메뉴 건너뛰기




Volumn 587, Issue 15, 2013, Pages 2319-2324

Insulin receptor substrate-1 (IRS-1) forms a ribonucleoprotein complex associated with polysomes

Author keywords

Insulin receptor substrate; Insulin like growth factor I (IGF I); RNA; Translation

Indexed keywords

INSULIN RECEPTOR SUBSTRATE 1; MESSENGER RNA; RIBONUCLEASE; RIBONUCLEOPROTEIN;

EID: 84880703130     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.05.066     Document Type: Article
Times cited : (11)

References (36)
  • 1
    • 78650310616 scopus 로고    scopus 로고
    • Growth hormone, the insulin-like growth factor axis, insulin and cancer risk
    • P.E. Clayton, I. Banerjee, P.G. Murray, and A.G. Renehan Growth hormone, the insulin-like growth factor axis, insulin and cancer risk Nat. Rev. Endocrinol. 7 2010 11 24
    • (2010) Nat. Rev. Endocrinol. , vol.7 , pp. 11-24
    • Clayton, P.E.1    Banerjee, I.2    Murray, P.G.3    Renehan, A.G.4
  • 2
    • 84866122780 scopus 로고    scopus 로고
    • Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2
    • K.D. Copps, and M.F. White Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2 Diabetologia 55 2012 2565 2582
    • (2012) Diabetologia , vol.55 , pp. 2565-2582
    • Copps, K.D.1    White, M.F.2
  • 4
    • 0029148591 scopus 로고
    • Role of IRS-2 in insulin and cytokine signalling
    • X.J. Sun Role of IRS-2 in insulin and cytokine signalling Nature 377 1995 173 177
    • (1995) Nature , vol.377 , pp. 173-177
    • Sun, X.J.1
  • 5
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • J.A. Engelman, J. Luo, and L.C. Cantley The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism Nat. Rev. Genet. 7 2006 606 619
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.2    Cantley, L.C.3
  • 6
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • S. Wullschleger, R. Loewith, and M.N. Hall TOR signaling in growth and metabolism Cell 124 2006 471 484
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 7
    • 78751639015 scopus 로고    scopus 로고
    • Insulin receptor substrates form high-molecular-mass complexes that modulate their availability to insulin/insulin-like growth factor-I receptor tyrosine kinases
    • T. Fukushima Insulin receptor substrates form high-molecular-mass complexes that modulate their availability to insulin/insulin-like growth factor-I receptor tyrosine kinases Biochem. Biophys. Res. Commun. 404 2010 767 773
    • (2010) Biochem. Biophys. Res. Commun. , vol.404 , pp. 767-773
    • Fukushima, T.1
  • 8
    • 38049144506 scopus 로고    scopus 로고
    • 53BP2S, interacting with insulin receptor substrates, modulates insulin signaling
    • F. Hakuno, S. Kurihara, R.T. Watson, J.E. Pessin, and S. Takahashi 53BP2S, interacting with insulin receptor substrates, modulates insulin signaling J. Biol. Chem. 282 2007 37747 37758
    • (2007) J. Biol. Chem. , vol.282 , pp. 37747-37758
    • Hakuno, F.1    Kurihara, S.2    Watson, R.T.3    Pessin, J.E.4    Takahashi, S.5
  • 9
    • 84860388987 scopus 로고    scopus 로고
    • HSP90 interacting with IRS-2 is involved in cAMP-dependent potentiation of IGF-I signals in FRTL-5 cells
    • T. Fukushima HSP90 interacting with IRS-2 is involved in cAMP-dependent potentiation of IGF-I signals in FRTL-5 cells Mol. Cell. Endocrinol. 344 2011 81 89
    • (2011) Mol. Cell. Endocrinol. , vol.344 , pp. 81-89
    • Fukushima, T.1
  • 10
    • 84862696018 scopus 로고    scopus 로고
    • Insulin/insulin-like growth factor (IGF) stimulation abrogates an association between a deubiquitinating enzyme USP7 and insulin receptor substrates (IRSs) followed by proteasomal degradation of IRSs
    • H. Yoshihara Insulin/insulin-like growth factor (IGF) stimulation abrogates an association between a deubiquitinating enzyme USP7 and insulin receptor substrates (IRSs) followed by proteasomal degradation of IRSs Biochem. Biophys. Res. Commun. 423 2012 122 127
    • (2012) Biochem. Biophys. Res. Commun. , vol.423 , pp. 122-127
    • Yoshihara, H.1
  • 11
    • 0034595315 scopus 로고    scopus 로고
    • Binding of IRS proteins to calmodulin is enhanced in insulin resistance
    • Z. Li, J.L. Joyal, and D.B. Sacks Binding of IRS proteins to calmodulin is enhanced in insulin resistance Biochemistry 39 2000 5089 5096
    • (2000) Biochemistry , vol.39 , pp. 5089-5096
    • Li, Z.1    Joyal, J.L.2    Sacks, D.B.3
  • 12
    • 0034704113 scopus 로고    scopus 로고
    • Cloning and characterization of PHIP, a novel insulin receptor substrate-1 pleckstrin homology domain interacting protein
    • J. Farhang-Fallah, X. Yin, G. Trentin, A.M. Cheng, and M. Rozakis-Adcock Cloning and characterization of PHIP, a novel insulin receptor substrate-1 pleckstrin homology domain interacting protein J. Biol. Chem. 275 2000 40492 40497
    • (2000) J. Biol. Chem. , vol.275 , pp. 40492-40497
    • Farhang-Fallah, J.1    Yin, X.2    Trentin, G.3    Cheng, A.M.4    Rozakis-Adcock, M.5
  • 13
    • 17744404883 scopus 로고    scopus 로고
    • Association of insulin receptor substrate proteins with Bcl-2 and their effects on its phosphorylation and antiapoptotic function
    • H. Ueno Association of insulin receptor substrate proteins with Bcl-2 and their effects on its phosphorylation and antiapoptotic function Mol. Biol. Cell 11 2000 735 746
    • (2000) Mol. Biol. Cell , vol.11 , pp. 735-746
    • Ueno, H.1
  • 14
    • 0032491399 scopus 로고    scopus 로고
    • Interaction of insulin receptor substrate-1 with the sigma3A subunit of the adaptor protein complex-3 in cultured adipocytes
    • B. VanRenterghem, M. Morin, M.P. Czech, and R.A. Heller-Harrison Interaction of insulin receptor substrate-1 with the sigma3A subunit of the adaptor protein complex-3 in cultured adipocytes J. Biol. Chem. 273 1998 29942 29949
    • (1998) J. Biol. Chem. , vol.273 , pp. 29942-29949
    • Vanrenterghem, B.1    Morin, M.2    Czech, M.P.3    Heller-Harrison, R.A.4
  • 15
    • 15444344415 scopus 로고    scopus 로고
    • 14-3-3 Protein binds to insulin receptor substrate-1, one of the binding sites of which is in the phosphotyrosine binding domain
    • T. Ogihara 14-3-3 Protein binds to insulin receptor substrate-1, one of the binding sites of which is in the phosphotyrosine binding domain J. Biol. Chem. 272 1997 25267 25274
    • (1997) J. Biol. Chem. , vol.272 , pp. 25267-25274
    • Ogihara, T.1
  • 17
    • 0028024251 scopus 로고
    • Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap binding protein
    • N. Kataoka, M. Ohno, K. Kangawa, Y. Tokoro, and Y. Shimura Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap binding protein Nucleic Acids Res. 22 1994 3861 3865
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3861-3865
    • Kataoka, N.1    Ohno, M.2    Kangawa, K.3    Tokoro, Y.4    Shimura, Y.5
  • 18
    • 2342540912 scopus 로고    scopus 로고
    • The ever-increasing complexities of the exon junction complex
    • T.O. Tange, A. Nott, and M.J. Moore The ever-increasing complexities of the exon junction complex Curr. Opin. Cell Biol. 16 2004 279 284
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 279-284
    • Tange, T.O.1    Nott, A.2    Moore, M.J.3
  • 19
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • H. Le Hir, E. Izaurralde, L.E. Maquat, and M.J. Moore The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions EMBO J. 19 2000 6860 6869
    • (2000) EMBO J. , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 20
    • 0033634824 scopus 로고    scopus 로고
    • Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm
    • N. Kataoka, J. Yong, V.N. Kim, F. Velazquez, R.A. Perkinson, F. Wang, and G. Dreyfuss Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm Mol. Cell 6 2000 673 682
    • (2000) Mol. Cell , vol.6 , pp. 673-682
    • Kataoka, N.1    Yong, J.2    Kim, V.N.3    Velazquez, F.4    Perkinson, R.A.5    Wang, F.6    Dreyfuss, G.7
  • 21
    • 0035890258 scopus 로고    scopus 로고
    • Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex
    • N. Kataoka, M.D. Diem, V.N. Kim, J. Yong, and G. Dreyfuss Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex EMBO J. 20 2001 6424 6433
    • (2001) EMBO J. , vol.20 , pp. 6424-6433
    • Kataoka, N.1    Diem, M.D.2    Kim, V.N.3    Yong, J.4    Dreyfuss, G.5
  • 22
    • 0035801373 scopus 로고    scopus 로고
    • The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay
    • H. Le Hir, D. Gatfield, E. Izaurralde, and M.J. Moore The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay EMBO J. 20 2001 4987 4997
    • (2001) EMBO J. , vol.20 , pp. 4987-4997
    • Le Hir, H.1    Gatfield, D.2    Izaurralde, E.3    Moore, M.J.4
  • 23
    • 0036645697 scopus 로고    scopus 로고
    • The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling
    • F. Lejeune, Y. Ishigaki, X. Li, and L.E. Maquat The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling EMBO J. 21 2002 3536 3545
    • (2002) EMBO J. , vol.21 , pp. 3536-3545
    • Lejeune, F.1    Ishigaki, Y.2    Li, X.3    Maquat, L.E.4
  • 24
    • 0037046798 scopus 로고    scopus 로고
    • Translation is required to remove Y14 from mRNAs in the cytoplasm
    • J. Dostie, and G. Dreyfuss Translation is required to remove Y14 from mRNAs in the cytoplasm Curr. Biol. 12 2002 1060 1067
    • (2002) Curr. Biol. , vol.12 , pp. 1060-1067
    • Dostie, J.1    Dreyfuss, G.2
  • 25
    • 1842682946 scopus 로고    scopus 로고
    • The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex
    • S.Y. Chiu, F. Lejeune, A.C. Ranganathan, and L.E. Maquat The pioneer translation initiation complex is functionally distinct from but structurally overlaps with the steady-state translation initiation complex Genes Dev. 18 2004 745 754
    • (2004) Genes Dev. , vol.18 , pp. 745-754
    • Chiu, S.Y.1    Lejeune, F.2    Ranganathan, A.C.3    Maquat, L.E.4
  • 26
    • 0022766180 scopus 로고
    • MRNA polyadenylate-binding protein: Gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence
    • S.A. Adam, T. Nakagawa, M.S. Swanson, T.K. Woodruff, and G. Dreyfuss MRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence Mol. Cell. Biol. 6 1986 2932 2943
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2932-2943
    • Adam, S.A.1    Nakagawa, T.2    Swanson, M.S.3    Woodruff, T.K.4    Dreyfuss, G.5
  • 27
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • X.M. Ma, and J. Blenis Molecular mechanisms of mTOR-mediated translational control Nat. Rev. Mol. Cell Biol. 10 2009 307 318
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 28
    • 0032834055 scopus 로고    scopus 로고
    • EIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • A.C. Gingras, B. Raught, and N. Sonenberg EIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation Annu. Rev. Biochem. 68 1999 913 963
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 29
    • 0030952218 scopus 로고    scopus 로고
    • Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity
    • H. Le, R.L. Tanguay, M.L. Balasta, C.C. Wei, K.S. Browning, A.M. Metz, D.J. Goss, and D.R. Gallie Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity J. Biol. Chem. 272 1997 16247 16255
    • (1997) J. Biol. Chem. , vol.272 , pp. 16247-16255
    • Le, H.1    Tanguay, R.L.2    Balasta, M.L.3    Wei, C.C.4    Browning, K.S.5    Metz, A.M.6    Goss, D.J.7    Gallie, D.R.8
  • 30
    • 84861208388 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-binding protein, PI3KAP/XB130, is required for cAMP-induced amplification of IGF mitogenic activity in FRTL-5 thyroid cells
    • D. Yamanaka Phosphatidylinositol 3-kinase-binding protein, PI3KAP/XB130, is required for cAMP-induced amplification of IGF mitogenic activity in FRTL-5 thyroid cells Mol. Endocrinol. 26 2012 1043 1055
    • (2012) Mol. Endocrinol. , vol.26 , pp. 1043-1055
    • Yamanaka, D.1
  • 31
    • 11844281461 scopus 로고    scopus 로고
    • Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms
    • A. Kahvejian, Y.V. Svitkin, R. Sukarieh, M.N. M'Boutchou, and N. Sonenberg Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms Genes Dev. 19 2005 104 113
    • (2005) Genes Dev. , vol.19 , pp. 104-113
    • Kahvejian, A.1    Svitkin, Y.V.2    Sukarieh, R.3    M'Boutchou, M.N.4    Sonenberg, N.5
  • 33
    • 0032520009 scopus 로고    scopus 로고
    • 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway
    • A.C. Gingras, S.G. Kennedy, M.A. O'Leary, N. Sonenberg, and N. Hay 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway Genes Dev. 12 1998 502 513
    • (1998) Genes Dev. , vol.12 , pp. 502-513
    • Gingras, A.C.1    Kennedy, S.G.2    O'Leary, M.A.3    Sonenberg, N.4    Hay, N.5
  • 34
    • 0031803329 scopus 로고    scopus 로고
    • Insulin receptor substrate-2 amino acid polymorphisms are not associated with random type 2 diabetes among Caucasians
    • D. Bernal, K. Almind, L. Yenush, M. Ayoub, Y. Zhang, L. Rosshani, C. Larsson, O. Pedersen, and M.F. White Insulin receptor substrate-2 amino acid polymorphisms are not associated with random type 2 diabetes among Caucasians Diabetes 47 1998 976 979
    • (1998) Diabetes , vol.47 , pp. 976-979
    • Bernal, D.1    Almind, K.2    Yenush, L.3    Ayoub, M.4    Zhang, Y.5    Rosshani, L.6    Larsson, C.7    Pedersen, O.8    White, M.F.9
  • 35
    • 84862543951 scopus 로고    scopus 로고
    • From signal transduction to signal interpretation: An alternative model for the molecular function of insulin receptor substrates
    • S. Boller, B.A. Joblin, L. Xu, F. Item, T. Trub, N. Boschetti, G.A. Spinas, and M. Niessen From signal transduction to signal interpretation: an alternative model for the molecular function of insulin receptor substrates Arch. Physiol. Biochem. 118 2012 148 155
    • (2012) Arch. Physiol. Biochem. , vol.118 , pp. 148-155
    • Boller, S.1    Joblin, B.A.2    Xu, L.3    Item, F.4    Trub, T.5    Boschetti, N.6    Spinas, G.A.7    Niessen, M.8
  • 36
    • 84878965414 scopus 로고    scopus 로고
    • The AP-1 complex regulates intracellular localization of insulin receptor substrate 1, which is required for insulin-like growth factor i-dependent cell proliferation
    • Y. Yoneyama, M. Matsuo, K. Take, T. Kabuta, K. Chida, F. Hakuno, and S.-I. Takahashi The AP-1 complex regulates intracellular localization of insulin receptor substrate 1, which is required for insulin-like growth factor i-dependent cell proliferation Mol. Cell. Biol. 33 2013 1991 2003
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 1991-2003
    • Yoneyama, Y.1    Matsuo, M.2    Take, K.3    Kabuta, T.4    Chida, K.5    Hakuno, F.6    Takahashi, S.-I.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.