E-binding protein family. J. Biol. Chem. 273, 14002-14007
    • (1998) J. Biol. Chem. , vol.273 , pp. 14002-14007
    • Poulin, F.1    Gingras, A.C.2    Olsen, H.3    Chevalier, S.4    Sonenberg, N.5
  • 47
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5 cap
    • Lazaris-Karatzas, A., Montine, K. S., and Sonenberg, N. (1990) Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5 cap. Nature 345, 544-547
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 48
    • 0037363075 scopus 로고    scopus 로고
    • Does the ribosome translate cancer?
    • Ruggero, D., and Pandolfi, P. P. (2003) Does the ribosome translate cancer? Nat. Rev. Cancer 3, 179-192
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 179-192
    • Ruggero, D.1    Pandolfi, P.P.2
  • 49
    • 0030443685 scopus 로고    scopus 로고
    • The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth
    • Rousseau, D., Gingras, A. C., Pause, A., and Sonenberg, N. (1996) The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene 13, 2415-2420
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.C.2    Pause, A.3    Sonenberg, N.4


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