메뉴 건너뛰기




Volumn 30, Issue 12, 2009, Pages 1962-1974

Rck/p54 interacts with APP mRNA as part of a multi-protein complex and enhances APP mRNA and protein expression in neuronal cell lines

Author keywords

Amyloid precursor protein; 3 UTR regulatory elements; Alzheimer's disease; rck p54

Indexed keywords

AMYLOID PRECURSOR PROTEIN; DEAD BOX PROTEIN; ELONGATION FACTOR 1ALPHA; LA ANTIBODY; LA ANTIGEN; NUCLEOLIN; PLASMINOGEN ACTIVATOR INHIBITOR; PROTEIN P54; RNA BINDING PROTEIN; Y BOX BINDING PROTEIN 1;

EID: 70349984421     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2008.02.011     Document Type: Article
Times cited : (13)

References (47)
  • 1
    • 0029163508 scopus 로고
    • The rck/p54 candidate proto-oncogene product is a 54-kilodalton D-E-A-D box protein differentially expressed in human and mouse tissues
    • Akao Y., Marukawa O., Morikawa H., Nakao K., Kamei M., Hachiya T., and Tsujimoto Y. The rck/p54 candidate proto-oncogene product is a 54-kilodalton D-E-A-D box protein differentially expressed in human and mouse tissues. Cancer Res. 55 (1995) 3444-3449
    • (1995) Cancer Res. , vol.55 , pp. 3444-3449
    • Akao, Y.1    Marukawa, O.2    Morikawa, H.3    Nakao, K.4    Kamei, M.5    Hachiya, T.6    Tsujimoto, Y.7
  • 2
    • 0041564122 scopus 로고    scopus 로고
    • A tumour-associated DEAD-box protein, rck/p54 exhibits RNA unwinding activity toward c-myc RNAs in vitro
    • Akao Y., Yoshida H., Matsumoto K., Matsui T., Hogetu K., Tanaka N., and Usukura J. A tumour-associated DEAD-box protein, rck/p54 exhibits RNA unwinding activity toward c-myc RNAs in vitro. Genes Cells 8 (2003) 671-676
    • (2003) Genes Cells , vol.8 , pp. 671-676
    • Akao, Y.1    Yoshida, H.2    Matsumoto, K.3    Matsui, T.4    Hogetu, K.5    Tanaka, N.6    Usukura, J.7
  • 3
    • 0033029151 scopus 로고    scopus 로고
    • TGF-beta(1), regulation of alzheimer amyloid precursor protein mRNA expression in a normal human astrocyte cell line: mRNA stabilization
    • Amara F.M., Junaid A., Clough R.R., and Liang B. TGF-beta(1), regulation of alzheimer amyloid precursor protein mRNA expression in a normal human astrocyte cell line: mRNA stabilization. Brain Res. Mol. Brain Res. 71 (1999) 42-49
    • (1999) Brain Res. Mol. Brain Res. , vol.71 , pp. 42-49
    • Amara, F.M.1    Junaid, A.2    Clough, R.R.3    Liang, B.4
  • 4
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR
    • Balbach J.J., Ishii Y., Antzutkin O.N., Leapman R.D., Rizzo N.W., Dyda F., Reed J., and Tycko R. Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR. Biochemistry 39 (2000) 13748-13759
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzutkin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5    Dyda, F.6    Reed, J.7    Tycko, R.8
  • 5
    • 0029686696 scopus 로고    scopus 로고
    • Evolution of the neuropathology of Alzheimer's disease
    • Braak H., and Braak E. Evolution of the neuropathology of Alzheimer's disease. Acta Neurol. Scand. Suppl. 165 (1996) 3-12
    • (1996) Acta Neurol. Scand. Suppl. , vol.165 , pp. 3-12
    • Braak, H.1    Braak, E.2
  • 6
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • (Discussion 278-284)
    • Braak H., and Braak E. Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging 16 (1995) 271-278 (Discussion 278-284)
    • (1995) Neurobiol. Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 8
    • 0035889956 scopus 로고    scopus 로고
    • Y box-binding factor promotes eosinophil survival by stabilizing granulocyte-macrophage colony-stimulating factor mRNA
    • Capowski E.E., Esnault S., Bhattacharya S., and Malter J.S. Y box-binding factor promotes eosinophil survival by stabilizing granulocyte-macrophage colony-stimulating factor mRNA. J. Immunol. 167 (2001) 5970-5976
    • (2001) J. Immunol. , vol.167 , pp. 5970-5976
    • Capowski, E.E.1    Esnault, S.2    Bhattacharya, S.3    Malter, J.S.4
  • 9
    • 0023502397 scopus 로고
    • Human autoantibody-reactive epitopes of SS-B/La are highly conserved in comparison with epitopes recognized by murine monoclonal antibodies
    • Chan E.K., and Tan E.M. Human autoantibody-reactive epitopes of SS-B/La are highly conserved in comparison with epitopes recognized by murine monoclonal antibodies. J. Exp. Med. 166 (1987) 1627-1640
    • (1987) J. Exp. Med. , vol.166 , pp. 1627-1640
    • Chan, E.K.1    Tan, E.M.2
  • 10
    • 0028114995 scopus 로고
    • The effects of aging and hormonal manipulation on amyloid precursor protein APP695 mRNA expression in the rat hippocampus
    • Chao H.M., Spencer R.L., Frankfurt M., and McEwen B.S. The effects of aging and hormonal manipulation on amyloid precursor protein APP695 mRNA expression in the rat hippocampus. J. Neuroendocrinol. 6 (1994) 517-521
    • (1994) J. Neuroendocrinol. , vol.6 , pp. 517-521
    • Chao, H.M.1    Spencer, R.L.2    Frankfurt, M.3    McEwen, B.S.4
  • 11
    • 33745894330 scopus 로고    scopus 로고
    • Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54
    • Chu C.Y., and Rana T.M. Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54. PLoS Biol. 4 (2006) e210
    • (2006) PLoS Biol. , vol.4
    • Chu, C.Y.1    Rana, T.M.2
  • 12
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller J., and Parker R. General translational repression by activators of mRNA decapping. Cell 122 (2005) 875-886
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 13
    • 0035674477 scopus 로고    scopus 로고
    • The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes
    • Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., and Parker R. The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 7 (2001) 1717-1727
    • (2001) RNA , vol.7 , pp. 1717-1727
    • Coller, J.M.1    Tucker, M.2    Sheth, U.3    Valencia-Sanchez, M.A.4    Parker, R.5
  • 14
    • 33845483366 scopus 로고    scopus 로고
    • Progesterone regulation of human granulosa/luteal cell viability by an RU486-independent mechanism
    • Engmann L., Losel R., Wehling M., and Peluso J.J. Progesterone regulation of human granulosa/luteal cell viability by an RU486-independent mechanism. J. Clin. Endocrinol. Metab. 91 (2006) 4962-4968
    • (2006) J. Clin. Endocrinol. Metab. , vol.91 , pp. 4962-4968
    • Engmann, L.1    Losel, R.2    Wehling, M.3    Peluso, J.J.4
  • 16
    • 0035793586 scopus 로고    scopus 로고
    • Identification and cDNA cloning of a novel RNA-binding protein that interacts with the cyclic nucleotide-responsive sequence in the Type-1 plasminogen activator inhibitor mRNA
    • Heaton J.H., Dlakic W.M., Dlakic M., and Gelehrter T.D. Identification and cDNA cloning of a novel RNA-binding protein that interacts with the cyclic nucleotide-responsive sequence in the Type-1 plasminogen activator inhibitor mRNA. J. Biol. Chem. 276 (2001) 3341-3347
    • (2001) J. Biol. Chem. , vol.276 , pp. 3341-3347
    • Heaton, J.H.1    Dlakic, W.M.2    Dlakic, M.3    Gelehrter, T.D.4
  • 17
    • 0038150766 scopus 로고    scopus 로고
    • Posttranscriptional regulation of PAI-1 gene expression
    • Heaton J.H., Dlakic W.M., and Gelehrter T.D. Posttranscriptional regulation of PAI-1 gene expression. Thromb. Haemost. 89 (2003) 959-966
    • (2003) Thromb. Haemost. , vol.89 , pp. 959-966
    • Heaton, J.H.1    Dlakic, W.M.2    Gelehrter, T.D.3
  • 19
    • 13444251381 scopus 로고    scopus 로고
    • Human ribosomal protein S26 suppresses the splicing of its pre-mRNA
    • Ivanov A.V., Malygin A.A., and Karpova G.G. Human ribosomal protein S26 suppresses the splicing of its pre-mRNA. Biochim. Biophys. Acta 1727 (2005) 134-140
    • (2005) Biochim. Biophys. Acta , vol.1727 , pp. 134-140
    • Ivanov, A.V.1    Malygin, A.A.2    Karpova, G.G.3
  • 20
    • 4143051231 scopus 로고    scopus 로고
    • Structural basis for the binding of didemnins to human elongation factor eEF1A and rationale for the potent antitumor activity of these marine natural products
    • Marco E., Martin-Santamaria S., Cuevas C., and Gago F. Structural basis for the binding of didemnins to human elongation factor eEF1A and rationale for the potent antitumor activity of these marine natural products. J. Med. Chem. 47 (2004) 4439-4452
    • (2004) J. Med. Chem. , vol.47 , pp. 4439-4452
    • Marco, E.1    Martin-Santamaria, S.2    Cuevas, C.3    Gago, F.4
  • 21
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 430 (2004) 631-639
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 22
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson M.P. Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol. Rev. 77 (1997) 1081-1132
    • (1997) Physiol. Rev. , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 23
    • 0031010632 scopus 로고    scopus 로고
    • Human La protein: a stabilizer of histone mRNA
    • McLaren R.S., Caruccio N., and Ross J. Human La protein: a stabilizer of histone mRNA. Mol. Cell. Biol 17 (1997) 3028-3036
    • (1997) Mol. Cell. Biol , vol.17 , pp. 3028-3036
    • McLaren, R.S.1    Caruccio, N.2    Ross, J.3
  • 24
    • 0025099393 scopus 로고
    • A high yield affinity purification method for specific RNA-binding proteins: isolation of the iron regulatory factor from human placenta
    • Neupert B., Thompson N.A., Meyer C., and Kuhn L.C. A high yield affinity purification method for specific RNA-binding proteins: isolation of the iron regulatory factor from human placenta. Nucleic Acids Res. 18 (1990) 51-55
    • (1990) Nucleic Acids Res. , vol.18 , pp. 51-55
    • Neupert, B.1    Thompson, N.A.2    Meyer, C.3    Kuhn, L.C.4
  • 25
    • 0024093904 scopus 로고
    • Expression of the Alzheimer amyloid precursor gene transcripts in the human brain
    • Neve R.L., Finch E.A., and Dawes L.R. Expression of the Alzheimer amyloid precursor gene transcripts in the human brain. Neuron 1 (1988) 669-677
    • (1988) Neuron , vol.1 , pp. 669-677
    • Neve, R.L.1    Finch, E.A.2    Dawes, L.R.3
  • 26
    • 0028055038 scopus 로고
    • Down's syndrome: up-regulation of beta-amyloid protein precursor and tau mRNAs and their defective coordination
    • Oyama F., Cairns N.J., Shimada H., Oyama R., Titani K., and Ihara Y. Down's syndrome: up-regulation of beta-amyloid protein precursor and tau mRNAs and their defective coordination. J. Neurochem. 62 (1994) 1062-1066
    • (1994) J. Neurochem. , vol.62 , pp. 1062-1066
    • Oyama, F.1    Cairns, N.J.2    Shimada, H.3    Oyama, R.4    Titani, K.5    Ihara, Y.6
  • 28
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNA turnover
    • Parker R., and Song H. The enzymes and control of eukaryotic mRNA turnover. Nat. Struct. Mol. Biol. 11 (2004) 121-127
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2
  • 29
    • 22544457891 scopus 로고    scopus 로고
    • Expression and function of PAIRBP1 within gonadotropin-primed immature rat ovaries: PAIRBP1 regulation of granulosa and luteal cell viability
    • Peluso J.J., Pappalardo A., Losel R., and Wehling M. Expression and function of PAIRBP1 within gonadotropin-primed immature rat ovaries: PAIRBP1 regulation of granulosa and luteal cell viability. Biol. Reprod. 73 (2005) 261-270
    • (2005) Biol. Reprod. , vol.73 , pp. 261-270
    • Peluso, J.J.1    Pappalardo, A.2    Losel, R.3    Wehling, M.4
  • 30
    • 0028885682 scopus 로고
    • Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro
    • Pike C.J., Overman M.J., and Cotman C.W. Amino-terminal deletions enhance aggregation of beta-amyloid peptides in vitro. J. Biol. Chem. 270 (1995) 23895-23898
    • (1995) J. Biol. Chem. , vol.270 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 31
    • 0025287621 scopus 로고
    • Purification and characterization of proteins of heterogeneous nuclear ribonucleoprotein complexes by affinity chromatography
    • Pinol-Roma S., Swanson M.S., Matunis M.J., and Dreyfuss G. Purification and characterization of proteins of heterogeneous nuclear ribonucleoprotein complexes by affinity chromatography. Methods Enzymol. 181 (1990) 326-331
    • (1990) Methods Enzymol. , vol.181 , pp. 326-331
    • Pinol-Roma, S.1    Swanson, M.S.2    Matunis, M.J.3    Dreyfuss, G.4
  • 32
    • 0029111450 scopus 로고
    • Anti-La monoclonal antibodies recognizing epitopes within the RNA-binding domain of the La protein show differential capacities to immunoprecipitate RNA-associated La protein
    • Pruijn G.J., Thijssen J.P., Smith P.R., Williams D.G., and Van Venrooij W.J. Anti-La monoclonal antibodies recognizing epitopes within the RNA-binding domain of the La protein show differential capacities to immunoprecipitate RNA-associated La protein. Eur. J. Biochem. 232 (1995) 611-619
    • (1995) Eur. J. Biochem. , vol.232 , pp. 611-619
    • Pruijn, G.J.1    Thijssen, J.P.2    Smith, P.R.3    Williams, D.G.4    Van Venrooij, W.J.5
  • 35
    • 1642442715 scopus 로고    scopus 로고
    • Identification of nucleolin as an AU-rich element binding protein involved in bcl-2 mRNA stabilization
    • Sengupta T.K., Bandyopadhyay S., Fernandes D.J., and Spicer E.K. Identification of nucleolin as an AU-rich element binding protein involved in bcl-2 mRNA stabilization. J. Biol. Chem. 279 (2004) 10855-10863
    • (2004) J. Biol. Chem. , vol.279 , pp. 10855-10863
    • Sengupta, T.K.1    Bandyopadhyay, S.2    Fernandes, D.J.3    Spicer, E.K.4
  • 36
    • 3142728532 scopus 로고    scopus 로고
    • Nucleolin is a second component of the CD154 mRNA stability complex that regulates mRNA turnover in activated T cells
    • Singh K., Laughlin J., Kosinski P.A., and Covey L.R. Nucleolin is a second component of the CD154 mRNA stability complex that regulates mRNA turnover in activated T cells. J. Immunol. 173 (2004) 976-985
    • (2004) J. Immunol. , vol.173 , pp. 976-985
    • Singh, K.1    Laughlin, J.2    Kosinski, P.A.3    Covey, L.R.4
  • 37
    • 0024009108 scopus 로고
    • Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities
    • Swanson M.S., and Dreyfuss G. Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities. Mol. Cell. Biol. 8 (1988) 2237-2241
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2237-2241
    • Swanson, M.S.1    Dreyfuss, G.2
  • 38
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: from generic motors to specific dissociation functions
    • Tanner N.K., and Linder P. DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol. Cell 8 (2001) 251-262
    • (2001) Mol. Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 40
    • 0033927385 scopus 로고    scopus 로고
    • Transduction of full-length Tat fusion proteins directly into mammalian cells: analysis of T cell receptor activation-induced cell death
    • Vocero-Akbani A., Lissy N.A., and Dowdy S.F. Transduction of full-length Tat fusion proteins directly into mammalian cells: analysis of T cell receptor activation-induced cell death. Methods Enzymol. 322 (2000) 508-521
    • (2000) Methods Enzymol. , vol.322 , pp. 508-521
    • Vocero-Akbani, A.1    Lissy, N.A.2    Dowdy, S.F.3
  • 41
    • 0035919129 scopus 로고    scopus 로고
    • Extracellular-regulated kinase controls beta-amyloid precursor protein mRNA decay
    • Westmark C.J., and Malter J.S. Extracellular-regulated kinase controls beta-amyloid precursor protein mRNA decay. Brain Res. Mol. Brain Res. 90 (2001) 193-201
    • (2001) Brain Res. Mol. Brain Res. , vol.90 , pp. 193-201
    • Westmark, C.J.1    Malter, J.S.2
  • 43
    • 33745159015 scopus 로고    scopus 로고
    • Xp54 and related (DDX6-like) RNA helicases: roles in messenger RNP assembly, translation regulation and RNA degradation
    • Weston A., and Sommerville J. Xp54 and related (DDX6-like) RNA helicases: roles in messenger RNP assembly, translation regulation and RNA degradation. Nucleic Acids Res. 34 (2006) 3082-3094
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3082-3094
    • Weston, A.1    Sommerville, J.2
  • 44
    • 33746334783 scopus 로고    scopus 로고
    • Endogenous neuroprotective factors: neurosteroids
    • Wojtal K., Trojnar M.K., and Czuczwar S.J. Endogenous neuroprotective factors: neurosteroids. Pharmacol. Rep. 58 (2006) 335-340
    • (2006) Pharmacol. Rep. , vol.58 , pp. 335-340
    • Wojtal, K.1    Trojnar, M.K.2    Czuczwar, S.J.3
  • 45
    • 0028096546 scopus 로고
    • Multiple proteins interact at a unique cis-element in the 3′-untranslated region of amyloid precursor protein mRNA
    • Zaidi S.H., Denman R., and Malter J.S. Multiple proteins interact at a unique cis-element in the 3′-untranslated region of amyloid precursor protein mRNA. J. Biol. Chem. 269 (1994) 24000-24006
    • (1994) J. Biol. Chem. , vol.269 , pp. 24000-24006
    • Zaidi, S.H.1    Denman, R.2    Malter, J.S.3
  • 46
    • 0029125216 scopus 로고
    • Nucleolin and heterogeneous nuclear ribonucleoprotein C proteins specifically interact with the 3′-untranslated region of amyloid protein precursor mRNA
    • Zaidi S.H., and Malter J.S. Nucleolin and heterogeneous nuclear ribonucleoprotein C proteins specifically interact with the 3′-untranslated region of amyloid protein precursor mRNA. J. Biol. Chem. 270 (1995) 17292-17298
    • (1995) J. Biol. Chem. , vol.270 , pp. 17292-17298
    • Zaidi, S.H.1    Malter, J.S.2
  • 47
    • 0028061197 scopus 로고
    • Amyloid precursor protein mRNA stability is controlled by a 29-base element in the 3′-untranslated region
    • Zaidi S.H., and Malter J.S. Amyloid precursor protein mRNA stability is controlled by a 29-base element in the 3′-untranslated region. J. Biol. Chem. 269 (1994) 24007-24013
    • (1994) J. Biol. Chem. , vol.269 , pp. 24007-24013
    • Zaidi, S.H.1    Malter, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.