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Volumn 15, Issue 1, 2005, Pages 19-23

Modulation of the MAP kinase signaling cascade by Raf kinase inhibitory protein

Author keywords

MAPK; PKC; Raf; RKIP

Indexed keywords

PROTEIN KINASE C; RAF PROTEIN;

EID: 19644383643     PISSN: 10010602     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cr.7290258     Document Type: Short Survey
Times cited : (88)

References (34)
  • 1
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: Regulation and physiological functions
    • Pearson G, Robinson F, Beers Gibson, et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr Rev 2001; 22:153-83.
    • (2001) Endocr Rev , vol.22 , pp. 153-183
    • Pearson, G.1    Robinson, F.2    Gibson, B.3
  • 2
    • 0034667593 scopus 로고    scopus 로고
    • Meaningful relationships: The regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
    • Kolch W. Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions. Biochem J 2000; 351 Pt 2:289-305.
    • (2000) Biochem J , vol.351 , Issue.2 PART , pp. 289-305
    • Kolch, W.1
  • 4
    • 0032511882 scopus 로고    scopus 로고
    • The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
    • King AJ, Sun H, Diaz B, et al. The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature 1998; 396:180-3.
    • (1998) Nature , vol.396 , pp. 180-183
    • King, A.J.1    Sun, H.2    Diaz, B.3
  • 5
    • 0027168907 scopus 로고
    • Identification of the major phosphorylation sites of the Raf-1 kinase
    • Morrison DK, Heidecker G, Rapp UR, Copeland TD. Identification of the major phosphorylation sites of the Raf-1 kinase. J Biol Chem 1993; 268:17309-16.
    • (1993) J Biol Chem , vol.268 , pp. 17309-17316
    • Morrison, D.K.1    Heidecker, G.2    Rapp, U.R.3    Copeland, T.D.4
  • 6
    • 1342301559 scopus 로고    scopus 로고
    • Conferring specificity on the ubiquitous Raf/MEK signalling pathway
    • O'Neill E, Kolch W. Conferring specificity on the ubiquitous Raf/MEK signalling pathway. Br J Cancer 2004; 90:283-8.
    • (2004) Br J Cancer , vol.90 , pp. 283-288
    • O'Neill, E.1    Kolch, W.2
  • 7
    • 0034306451 scopus 로고    scopus 로고
    • Regulation of the Raf-1 kinase domain by phosphorylation and 14-3-3 association
    • Yip-Schneider MT, Miao W, Lin A, et al. Regulation of the Raf-1 kinase domain by phosphorylation and 14-3-3 association. Biochem J 2000; 351:151-9.
    • (2000) Biochem J , vol.351 , pp. 151-159
    • Yip-Schneider, M.T.1    Miao, W.2    Lin, A.3
  • 8
    • 0022445734 scopus 로고    scopus 로고
    • Ligand-binding studies with a 23 kDa protein purified from bovine brain cytosol
    • Bernier I, Tresca JP, Jolles P. Ligand-binding studies with a 23 kDa protein purified from bovine brain cytosol. Biochim Biophys Acta 1998; 871:19-23.
    • (1998) Biochim Biophys Acta , vol.871 , pp. 19-23
    • Bernier, I.1    Tresca, J.P.2    Jolles, P.3
  • 9
    • 0032748447 scopus 로고    scopus 로고
    • Localisation of phosphatidylethanolamine-binding protein in the brain and other tissues of the rat
    • Frayne J, Ingram C, Love S, Hall L. Localisation of phosphatidylethanolamine-binding protein in the brain and other tissues of the rat. Cell Tissue Res 1999; 298:415-23.
    • (1999) Cell Tissue Res , vol.298 , pp. 415-423
    • Frayne, J.1    Ingram, C.2    Love, S.3    Hall, L.4
  • 10
    • 0032532458 scopus 로고    scopus 로고
    • Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction
    • Banfield MJ, Barker JJ, Perry AC, Brady RL. Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure 1998; 6:1245-54.
    • (1998) Structure , vol.6 , pp. 1245-1254
    • Banfield, M.J.1    Barker, J.J.2    Perry, A.C.3    Brady, R.L.4
  • 11
    • 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, Vallee B, Bureaud N, Schoentgen F, Zelwer C. Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins. Structure 1998; 6:1255-65.
    • (1998) Structure , vol.6 , pp. 1255-1265
    • Serre, L.1    Vallee, B.2    Bureaud, N.3    Schoentgen, F.4    Zelwer, C.5
  • 12
    • 0035854480 scopus 로고    scopus 로고
    • Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein
    • Serre L, Pereira de Jesus K, Zelwer C, et al. Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein. J Mol Biol 2001; 310:617-34.
    • (2001) J Mol Biol , vol.310 , pp. 617-634
    • Serre, L.1    De Pereira Jesus, K.2    Zelwer, C.3
  • 13
    • 0032532458 scopus 로고    scopus 로고
    • Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction
    • Banfield MJ, Barker JJ, Perry AC, Brady RL. Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure 1998; 6:1245-54.
    • (1998) Structure , vol.6 , pp. 1245-1254
    • Banfield, M.J.1    Barker, J.J.2    Perry, A.C.3    Brady, R.L.4
  • 15
    • 0035170831 scopus 로고    scopus 로고
    • Behaviour of bovine phosphatidylethanolamine-binding protein with model membranes. Evidence of affinity for negatively charged membranes
    • Vallee BS, Tauc P, Brochon JC, et al. Behaviour of bovine phosphatidylethanolamine-binding protein with model membranes. Evidence of affinity for negatively charged membranes. Eur J Biochem 2001; 268:5831-41.
    • (2001) Eur J Biochem , vol.268 , pp. 5831-5841
    • Vallee, B.S.1    Tauc, P.2    Brochon, J.C.3
  • 16
    • 0032502257 scopus 로고    scopus 로고
    • A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins
    • Bruun AW, Svendsen I, Sorensen SO, Kielland-Brandt MC, Winther JR. A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins. Biochemistry 1998; 37:3351-7.
    • (1998) Biochemistry , vol.37 , pp. 3351-3357
    • Bruun, A.W.1    Svendsen, I.2    Sorensen, S.O.3    Kielland-Brandt, M.C.4    Winther, J.R.5
  • 17
    • 0035542777 scopus 로고    scopus 로고
    • Tomato SP-interacting proteins define a conserved signaling system that regulates shoot architecture and flowering
    • Pnueli L, Gutfinger T, Hareven D, et al. Tomato SP-interacting proteins define a conserved signaling system that regulates shoot architecture and flowering. Plant Cell 2001; 13:2687-702.
    • (2001) Plant Cell , vol.13 , pp. 2687-2702
    • Pnueli, L.1    Gutfinger, T.2    Hareven, D.3
  • 18
    • 0035808362 scopus 로고    scopus 로고
    • The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors
    • Hengst U, Albrecht H, Hess D, Monard D. The phosphatidylethanolamine- binding protein is the prototype of a novel family of serine protease inhibitors. J Biol Chem 2001; 276:535-40.
    • (2001) J Biol Chem , vol.276 , pp. 535-540
    • Hengst, U.1    Albrecht, H.2    Hess, D.3    Monard, D.4
  • 19
    • 0033988536 scopus 로고    scopus 로고
    • Hippocampal cholinergic neurostimulating peptides (HCNP)
    • Ojika K, Mitake S, Tohdoh N, et al. Hippocampal cholinergic neurostimulating peptides (HCNP). Prog Neurobiol 2000; 60:37-83.
    • (2000) Prog Neurobiol , vol.60 , pp. 37-83
    • Ojika, K.1    Mitake, S.2    Tohdoh, N.3
  • 20
    • 0031735328 scopus 로고    scopus 로고
    • High levels of hippocampal cholinergic neurostimulating peptide (HCNP) in the CSF of some patients with Alzheimer's disease
    • Tsugu Y, Ojika K, Matsukawa N, et al. High levels of hippocampal cholinergic neurostimulating peptide (HCNP) in the CSF of some patients with Alzheimer's disease. Eur J Neurol 1998; 5:561-9.
    • (1998) Eur J Neurol , vol.5 , pp. 561-569
    • Tsugu, Y.1    Ojika, K.2    Matsukawa, N.3
  • 21
    • 0032889093 scopus 로고    scopus 로고
    • Increased expression of hippocampal cholinergic neurostimulating peptide-related components and their messenger RNAs in the hippocampus of aged senescence-accelerated mice
    • Matsukawa N, Tooyama I, Kimura H, et al. Increased expression of hippocampal cholinergic neurostimulating peptide-related components and their messenger RNAs in the hippocampus of aged senescence-accelerated mice. Neuroscience 1999; 88:79-92.
    • (1999) Neuroscience , vol.88 , pp. 79-92
    • Matsukawa, N.1    Tooyama, I.2    Kimura, H.3
  • 22
    • 0028860356 scopus 로고
    • Phosphatidylethanolamine binding protein is an abundant secretory product of haploid testicular germ cells in the rat
    • Saunders PT, McKinnell C, Millar MR, et al. Phosphatidylethanolamine binding protein is an abundant secretory product of haploid testicular germ cells in the rat. Mol Cell Endocrinol 1995; 107:221-30.
    • (1995) Mol Cell Endocrinol , vol.107 , pp. 221-230
    • Saunders, P.T.1    McKinnell, C.2    Millar, M.R.3
  • 23
    • 18544363595 scopus 로고    scopus 로고
    • Identification of a novel testis-specific member of the phosphatidylethanolamine binding protein family, pebp-2
    • Hickox DM, Gibbs G, Morrison JR, et al. Identification of a novel testis-specific member of the phosphatidylethanolamine binding protein family, pebp-2. Biol Reprod 2002; 67:917-27.
    • (2002) Biol Reprod , vol.67 , pp. 917-927
    • Hickox, D.M.1    Gibbs, G.2    Morrison, J.R.3
  • 24
    • 0033539167 scopus 로고    scopus 로고
    • Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP
    • Yeung K, Seitz T, Li S, et al. Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP. Nature 1999; 401:173-7.
    • (1999) Nature , vol.401 , pp. 173-177
    • Yeung, K.1    Seitz, T.2    Li, S.3
  • 25
    • 0034791116 scopus 로고    scopus 로고
    • Raf kinase inhibitor protein interacts with NF-kappaB-inducing kinase and TAK1 and inhibits NF-kappaB activation
    • Yeung KC, Rose DW, Dhillon AS, et al. Raf kinase inhibitor protein interacts with NF-kappaB-inducing kinase and TAK1 and inhibits NF-kappaB activation. Mol Cell Biol 2001; 21:7207-17.
    • (2001) Mol Cell Biol , vol.21 , pp. 7207-7217
    • Yeung, K.C.1    Rose, D.W.2    Dhillon, A.S.3
  • 26
    • 0035955736 scopus 로고    scopus 로고
    • Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling
    • Kroslak T, Koch T, Kahl E, Hollt V. Human phosphatidylethanolamine- binding protein facilitates heterotrimeric G protein-dependent signaling. J Biol Chem 2001; 276:39772-8.
    • (2001) J Biol Chem , vol.276 , pp. 39772-39778
    • Kroslak, T.1    Koch, T.2    Kahl, E.3    Hollt, V.4
  • 27
    • 0346874333 scopus 로고    scopus 로고
    • Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2
    • Lorenz K, Lohse MJ, Quitterer U. Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2. Nature 2003; 426:574-9.
    • (2003) Nature , vol.426 , pp. 574-579
    • Lorenz, K.1    Lohse, M.J.2    Quitterer, U.3
  • 28
    • 0037631323 scopus 로고    scopus 로고
    • Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein
    • Corbit KC, Trakul N, Eves EM, et al. Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J Biol Chem 2003; 278:13061-8.
    • (2003) J Biol Chem , vol.278 , pp. 13061-13068
    • Corbit, K.C.1    Trakul, N.2    Eves, E.M.3
  • 29
    • 0038275924 scopus 로고    scopus 로고
    • Effects of raf kinase inhibitor protein expression on suppression of prostate cancer metastasis
    • Fu Z, Smith PC, Zhang L, et al. Effects of raf kinase inhibitor protein expression on suppression of prostate cancer metastasis. J Natl Cancer Inst 2003; 95:878-89.
    • (2003) J Natl Cancer Inst , vol.95 , pp. 878-889
    • Fu, Z.1    Smith, P.C.2    Zhang, L.3
  • 30
    • 2342435822 scopus 로고    scopus 로고
    • RKIP sensitizes prostate and breast cancer cells to drug-induced apoptosis
    • Chatterjee D, Bai Y, Wang Z, et al. RKIP sensitizes prostate and breast cancer cells to drug-induced apoptosis. J Biol Chem 2004; 279:17515-23.
    • (2004) J Biol Chem , vol.279 , pp. 17515-17523
    • Chatterjee, D.1    Bai, Y.2    Wang, Z.3
  • 31
    • 0037631323 scopus 로고    scopus 로고
    • Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein
    • Corbit KC, Trakul N, Eves EM, et al. Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J Biol Chem 2003; 278:13061-8.
    • (2003) J Biol Chem , vol.278 , pp. 13061-13068
    • Corbit, K.C.1    Trakul, N.2    Eves, E.M.3
  • 33
    • 0033927901 scopus 로고    scopus 로고
    • Different protein kinase C isoforms determine growth factor specificity in neuronal cells
    • Corbit KC, Soh JW, Yoshida K, et al. Different protein kinase C isoforms determine growth factor specificity in neuronal cells. Mol Cell Biol 2000; 20:5392-403.
    • (2000) Mol Cell Biol , vol.20 , pp. 5392-5403
    • Corbit, K.C.1    Soh, J.W.2    Yoshida, K.3
  • 34
    • 0032588943 scopus 로고    scopus 로고
    • Protein kinase Cdelta mediates neurogenic but not mitogenic activation of mitogen-activated protein kinase in neuronal cells
    • Corbit KC, Foster DA, Rosner MR. Protein kinase Cdelta mediates neurogenic but not mitogenic activation of mitogen-activated protein kinase in neuronal cells. Mol Cell Biol 1999; 19:4209-18.
    • (1999) Mol Cell Biol , vol.19 , pp. 4209-4218
    • Corbit, K.C.1    Foster, D.A.2    Rosner, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.