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Volumn 288, Issue 4, 2013, Pages 2816-2828

Serine arginine splicing factor 3 is involved in enhanced splicing of glucose-6-phosphate dehydrogenase RNA in response to nutrients and hormones in liver

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONIC ACIDS; COACTIVATORS; GLUCOSE-6-PHOSPHATE DEHYDROGENASE; IMMUNOPRECIPITATION ANALYSIS; INTACT CELLS; LIVER CELLS; NUCLEAR EXTRACTS; RAT HEPATOCYTES; REFEEDING; REGULATORY MECHANISM; SPLICING ENHANCER; SPLICING FACTORS; SR PROTEIN;

EID: 84873832617     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.410803     Document Type: Article
Times cited : (32)

References (50)
  • 2
    • 33845948995 scopus 로고    scopus 로고
    • An exonic splicing silencer is involved in the regulated splicing of glucose-6-phosphate dehydrogenase mRNA
    • Szeszel-Fedorowicz, W., Talukdar, I., Griffith, B. N., Walsh, C. M., and Salati, L. M. (2006) An exonic splicing silencer is involved in the regulated splicing of glucose-6-phosphate dehydrogenase mRNA. J. Biol. Chem. 281, 34146-34158
    • (2006) J. Biol. Chem. , vol.281 , pp. 34146-34158
    • Szeszel-Fedorowicz, W.1    Talukdar, I.2    Griffith, B.N.3    Walsh, C.M.4    Salati, L.M.5
  • 3
    • 80053027909 scopus 로고    scopus 로고
    • Functional consequences of developmentally regulated alternative splicing
    • Kalsotra, A., and Cooper, T. A. (2011) Functional consequences of developmentally regulated alternative splicing. Nat. Rev. Genet. 12, 715-729
    • (2011) Nat. Rev. Genet. , vol.12 , pp. 715-729
    • Kalsotra, A.1    Cooper, T.A.2
  • 4
    • 38349085591 scopus 로고    scopus 로고
    • Regulation of alternative splicing by reversible protein phosphorylation
    • Stamm, S. (2008) Regulation of alternative splicing by reversible protein phosphorylation. J. Biol. Chem. 283, 1223-1227
    • (2008) J. Biol. Chem. , vol.283 , pp. 1223-1227
    • Stamm, S.1
  • 5
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
    • Pan, Q., Shai, O., Lee, L. J., Frey, B. J., and Blencowe, B. J. (2008) Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing. Nat. Genet. 40, 1413-1415
    • (2008) Nat. Genet. , vol.40 , pp. 1413-1415
    • Pan, Q.1    Shai, O.2    Lee, L.J.3    Frey, B.J.4    Blencowe, B.J.5
  • 6
    • 58249093940 scopus 로고    scopus 로고
    • The SR protein family of splicing factors. Master regulators of gene expression
    • Long, J. C., and Caceres, J. F. (2009) The SR protein family of splicing factors. Master regulators of gene expression. Biochem. J. 417, 15-27
    • (2009) Biochem. J. , vol.417 , pp. 15-27
    • Long, J.C.1    Caceres, J.F.2
  • 7
    • 0035691667 scopus 로고    scopus 로고
    • Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins
    • Zhu, J., Mayeda, A., and Krainer, A. R. (2001) Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins. Mol. Cell 8, 1351-1361
    • (2001) Mol. Cell , vol.8 , pp. 1351-1361
    • Zhu, J.1    Mayeda, A.2    Krainer, A.R.3
  • 8
    • 42449159377 scopus 로고    scopus 로고
    • SR proteins and related factors in alternative splicing
    • Lin, S., and Fu, X. D. (2007) SR proteins and related factors in alternative splicing. Adv. Exp. Med. Biol. 623, 107-122
    • (2007) Adv. Exp. Med. Biol. , vol.623 , pp. 107-122
    • Lin, S.1    Fu, X.D.2
  • 10
    • 66449111724 scopus 로고    scopus 로고
    • Akt2 regulation of Cdc2-like kinases (Clk/Sty), serine/arginine-rich (SR) protein phosphorylation, and insulin-induced alternative splicing of PKCbetaII messenger ribonucleic acid
    • Jiang, K., Patel, N. A., Watson, J. E., Apostolatos, H., Kleiman, E., Hanson, O., Hagiwara, M., and Cooper, D. R. (2009) Akt2 regulation of Cdc2-like kinases (Clk/Sty), serine/arginine-rich (SR) protein phosphorylation, and insulin-induced alternative splicing of PKCbetaII messenger ribonucleic acid. Endocrinology 150, 2087-2097
    • (2009) Endocrinology , vol.150 , pp. 2087-2097
    • Jiang, K.1    Patel, N.A.2    Watson, J.E.3    Apostolatos, H.4    Kleiman, E.5    Hanson, O.6    Hagiwara, M.7    Cooper, D.R.8
  • 11
    • 20244372405 scopus 로고    scopus 로고
    • Molecular and genetic studies imply Akt-mediated signaling promotes protein kinase CβII alternative splicing via phosphorylation of serine/arginine-rich splicing factor SRp40
    • Patel, N. A., Kaneko, S., Apostolatos, H. S., Bae, S. S., Watson, J. E., Davidowitz, K., Chappell, D. S., Birnbaum, M. J., Cheng, J. Q., and Cooper, D. R. (2005) Molecular and genetic studies imply Akt-mediated signaling promotes protein kinase CβII alternative splicing via phosphorylation of serine/arginine-rich splicing factor SRp40. J. Biol. Chem. 280, 14302-14309
    • (2005) J. Biol. Chem. , vol.280 , pp. 14302-14309
    • Patel, N.A.1    Kaneko, S.2    Apostolatos, H.S.3    Bae, S.S.4    Watson, J.E.5    Davidowitz, K.6    Chappell, D.S.7    Birnbaum, M.J.8    Cheng, J.Q.9    Cooper, D.R.10
  • 12
    • 0018800384 scopus 로고
    • Rate-limiting steps in metabolic pathways
    • Rognstad, R. (1979) Rate-limiting steps in metabolic pathways. J. Biol. Chem. 254, 1875-1878
    • (1979) J. Biol. Chem. , vol.254 , pp. 1875-1878
    • Rognstad, R.1
  • 13
    • 0035971196 scopus 로고    scopus 로고
    • Regulation of the processing of glucose-6-phosphate dehydrogenase mRNA by nutritional status
    • Amir-Ahmady, B., and Salati, L. M. (2001) Regulation of the processing of glucose-6-phosphate dehydrogenase mRNA by nutritional status. J. Biol. Chem. 276, 10514-10523
    • (2001) J. Biol. Chem. , vol.276 , pp. 10514-10523
    • Amir-Ahmady, B.1    Salati, L.M.2
  • 14
    • 0030586745 scopus 로고    scopus 로고
    • Posttranscriptional regulation of glucose-6-phosphate dehydrogenase by dietary polyunsaturated fat
    • Stabile, L. P., Hodge, D. L., Klautky, S. A., and Salati, L. M. (1996) Posttranscriptional regulation of glucose-6-phosphate dehydrogenase by dietary polyunsaturated fat. Arch Biochem. Biophys 332, 269-279
    • (1996) Arch Biochem. Biophys , vol.332 , pp. 269-279
    • Stabile, L.P.1    Hodge, D.L.2    Klautky, S.A.3    Salati, L.M.4
  • 15
    • 0037163115 scopus 로고    scopus 로고
    • Inhibition of the splicing of glucose-6- phosphate dehydrogenase precursor mRNA by polyunsaturated fatty acids
    • Tao, H., Szeszel-Fedorowicz, W., Amir-Ahmady, B., Gibson, M. A., Stabile, L. P., and Salati, L. M. (2002) Inhibition of the splicing of glucose-6- phosphate dehydrogenase precursor mRNA by polyunsaturated fatty acids. J. Biol. Chem. 277, 31270-31278
    • (2002) J. Biol. Chem. , vol.277 , pp. 31270-31278
    • Tao, H.1    Szeszel-Fedorowicz, W.2    Amir-Ahmady, B.3    Gibson, M.A.4    Stabile, L.P.5    Salati, L.M.6
  • 16
    • 0031660939 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids inhibit the expression of the glucose-6-phosphate dehydrogenase gene in primary rat hepatocytes by a nuclear posttranscriptional mechanism
    • Stabile, L. P., Klautky, S. A., Minor, S. M., and Salati, L. M. (1998) Polyunsaturated fatty acids inhibit the expression of the glucose-6-phosphate dehydrogenase gene in primary rat hepatocytes by a nuclear posttranscriptional mechanism. J. Lipid Res. 39, 1951-1963
    • (1998) J. Lipid Res. , vol.39 , pp. 1951-1963
    • Stabile, L.P.1    Klautky, S.A.2    Minor, S.M.3    Salati, L.M.4
  • 17
    • 0021100690 scopus 로고
    • Accurate transcription initiation byRNApolymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., Lebovitz, R. M., and Roeder, R. G. (1983) Accurate transcription initiation byRNApolymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 18
    • 0020548847 scopus 로고
    • Two promoters of different strengths control the transcription of the mouse alpha-amylase gene Amy-1a in the parotid gland and the liver
    • Schibler, U., Hagenbüchle, O., Wellauer, P. K., and Pittet, A. C. (1983) Two promoters of different strengths control the transcription of the mouse alpha-amylase gene Amy-1a in the parotid gland and the liver. Cell 33, 501-508
    • (1983) Cell , vol.33 , pp. 501-508
    • Schibler, U.1    Hagenbüchle, O.2    Wellauer, P.K.3    Pittet, A.C.4
  • 19
    • 33845998944 scopus 로고    scopus 로고
    • Identification of hnRNPs K, L and A2/B1 as candidate proteins involved in the nutritional regulation of mRNA splicing
    • Griffith, B. N., Walsh, C. M., Szeszel-Fedorowicz, W., Timperman, A. T., and Salati, L. M. (2006) Identification of hnRNPs K, L and A2/B1 as candidate proteins involved in the nutritional regulation of mRNA splicing. Biochim. Biophys. Acta 1759, 552-561
    • (2006) Biochim. Biophys. Acta , vol.1759 , pp. 552-561
    • Griffith, B.N.1    Walsh, C.M.2    Szeszel-Fedorowicz, W.3    Timperman, A.T.4    Salati, L.M.5
  • 21
    • 30044445758 scopus 로고    scopus 로고
    • Role of CCAAT/enhancer-binding protein, histone acetylation, and coactivator recruitment in the regulation of malic enzyme transcription by thyroid hormone
    • Yin, L., Wang, Y., Dridi, S., Vinson, C., and Hillgartner, F. B. (2005) Role of CCAAT/enhancer-binding protein, histone acetylation, and coactivator recruitment in the regulation of malic enzyme transcription by thyroid hormone. Mol. Cell. Endocrinol. 245, 43-52
    • (2005) Mol. Cell. Endocrinol. , vol.245 , pp. 43-52
    • Yin, L.1    Wang, Y.2    Dridi, S.3    Vinson, C.4    Hillgartner, F.B.5
  • 22
    • 0035881472 scopus 로고    scopus 로고
    • Binding of c-Myc to chromatin mediates mitogen-induced acetylation of histone H4 and gene activation
    • Frank, S. R., Schroeder, M., Fernandez, P., Taubert, S., and Amati, B. (2001) Binding of c-Myc to chromatin mediates mitogen-induced acetylation of histone H4 and gene activation. Genes Dev. 15, 2069-2082
    • (2001) Genes Dev. , vol.15 , pp. 2069-2082
    • Frank, S.R.1    Schroeder, M.2    Fernandez, P.3    Taubert, S.4    Amati, B.5
  • 23
    • 34548169696 scopus 로고    scopus 로고
    • Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions
    • Hellman, L. M., and Fried, M. G. (2007) Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions. Nat. Protoc. 2, 1849-1861
    • (2007) Nat. Protoc. , vol.2 , pp. 1849-1861
    • Hellman, L.M.1    Fried, M.G.2
  • 24
    • 79957586580 scopus 로고    scopus 로고
    • A disease-associated polymorphism alters splicing of the human CD45 phosphatase gene by disrupting combinatorial repression by heterogeneous nuclear ribonucleoproteins (hnRNPs)
    • Motta-Mena, L. B., Smith, S. A., Mallory, M. J., Jackson, J., Wang, J., and Lynch, K. W. (2011) A disease-associated polymorphism alters splicing of the human CD45 phosphatase gene by disrupting combinatorial repression by heterogeneous nuclear ribonucleoproteins (hnRNPs). J. Biol. Chem. 286, 20043-20053
    • (2011) J. Biol. Chem. , vol.286 , pp. 20043-20053
    • Motta-Mena, L.B.1    Smith, S.A.2    Mallory, M.J.3    Jackson, J.4    Wang, J.5    Lynch, K.W.6
  • 25
    • 0032679323 scopus 로고    scopus 로고
    • Measuring equilibrium and kinetic constants using gel retardation assays
    • Setzer, D. R. (1999) Measuring equilibrium and kinetic constants using gel retardation assays. Methods Mol. Biol. 118, 115-128
    • (1999) Methods Mol. Biol. , vol.118 , pp. 115-128
    • Setzer, D.R.1
  • 27
    • 27944508215 scopus 로고    scopus 로고
    • CLIP. A method for identifying protein-RNA interaction sites in living cells
    • Ule, J., Jensen, K., Mele, A., and Darnell, R. B. (2005) CLIP. A method for identifying protein-RNA interaction sites in living cells. Methods 37, 376-386
    • (2005) Methods , vol.37 , pp. 376-386
    • Ule, J.1    Jensen, K.2    Mele, A.3    Darnell, R.B.4
  • 28
    • 0037387122 scopus 로고    scopus 로고
    • ICP27 interacts with SRPK1 to mediate HSV splicing inhibition by altering SR protein phosphorylation
    • Sciabica, K. S., Dai, Q. J., and Sandri-Goldin, R. M. (2003) ICP27 interacts with SRPK1 to mediate HSV splicing inhibition by altering SR protein phosphorylation. EMBO J. 22, 1608-1619
    • (2003) EMBO J. , vol.22 , pp. 1608-1619
    • Sciabica, K.S.1    Dai, Q.J.2    Sandri-Goldin, R.M.3
  • 29
    • 0028855519 scopus 로고
    • Physiological and molecular mechanisms involved in nutritional regulation of fatty acid synthesis
    • Hillgartner, F. B., Salati, L. M., and Goodridge, A. G. (1995) Physiological and molecular mechanisms involved in nutritional regulation of fatty acid synthesis. Physiol. Rev. 75, 47-76
    • (1995) Physiol. Rev. , vol.75 , pp. 47-76
    • Hillgartner, F.B.1    Salati, L.M.2    Goodridge, A.G.3
  • 30
    • 42449089029 scopus 로고    scopus 로고
    • Coupling transcription and alternative splicing
    • Kornblihtt, A. R. (2007) Coupling transcription and alternative splicing. Adv. Exp. Med. Biol. 623, 175-189
    • (2007) Adv. Exp. Med. Biol. , vol.623 , pp. 175-189
    • Kornblihtt, A.R.1
  • 31
    • 33748351186 scopus 로고    scopus 로고
    • Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells
    • Listerman, I., Sapra, A. K., and Neugebauer, K. M. (2006) Cotranscriptional coupling of splicing factor recruitment and precursor messenger RNA splicing in mammalian cells. Nat. Struct. Mol. Biol. 13, 815-822
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 815-822
    • Listerman, I.1    Sapra, A.K.2    Neugebauer, K.M.3
  • 32
    • 12244297083 scopus 로고    scopus 로고
    • The distribution of RNA polymerase II largest subunit (RPB1) in the Xenopus germinal vesicle
    • Doyle, O., Corden, J. L., Murphy, C., and Gall, J. G. (2002) The distribution of RNA polymerase II largest subunit (RPB1) in the Xenopus germinal vesicle. J. Struct. Biol. 140, 154-166
    • (2002) J. Struct. Biol. , vol.140 , pp. 154-166
    • Doyle, O.1    Corden, J.L.2    Murphy, C.3    Gall, J.G.4
  • 33
    • 0029050868 scopus 로고
    • Aconserved epitope on a subset of SR proteins defines a larger family of pre-mRNA splicing factors
    • Neugebauer, K. M., Stolk, J. A., and Roth, M. B. (1995)Aconserved epitope on a subset of SR proteins defines a larger family of pre-mRNA splicing factors. J. Cell Biol. 129, 899-908
    • (1995) J. Cell Biol. , vol.129 , pp. 899-908
    • Neugebauer, K.M.1    Stolk, J.A.2    Roth, M.B.3
  • 35
    • 0035025061 scopus 로고    scopus 로고
    • Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA
    • Huang, Y., and Steitz, J. A. (2001) Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA. Mol. Cell 7, 899-905
    • (2001) Mol. Cell , vol.7 , pp. 899-905
    • Huang, Y.1    Steitz, J.A.2
  • 36
    • 59249087922 scopus 로고    scopus 로고
    • SRp20 and CUG-BP1 modulate insulin receptor exon 11 alternative splicing
    • Sen, S., Talukdar, I., and Webster, N. J. (2009) SRp20 and CUG-BP1 modulate insulin receptor exon 11 alternative splicing. Mol. Cell. Biol. 29, 871-880
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 871-880
    • Sen, S.1    Talukdar, I.2    Webster, N.J.3
  • 38
    • 0033019048 scopus 로고    scopus 로고
    • Selection and characterization of pre-mRNA splicing enhancers. Identification of novel SR protein-specific enhancer sequences
    • Schaal, T. D., and Maniatis, T. (1999) Selection and characterization of pre-mRNA splicing enhancers. Identification of novel SR protein-specific enhancer sequences. Mol. Cell. Biol. 19, 1705-1719
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1705-1719
    • Schaal, T.D.1    Maniatis, T.2
  • 39
    • 0034599949 scopus 로고    scopus 로고
    • Functional characterization of SR and SR-related genes in Caenorhabditis elegans
    • Longman, D., Johnstone, I. L., and Cáceres, J. F. (2000) Functional characterization of SR and SR-related genes in Caenorhabditis elegans. EMBO J. 19, 1625-1637
    • (2000) EMBO J. , vol.19 , pp. 1625-1637
    • Longman, D.1    Johnstone, I.L.2    Cáceres, J.F.3
  • 40
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao, S. H., and Manley, J. L. (1997) Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev. 11, 334-344
    • (1997) Genes Dev. , vol.11 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 41
    • 0344654761 scopus 로고    scopus 로고
    • Phosphorylation regulates in vivo interaction and molecular targeting of serine/arginine-rich pre-mRNA splicing factors
    • Yeakley, J. M., Tronchère, H., Olesen, J., Dyck, J. A., Wang, H. Y., and Fu, X. D. (1999) Phosphorylation regulates in vivo interaction and molecular targeting of serine/arginine-rich pre-mRNA splicing factors. J. Cell Biol. 145, 447-455
    • (1999) J. Cell Biol. , vol.145 , pp. 447-455
    • Yeakley, J.M.1    Tronchère, H.2    Olesen, J.3    Dyck, J.A.4    Wang, H.Y.5    Fu, X.D.6
  • 42
    • 33845715579 scopus 로고    scopus 로고
    • SAP155 Binds to ceramide-responsive RNA cis-element 1 and regulates the alternative 5' splice site selection of Bcl-x pre-mRNA
    • Massiello, A., Roesser, J. R., and Chalfant, C. E. (2006) SAP155 Binds to ceramide-responsive RNA cis-element 1 and regulates the alternative 5' splice site selection of Bcl-x pre-mRNA. FASEB J. 20, 1680-1682
    • (2006) FASEB J. , vol.20 , pp. 1680-1682
    • Massiello, A.1    Roesser, J.R.2    Chalfant, C.E.3
  • 43
    • 45249091505 scopus 로고    scopus 로고
    • Substances that can change alternative splice-site selection
    • Sumanasekera, C., Watt, D. S., and Stamm, S. (2008) Substances that can change alternative splice-site selection. Biochem. Soc. Trans. 36, 483-490
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 483-490
    • Sumanasekera, C.1    Watt, D.S.2    Stamm, S.3
  • 44
    • 61649125623 scopus 로고    scopus 로고
    • Global analysis of alternative splicing regulation by insulin and wingless signaling in Drosophila cells
    • Hartmann, B., Castelo, R., Blanchette, M., Boue, S., Rio, D. C., and Valcárcel, J. (2009) Global analysis of alternative splicing regulation by insulin and wingless signaling in Drosophila cells. Genome Biol. 10, R11
    • (2009) Genome Biol , vol.10
    • Hartmann, B.1    Castelo, R.2    Blanchette, M.3    Boue, S.4    Rio, D.C.5    Valcárcel, J.6
  • 46
    • 0031985121 scopus 로고    scopus 로고
    • Insulin regulates protein kinase CδII expression through enhanced exon inclusion in L6 skeletal muscle cells. A novel mechanism of insulin- and insulin-like growth factor- I-induced 5' splice site selection
    • Chalfant, C. E., Watson, J. E., Bisnauth, L. D., Kang, J. B., Patel, N., Obeid, L. M., Eichler, D. C., and Cooper, D. R. (1998) Insulin regulates protein kinase CδII expression through enhanced exon inclusion in L6 skeletal muscle cells. A novel mechanism of insulin- and insulin-like growth factor- I-induced 5' splice site selection. J. Biol. Chem. 273, 910-916
    • (1998) J. Biol. Chem. , vol.273 , pp. 910-916
    • Chalfant, C.E.1    Watson, J.E.2    Bisnauth, L.D.3    Kang, J.B.4    Patel, N.5    Obeid, L.M.6    Eichler, D.C.7    Cooper, D.R.8
  • 47
    • 28844478772 scopus 로고    scopus 로고
    • Arachidonic acid inhibits the insulin induction of glucose-6-phosphate dehydrogenase via p38 MAP kinase
    • Talukdar, I., Szeszel-Fedorowicz, W., and Salati, L. M. (2005) Arachidonic acid inhibits the insulin induction of glucose-6-phosphate dehydrogenase via p38 MAP kinase. J. Biol. Chem. 280, 40660-40667
    • (2005) J. Biol. Chem. , vol.280 , pp. 40660-40667
    • Talukdar, I.1    Szeszel-Fedorowicz, W.2    Salati, L.M.3
  • 48
    • 0037044763 scopus 로고    scopus 로고
    • Acute activation of de novo sphingolipid biosynthesis upon heat shock causes an accumulation of ceramide and subsequent dephosphorylation of SR proteins
    • Jenkins, G. M., Cowart, L. A., Signorelli, P., Pettus, B. J., Chalfant, C. E., and Hannun, Y. A. (2002) Acute activation of de novo sphingolipid biosynthesis upon heat shock causes an accumulation of ceramide and subsequent dephosphorylation of SR proteins. J. Biol. Chem. 277, 42572-42578
    • (2002) J. Biol. Chem. , vol.277 , pp. 42572-42578
    • Jenkins, G.M.1    Cowart, L.A.2    Signorelli, P.3    Pettus, B.J.4    Chalfant, C.E.5    Hannun, Y.A.6
  • 49
    • 0028070326 scopus 로고
    • Identification of arachidonic acid as a mediator of sphingomyelin hydrolysis in response to tumor necrosis factor α
    • Jayadev, S., Linardic, C. M., and Hannun, Y. A. (1994) Identification of arachidonic acid as a mediator of sphingomyelin hydrolysis in response to tumor necrosis factor α. J. Biol. Chem. 269, 5757-5763
    • (1994) J. Biol. Chem. , vol.269 , pp. 5757-5763
    • Jayadev, S.1    Linardic, C.M.2    Hannun, Y.A.3
  • 50
    • 77955416143 scopus 로고    scopus 로고
    • Global analysis reveals SRp20- and SRp75-specific mRNPs in cycling and neural cells
    • Ankö, M. L., Morales, L., Henry, I., Beyer, A., and Neugebauer, K. M. (2010) Global analysis reveals SRp20- and SRp75-specific mRNPs in cycling and neural cells. Nat. Struct. Mol. Biol. 17, 962-970
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 962-970
    • Ankö, M.L.1    Morales, L.2    Henry, I.3    Beyer, A.4    Neugebauer, K.M.5


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