메뉴 건너뛰기




Volumn 287, Issue 28, 2012, Pages 23407-23417

Raf kinase inhibitor protein (RKIP) dimer formation controls its target switch from Raf1 to G protein-coupled receptor kinase (GRK) 2

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR NETWORK; CO-IMMUNOPRECIPITATIONS; DIMER FORMATION; DIRECT INTERACTIONS; G PROTEIN-COUPLED RECEPTOR KINASE; KINASE INHIBITORS; PROTEIN-PROTEIN INTERACTIONS; PURIFIED PROTEIN; SIGNALING FUNCTIONS;

EID: 84863609981     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.363812     Document Type: Article
Times cited : (65)

References (53)
  • 4
    • 0346874333 scopus 로고    scopus 로고
    • Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2
    • DOI 10.1038/nature02158
    • Lorenz, K., Lohse, M. J., and Quitterer, U. (2003) Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2. Nature 426, 574-579 (Pubitemid 37522645)
    • (2003) Nature , vol.426 , Issue.6966 , pp. 574-579
    • Lorenz, K.1    Lohse, M.J.2    Quitterer, U.3
  • 5
    • 0035955736 scopus 로고    scopus 로고
    • Human phosphatidylethanolamine-binding protein facilitates heterotrimericGprotein-dependent signaling
    • Kroslak, T. (2001) Human phosphatidylethanolamine-binding protein facilitates heterotrimericGprotein-dependent signaling. J. Biol. Chem. 276, 39772-39778
    • (2001) J. Biol. Chem. , vol.276 , pp. 39772-39778
    • Kroslak, T.1
  • 7
    • 0035170831 scopus 로고    scopus 로고
    • Behaviour of bovine phosphatidylethanolamine-binding protein with model membranes: Evidence of affinity for negatively charged membranes
    • DOI 10.1046/j.0014-2956.2001.02528.x
    • Vallée, B. S., Tauc, P., Brochon, J. C., Maget-Dana, R., Lelièvre, D., Metz-Boutigue, M. H., Bureaud, N., and Schoentgen, F. (2001) Behavior of bovine phosphatidylethanolamine-binding protein with model membranes. Evidence of affinity for negatively charged membranes. Eur. J. Biochem. 268, 5831-5841 (Pubitemid 33079318)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.22 , pp. 5831-5841
    • Vallee, B.S.1    Tauc, P.2    Brochon, J.-C.3    Maget-Dana, R.4    Lelievre, D.5    Metz-Boutigue, M.-H.6    Bureaud, N.7    Schoentgen, F.8
  • 8
    • 0032532458 scopus 로고    scopus 로고
    • Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction
    • Banfield, M. J., Barker, J. J., Perry, A. C., and Brady, R. L. (1998) Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure 6, 1245-1254 (Pubitemid 28485957)
    • (1998) Structure , vol.6 , Issue.10 , pp. 1245-1254
    • Banfield, M.J.1    Barker, J.J.2    Perry, A.C.F.3    Brady, R.L.4
  • 9
    • 54349109317 scopus 로고    scopus 로고
    • Raf kinase inhibitory protein (RKIP). A physiological regulator and future therapeutic target
    • Zeng, L., Imamoto, A., and Rosner, M. R. (2008) Raf kinase inhibitory protein (RKIP). A physiological regulator and future therapeutic target. Expert Opin. Ther. Targets 12, 1275-1287
    • (2008) Expert Opin. Ther. Targets , vol.12 , pp. 1275-1287
    • Zeng, L.1    Imamoto, A.2    Rosner, M.R.3
  • 10
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • Kolch, W. (2005) Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat. Rev. Mol. Cell Biol. 6, 827-837
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 827-837
    • Kolch, W.1
  • 11
    • 4143071652 scopus 로고    scopus 로고
    • The role of Raf kinase inhibitor protein (RKIP) in health and disease
    • DOI 10.1016/j.bcp.2004.04.024, PII S0006295204003600
    • Keller, E. T., Fu, Z., and Brennan, M. (2004) The role of Raf kinase inhibitor protein (RKIP) in health and disease. Biochem. Pharmacol. 68, 1049-1053 (Pubitemid 39094269)
    • (2004) Biochemical Pharmacology , vol.68 , Issue.6 , pp. 1049-1053
    • Keller, E.T.1    Fu, Z.2    Brennan, M.3
  • 12
    • 41849102400 scopus 로고    scopus 로고
    • Raf kinase inhibitory protein: A signal transduction modulator and metastasis suppressor
    • DOI 10.1038/cr.2008.43, PII CR200843
    • Granovsky, A. E., and Rosner, M. R. (2008) Raf kinase inhibitory protein.A signal transduction modulator and metastasis suppressor. Cell Res. 18, 452-457 (Pubitemid 351498852)
    • (2008) Cell Research , vol.18 , Issue.4 , pp. 452-457
    • Granovsky, A.E.1    Rosner, M.R.2
  • 13
    • 0035854480 scopus 로고    scopus 로고
    • Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein
    • DOI 10.1006/jmbi.2001.4784
    • Serre, L., Pereira de Jesus, K., Zelwer, C., Bureaud, N., Schoentgen, F., and Bénédetti, H. (2001) Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein. J. Mol. Biol. 310, 617-634 (Pubitemid 32692574)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.3 , pp. 617-634
    • Serre, L.1    Pereira, D.J.K.2    Zelwer, C.3    Bureaud, N.4    Schoentgen, F.5    Benedetti, H.6
  • 15
    • 0032532743 scopus 로고    scopus 로고
    • Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: A novel structural class of phospholipid-binding proteins
    • Serre, L., Vallée, B., Bureaud, N., Schoentgen, F., and Zelwer, C. (1998) Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain. A novel structural class of phospholipid-binding proteins. Structure 6, 1255-1265 (Pubitemid 28485958)
    • (1998) Structure , vol.6 , Issue.10 , pp. 1255-1265
    • Serre, L.1    Vallee, B.2    Bureaud, N.3    Schoentgen, F.4    Zelwer, C.5
  • 16
    • 77956270130 scopus 로고    scopus 로고
    • Characterization of the Raf kinase inhibitory protein (RKIP) binding pocket. NMR-based screening identifies small-molecule ligands
    • Shemon, A. N., Heil, G. L., Granovsky, A. E., Clark, M. M., McElheny, D., Chimon, A., Rosner, M. R., and Koide, S. (2010) Characterization of the Raf kinase inhibitory protein (RKIP) binding pocket. NMR-based screening identifies small-molecule ligands. PLoS ONE 5, e10479
    • (2010) PLoS ONE , vol.5
    • Shemon, A.N.1    Heil, G.L.2    Granovsky, A.E.3    Clark, M.M.4    McElheny, D.5    Chimon, A.6    Rosner, M.R.7    Koide, S.8
  • 17
    • 39849107306 scopus 로고    scopus 로고
    • The RKIP (Raf-1 kinase inhibitor protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK
    • Rath, O., Park, S., Tang, H. H., Banfield, M. J., Brady, R. L., Lee, Y. C., Dignam, J. D., Sedivy, J. M., Kolch, W., and Yeung, K. C. (2008) The RKIP (Raf-1 kinase inhibitor protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK. Cell Signal 20, 935-941
    • (2008) Cell Signal , vol.20 , pp. 935-941
    • Rath, O.1    Park, S.2    Tang, H.H.3    Banfield, M.J.4    Brady, R.L.5    Lee, Y.C.6    Dignam, J.D.7    Sedivy, J.M.8    Kolch, W.9    Yeung, K.C.10
  • 18
    • 0034003003 scopus 로고    scopus 로고
    • Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the Raf kinase inhibitor protein
    • DOI 10.1128/MCB.20.9.3079-3085.2000
    • Yeung, K., Janosch, P., McFerran, B., Rose, D. W., Mischak, H., Sedivy, J. M., and Kolch, W. (2000) Mechanism of suppression of the Raf/MEK/ extracellular signal-regulated kinase pathway by the Raf kinase inhibitor protein. Mol. Cell. Biol. 20, 3079-3085 (Pubitemid 30215020)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.9 , pp. 3079-3085
    • Yeung, K.1    Janosch, P.2    McFerran, B.3    Rose, D.W.4    Mischak, H.5    Sedivy, J.M.6    Kolch, W.7
  • 19
    • 0034646560 scopus 로고    scopus 로고
    • The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator
    • Banfield, M. J., and Brady, R. L. (2000) The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator. J. Mol. Biol. 297, 1159-1170
    • (2000) J. Mol. Biol. , vol.297 , pp. 1159-1170
    • Banfield, M.J.1    Brady, R.L.2
  • 20
    • 79960223285 scopus 로고    scopus 로고
    • Molecular mechanism of selectivity among G protein-coupled receptor kinase 2 inhibitors
    • Thal, D. M., Yeow, R. Y., Schoenau, C., Huber, J., and Tesmer, J. J. (2011) Molecular mechanism of selectivity among G protein-coupled receptor kinase 2 inhibitors. Mol. Pharmacol. 80, 294-303
    • (2011) Mol. Pharmacol. , vol.80 , pp. 294-303
    • Thal, D.M.1    Yeow, R.Y.2    Schoenau, C.3    Huber, J.4    Tesmer, J.J.5
  • 22
    • 80051802020 scopus 로고    scopus 로고
    • Raf kinases in cancer roles and therapeutic opportunities
    • Maurer, G., Tarkowski, B., and Baccarini, M. (2011) Raf kinases in cancer roles and therapeutic opportunities. Oncogene 30, 3477-3488
    • (2011) Oncogene , vol.30 , pp. 3477-3488
    • Maurer, G.1    Tarkowski, B.2    Baccarini, M.3
  • 23
    • 1842557438 scopus 로고    scopus 로고
    • Raf kinase inhibitor protein: A prostate cancer metastasis suppressor gene
    • DOI 10.1016/j.canlet.2004.02.006, PII S0304383504001387
    • Keller, E. T., Fu, Z., Yeung, K., and Brennan, M. (2004) Raf kinase inhibitor protein. A prostate cancer metastasis suppressor gene. Cancer Lett. 207, 131-137 (Pubitemid 38457033)
    • (2004) Cancer Letters , vol.207 , Issue.2 , pp. 131-137
    • Keller, E.T.1    Fu, Z.2    Yeung, K.3    Brennan, M.4
  • 26
    • 83555168220 scopus 로고    scopus 로고
    • G protein-coupled receptor kinases. More than just kinases and not only for GPCRs
    • Gurevich, E. V., Tesmer, J. J., Mushegian, A., and Gurevich, V. V. (2012) G protein-coupled receptor kinases. More than just kinases and not only for GPCRs. Pharmacol. Ther. 133, 40-69
    • (2012) Pharmacol. Ther. , vol.133 , pp. 40-69
    • Gurevich, E.V.1    Tesmer, J.J.2    Mushegian, A.3    Gurevich, V.V.4
  • 28
    • 0037631323 scopus 로고    scopus 로고
    • Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein
    • DOI 10.1074/jbc.M210015200
    • Corbit, K. C., Trakul, N., Eves, E. M., Diaz, B., Marshall, M., and Rosner, M. R. (2003) Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J. Biol. Chem. 278, 13061-13068 (Pubitemid 36800074)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 13061-13068
    • Corbit, K.C.1    Trakul, N.2    Eves, E.M.3    Diaz, B.4    Marshall, M.5    Rosner, M.R.6
  • 29
  • 31
    • 0001248650 scopus 로고
    • α-helical coiled coils - A widespread motif in proteins
    • Cohen, C., and Parry, D. A. (1986) α-helical coiled coils - a widespread motif in proteins. Trends Biochem. Sci. 11, 245-248
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 245-248
    • Cohen, C.1    Parry, D.A.2
  • 32
    • 33746942671 scopus 로고    scopus 로고
    • Raf Kinase Inhibitory Protein Regulates Aurora B Kinase and the Spindle Checkpoint
    • DOI 10.1016/j.molcel.2006.07.015, PII S1097276506004965
    • Eves, E. M., Shapiro, P., Naik, K., Klein, U. R., Trakul, N., and Rosner, M. R. (2006) Raf kinase inhibitory protein regulates aurora B kinase and the spindle checkpoint. Mol. Cell 23, 561-574 (Pubitemid 44205493)
    • (2006) Molecular Cell , vol.23 , Issue.4 , pp. 561-574
    • Eves, E.M.1    Shapiro, P.2    Naik, K.3    Klein, U.R.4    Trakul, N.5    Rosner, M.6
  • 33
    • 18444400873 scopus 로고    scopus 로고
    • The biology of a prostate cancer metastasis suppressor protein: Raf kinase inhibitor protein
    • DOI 10.1002/jcb.20169
    • Keller, E. T., Fu, Z., and Brennan, M. (2005) The biology of a prostate cancer metastasis suppressor protein. Raf kinase inhibitor protein. J. Cell Biochem. 94, 273-278 (Pubitemid 41420306)
    • (2005) Journal of Cellular Biochemistry , vol.94 , Issue.2 , pp. 273-278
    • Keller, E.T.1    Fu, Z.2    Brennan, M.3
  • 34
    • 84862929922 scopus 로고    scopus 로고
    • A new model for Raf kinase inhibitory protein induced chemotherapeutic resistance
    • Al-Mulla, F., Bitar, M. S., Feng, J., Park, S., and Yeung, K. C. (2012) A new model for Raf kinase inhibitory protein induced chemotherapeutic resistance. PLoS One 7, e29532
    • (2012) PLoS One , vol.7
    • Al-Mulla, F.1    Bitar, M.S.2    Feng, J.3    Park, S.4    Yeung, K.C.5
  • 36
    • 77951499354 scopus 로고    scopus 로고
    • Raf kinase inhibitor protein enhances neuronal differentiation in human SH-SY5Y cells
    • Hellmann, J., Rommelspacher, H., Mühlbauer, E., and Wernicke, C. (2010) Raf kinase inhibitor protein enhances neuronal differentiation in human SH-SY5Y cells. Dev. Neurosci. 32, 33-46
    • (2010) Dev. Neurosci. , vol.32 , pp. 33-46
    • Hellmann, J.1    Rommelspacher, H.2    Mühlbauer, E.3    Wernicke, C.4
  • 37
    • 78650537920 scopus 로고    scopus 로고
    • Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states
    • Hashimoto, K., and Panchenko, A. R. (2010) Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states. Proc. Natl. Acad. Sci. U.S.A. 107, 20352-20357
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 20352-20357
    • Hashimoto, K.1    Panchenko, A.R.2
  • 38
    • 82955239916 scopus 로고    scopus 로고
    • Phosphorylation in protein-protein binding. Effect on stability and function
    • Nishi, H., Hashimoto, K., and Panchenko, A. R. (2011) Phosphorylation in protein-protein binding. Effect on stability and function. Structure 19, 1807-1815
    • (2011) Structure , vol.19 , pp. 1807-1815
    • Nishi, H.1    Hashimoto, K.2    Panchenko, A.R.3
  • 39
    • 6344260294 scopus 로고    scopus 로고
    • The power of two: Protein dimerization in biology
    • DOI 10.1016/j.tibs.2004.09.006, PII S0968000404002348
    • Marianayagam, N. J., Sunde, M., and Matthews, J. M. (2004) The power of two. Protein dimerization in biology. Trends Biochem. Sci. 29, 618-625 (Pubitemid 39389082)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.11 , pp. 618-625
    • Marianayagam, N.J.1    Sunde, M.2    Matthews, J.M.3
  • 40
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • DOI 10.1016/S0022-2836(02)01281-0
    • Nooren, I. M., and Thornton, J. M. (2003) Structural characterization and functional significance of transient protein-protein interactions. J. Mol. Biol. 325, 991-1018 (Pubitemid 36263408)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 41
    • 0032524356 scopus 로고    scopus 로고
    • Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation
    • DOI 10.1016/S0092-8674(00)81189-7
    • Khokhlatchev, A. V., Canagarajah, B., Wilsbacher, J., Robinson, M., Atkinson, M., Goldsmith, E., and Cobb, M. H. (1998) Phosphorylation of the MAP kinase ERK2 promotes its homodimerization and nuclear translocation. Cell 93, 605-615 (Pubitemid 28240721)
    • (1998) Cell , vol.93 , Issue.4 , pp. 605-615
    • Khokhlatchev, A.V.1    Canagarajah, B.2    Wilsbacher, J.3    Robinson, M.4    Atkinson, M.5    Goldsmith, E.6    Cobb, M.H.7
  • 42
    • 58149351369 scopus 로고    scopus 로고
    • A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy
    • Lorenz, K., Schmitt, J. P., Schmitteckert, E. M., and Lohse, M. J. (2009) A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy. Nat. Med. 15, 75-83
    • (2009) Nat. Med. , vol.15 , pp. 75-83
    • Lorenz, K.1    Schmitt, J.P.2    Schmitteckert, E.M.3    Lohse, M.J.4
  • 43
    • 76749150110 scopus 로고    scopus 로고
    • Analysis of monomeric and dimeric phosphorylated forms of protein kinase R
    • Anderson, E., Quartararo, C., Brown, R. S., Shi, Y., Yao, X., and Cole, J. L. (2010) Analysis of monomeric and dimeric phosphorylated forms of protein kinase R. Biochemistry 49, 1217-1225
    • (2010) Biochemistry , vol.49 , pp. 1217-1225
    • Anderson, E.1    Quartararo, C.2    Brown, R.S.3    Shi, Y.4    Yao, X.5    Cole, J.L.6
  • 45
    • 51649094321 scopus 로고    scopus 로고
    • Built-in loops allow versatility in domain-domain interactions. Lessons from self-interacting domains
    • Akiva, E., Itzhaki, Z., and Margalit, H. (2008) Built-in loops allow versatility in domain-domain interactions. Lessons from self-interacting domains. Proc. Natl. Acad. Sci. U.S.A. 105, 13292-13297
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13292-13297
    • Akiva, E.1    Itzhaki, Z.2    Margalit, H.3
  • 46
    • 0035866015 scopus 로고    scopus 로고
    • Sequence codes for extended conformation: A neighbor-dependent sequence analysis of loops in proteins
    • DOI 10.1002/1097-0134(20010215)42:3<399::AID-PROT100>3.0.CO;2-E
    • Crasto, C. J., and Feng, J. (2001) Sequence codes for extended conformation. A neighbor-dependent sequence analysis of loops in proteins. Proteins 42, 399-413 (Pubitemid 32107764)
    • (2001) Proteins: Structure, Function and Genetics , vol.42 , Issue.3 , pp. 399-413
    • Crasto, C.J.1    Feng, J.-A.2
  • 47
    • 0029109468 scopus 로고
    • Protein-protein interactions. A review of protein dimer structures
    • Jones, S., and Thornton, J. M. (1995) Protein-protein interactions. A review of protein dimer structures. Prog. Biophys. Mol. Biol. 63, 31-65
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 48
    • 32544448846 scopus 로고    scopus 로고
    • A divergent external loop confers antagonistic activity on floral regulators FT and TFL1
    • DOI 10.1038/sj.emboj.7600950, PII 7600950
    • Ahn, J. H., Miller, D., Winter, V. J., Banfield, M. J., Lee, J. H., Yoo, S. Y., Henz, S. R., Brady, R. L., and Weigel, D. (2006) A divergent external loop confers antagonistic activity on floral regulators FT and TFL1. EMBO J. 25, 605-614 (Pubitemid 43237667)
    • (2006) EMBO Journal , vol.25 , Issue.3 , pp. 605-614
    • Ahn, J.H.1    Miller, D.2    Winter, V.J.3    Banfield, M.J.4    Jeong, H.L.5    So, Y.Y.6    Henz, S.R.7    Brady, R.L.8    Weigel, D.9
  • 50
    • 0242637601 scopus 로고    scopus 로고
    • What Is the Role of β-Adrenergic Signaling in Heart Failure?
    • DOI 10.1161/01.RES.0000102042.83024.CA
    • Lohse, M. J., Engelhardt, S., and Eschenhagen, T. (2003) What is the role of β-adrenergic signaling in heart failure? Circ. Res. 93, 896-906 (Pubitemid 37433227)
    • (2003) Circulation Research , vol.93 , Issue.10 , pp. 896-906
    • Lohse, M.J.1    Engelhardt, S.2    Eschenhagen, T.3
  • 51
    • 79961074094 scopus 로고    scopus 로고
    • G protein-coupled receptor kinases as therapeutic targets in cardiovascular disease
    • Belmonte, S. L., and Blaxall, B. C. (2011) G protein-coupled receptor kinases as therapeutic targets in cardiovascular disease. Circ. Res. 109, 309-319
    • (2011) Circ. Res. , vol.109 , pp. 309-319
    • Belmonte, S.L.1    Blaxall, B.C.2
  • 53
    • 0029061324 scopus 로고
    • Cardiac function in mice overexpressing the beta-adrenergic receptor kinase or a β ARK inhibitor
    • Koch, W. J., Rockman, H. A., Samama, P., Hamilton, R. A., Bond, R. A., Milano, C. A., and Lefkowitz, R. J. (1995) Cardiac function in mice overexpressing the beta-adrenergic receptor kinase or a β ARK inhibitor. Science 268, 1350-1353
    • (1995) Science , vol.268 , pp. 1350-1353
    • Koch, W.J.1    Rockman, H.A.2    Samama, P.3    Hamilton, R.A.4    Bond, R.A.5    Milano, C.A.6    Lefkowitz, R.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.