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Volumn 27, Issue 16, 2013, Pages 1809-1820

A new role for the cellular PABP repressor Paip2 as an innate restriction factor capable of limiting productive cytomegalovirus replication

Author keywords

HCMV replication; Innate defense; mTORC1; PABP; Paip2; Translation control

Indexed keywords

MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN; PROTEIN EDD1; PROTEIN PAIP2; PROTEIN UL38; TRANSLATION INITIATION FACTOR EIF4F; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84882593141     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.221341.113     Document Type: Article
Times cited : (18)

References (45)
  • 1
    • 77249151465 scopus 로고    scopus 로고
    • Human cytomeglovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4E-BP1
    • Aoyagi M., Gaspar M, Shenk T. 2010. Human cytomeglovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4E-BP1. Proc Natl Acad Sci 107: 2640-2645.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 2640-2645
    • Aoyagi, M.1    Gaspar, M.2    Shenk, T.3
  • 2
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP1 enhances translation
    • Craig A.W., Haghighat A, Yu AT, Sonenberg N. 1998. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP1 enhances translation. Nature 392: 520-523.
    • (1998) Nature , vol.392 , pp. 520-523
    • Craig, A.W.1    Haghighat, A.2    Yu, A.T.3    Sonenberg, N.4
  • 6
    • 0036140217 scopus 로고    scopus 로고
    • Characterization of a human cytomegalovirus with phosphorylation site mutations in the immediate-early 2 protein
    • Heider J.A., Yu Y, Shenk T, Alwine JC. 2002. Characterization of a human cytomegalovirus with phosphorylation site mutations in the immediate-early 2 protein. J Virol 76: 928-932.
    • (2002) J Virol , vol.76 , pp. 928-932
    • Heider, J.A.1    Yu, Y.2    Shenk, T.3    Alwine, J.C.4
  • 7
    • 0033556419 scopus 로고    scopus 로고
    • The expression of the poly(A)-binding protein gene is trans-lationally regulated in a growth-dependent fashion through a 59terminal oligopyrimidine tract motif
    • Hornstein E., Git A, Braunstein I, Avni D, Meyuhas O. 1999a. The expression of the poly(A)-binding protein gene is trans-lationally regulated in a growth-dependent fashion through a 59terminal oligopyrimidine tract motif. J Biol Chem 274: 1708-1714.
    • (1999) J Biol Chem , vol.274 , pp. 1708-1714
    • Hornstein, E.1    Git, A.2    Braunstein, I.3    Avni, D.4    Meyuhas, O.5
  • 8
    • 0032772533 scopus 로고    scopus 로고
    • Overexpression of poly(A)-binding protein down-regulates the translation or the abundance of its own mRNA
    • Hornstein E., Harel H, Levy G, Meyuhas O. 1999b. Overexpression of poly(A)-binding protein down-regulates the translation or the abundance of its own mRNA. FEBS Lett 457: 209-213.
    • (1999) FEBS Lett , vol.457 , pp. 209-213
    • Hornstein, E.1    Harel, H.2    Levy, G.3    Meyuhas, O.4
  • 9
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • Isler J.A., Skalet AH, Alwine JC. 2005. Human cytomegalovirus infection activates and regulates the unfolded protein response. J Virol 79: 6890-6899.
    • (2005) J Virol , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 10
    • 75149196287 scopus 로고    scopus 로고
    • The mechanisms of eukaryotic translation initiation and principles of its regulation
    • Jackson R.J., Hellen CUT, Pestova TV. 2010. The mechanisms of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 10: 113-127.
    • (2010) Nat Rev Mol Cell Biol , vol.10 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.T.2    Pestova, T.V.3
  • 11
    • 0035787721 scopus 로고    scopus 로고
    • The mRNA closedloop model: The function of PABP and PABP-interacting proteins in mRNA translation
    • Kahvejian A., Roy G, Sonenberg N. 2001. The mRNA closedloop model: The function of PABP and PABP-interacting proteins in mRNA translation. Cold Spring Harb Symp Quant Biol 66: 293-300.
    • (2001) Cold Spring Harb Symp Quant Biol , vol.66 , pp. 293-300
    • Kahvejian, A.1    Roy, G.2    Sonenberg, N.3
  • 12
    • 11844281461 scopus 로고    scopus 로고
    • Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms
    • Kahvejian A., Svitkin YV, Sukarieh R, M'Boutchou M, Sonenberg N. 2005. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev 19: 104-113.
    • (2005) Genes Dev , vol.19 , pp. 104-113
    • Kahvejian, A.1    Svitkin, Y.V.2    Sukarieh, R.3    M'Boutchou, M.4    Sonenberg, N.5
  • 13
    • 33745450501 scopus 로고    scopus 로고
    • A mechanism of translational repression by competition of Paip2 with eIF4G for poly(A) binding protein (PABP) binding
    • Karim M.M., Svitkin YV, Kahvejian A, De Cerscenzo G, Costa-Mattiolo M., Sonenberg N. 2006. A mechanism of translational repression by competition of Paip2 with eIF4G for poly(A) binding protein (PABP) binding. Proc Natl Acad Sci 103: 9494-9499.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 9494-9499
    • Karim, M.M.1    Svitkin, Y.V.2    Kahvejian, A.3    de Cerscenzo, G.4    Costa-Mattiolo, M.5    Sonenberg, N.6
  • 17
    • 84864007849 scopus 로고    scopus 로고
    • Control of viral latency in neurons by axonal mTOR signaling and the 4E-BP translation repressor
    • Kobayashi M., Wilson AC, Chao MV, Mohr I. 2012. Control of viral latency in neurons by axonal mTOR signaling and the 4E-BP translation repressor. Genes Dev 14: 1527-1532.
    • (2012) Genes Dev , vol.14 , pp. 1527-1532
    • Kobayashi, M.1    Wilson, A.C.2    Chao, M.V.3    Mohr, I.4
  • 18
    • 4644252994 scopus 로고    scopus 로고
    • Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase
    • Kudchodkar S.B., Yu Y, Maguire TG, Alwine JC. 2004. Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase. J Virol 78: 11030-11039.
    • (2004) J Virol , vol.78 , pp. 11030-11039
    • Kudchodkar, S.B.1    Yu, Y.2    Maguire, T.G.3    Alwine, J.C.4
  • 19
    • 33749040235 scopus 로고    scopus 로고
    • Human cytomegalovirus infection alters the substrate specificities and rapamycin sensitivities of raptor-and rictor-containing complexes
    • Kudchodkar S.B., Yu Y, Maguire TG, Alwine JC. 2006. Human cytomegalovirus infection alters the substrate specificities and rapamycin sensitivities of raptor-and rictor-containing complexes. Proc Natl Acad Sci 103: 14182-14187.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 14182-14187
    • Kudchodkar, S.B.1    Yu, Y.2    Maguire, T.G.3    Alwine, J.C.4
  • 20
    • 0038063499 scopus 로고    scopus 로고
    • Xenopus poly(A) binding protein: Functional domains in RNA binding and protein-protein interaction
    • Kühn U, Pieler T. 1996. Xenopus poly(A) binding protein: Functional domains in RNA binding and protein-protein interaction. J Mol Biol 256: 20-30.
    • (1996) J Mol Biol , vol.256 , pp. 20-30
    • Kühn, U.1    Pieler, T.2
  • 21
    • 84863349204 scopus 로고    scopus 로고
    • Nanopore detachment kinetics of poly(A) binding proteins from RNA molecules reveals the critical role of C-terminus interactions
    • Lin J., Fabian M, Sonenberg N, Meller A. 2012. Nanopore detachment kinetics of poly(A) binding proteins from RNA molecules reveals the critical role of C-terminus interactions. Biophys J 102: 1427-1434.
    • (2012) Biophys J , vol.102 , pp. 1427-1434
    • Lin, J.1    Fabian, M.2    Sonenberg, N.3    Meller, A.4
  • 22
    • 33645641028 scopus 로고    scopus 로고
    • Reduced stability of mitogenactivated protein kinase-2 mRNA and phosphorylation of poly(A)-binding protein (PABP) in cells overexpressing PABP
    • Ma S., Musa T, Bag J. 2006. Reduced stability of mitogenactivated protein kinase-2 mRNA and phosphorylation of poly(A)-binding protein (PABP) in cells overexpressing PABP. J Biol Chem 281: 3145-3156.
    • (2006) J Biol Chem , vol.281 , pp. 3145-3156
    • Ma, S.1    Musa, T.2    Bag, J.3
  • 23
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus D.A., Evans MC, Jacobson A. 2003. Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol. 4: 223.
    • (2003) Genome Biol. , vol.4 , pp. 223
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 25
    • 84859597567 scopus 로고    scopus 로고
    • Poly(A) binding protein abundance regulates eukaryotic translation initiation factor 4F assembly in human cytomegalovirus-infected cells
    • McKinney C, Perez C, Mohr I. 2012. Poly(A) binding protein abundance regulates eukaryotic translation initiation factor 4F assembly in human cytomegalovirus-infected cells. Proc Natl Acad Sci 109: 5627-5632.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 5627-5632
    • McKinney, C.1    Perez, C.2    Mohr, I.3
  • 26
    • 0344012573 scopus 로고    scopus 로고
    • Identification of a C-terminal poly(A)-binding protein (PABP)-PABP interaction domain: Role in cooperative binding to poly (A) and efficient cap distal translational repression
    • Melo E.O., Dhalia R, Martins de Sa C, Standart N, de Melo Neto OP. 2003. Identification of a C-terminal poly(A)-binding protein (PABP)-PABP interaction domain: Role in cooperative binding to poly (A) and efficient cap distal translational repression. J Biol Chem 278: 46357-46368.
    • (2003) J Biol Chem , vol.278 , pp. 46357-46368
    • Melo, E.O.1    Dhalia, R.2    Martins de Sa, C.3    Standart, N.4    de Melo Neto, O.P.5
  • 27
    • 0033761629 scopus 로고    scopus 로고
    • Synthesis of the translational apparatus is regulated at the translational level
    • Meyuhas O. 2000. Synthesis of the translational apparatus is regulated at the translational level. Eur J Biochem 267: 6321-6330.
    • (2000) Eur J Biochem , vol.267 , pp. 6321-6330
    • Meyuhas, O.1
  • 28
    • 84867636500 scopus 로고    scopus 로고
    • Host translation at the nexus of infection and immunity
    • Mohr I., Sonenberg N. 2012. Host translation at the nexus of infection and immunity. Cell Host Microbe 12: 470-483.
    • (2012) Cell Host Microbe , vol.12 , pp. 470-483
    • Mohr, I.1    Sonenberg, N.2
  • 29
    • 41849101685 scopus 로고    scopus 로고
    • Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex
    • Moorman N.J., Cristea IM, Terhune S, Rout MP, Chait BT, Shenk T. 2008. Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex. Cell Host Microbe 3: 253-262.
    • (2008) Cell Host Microbe , vol.3 , pp. 253-262
    • Moorman, N.J.1    Cristea, I.M.2    Terhune, S.3    Rout, M.P.4    Chait, B.T.5    Shenk, T.6
  • 30
    • 31144443606 scopus 로고    scopus 로고
    • The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex
    • Patel G.P., Ma S, Bag J. 2005. The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex. Nucleic Acids Res 33: 7074-7089.
    • (2005) Nucleic Acids Res , vol.33 , pp. 7074-7089
    • Patel, G.P.1    Ma, S.2    Bag, J.3
  • 31
    • 78650074979 scopus 로고    scopus 로고
    • Translational control of cytoplasmic poly(A) binding protein in human cytomegalovirus-infected cells
    • Perez C., McKinney C, Chuluunbaatar U, Mohr I. 2011. Translational control of cytoplasmic poly(A) binding protein in human cytomegalovirus-infected cells. J Virol 85: 156-164.
    • (2011) J Virol , vol.85 , pp. 156-164
    • Perez, C.1    McKinney, C.2    Chuluunbaatar, U.3    Mohr, I.4
  • 32
    • 80052287736 scopus 로고    scopus 로고
    • The human cytomegalovirus protein pUL38 supresses endoplasmic reticulum stress-mediated cell death independently of its ability to induce mTORC1 activation
    • Qian Z., Xuan B, Gualberto N, Yu D. 2011. The human cytomegalovirus protein pUL38 supresses endoplasmic reticulum stress-mediated cell death independently of its ability to induce mTORC1 activation. J Virol 85: 9103-9113.
    • (2011) J Virol , vol.85 , pp. 9103-9113
    • Qian, Z.1    Xuan, B.2    Gualberto, N.3    Yu, D.4
  • 34
    • 0017662652 scopus 로고
    • Synthesis of proteins and glycoproteins in cells infected with human cytomegalovirus
    • Stinski M. 1977. Synthesis of proteins and glycoproteins in cells infected with human cytomegalovirus. J Virol 23: 751-767.
    • (1977) J Virol , vol.23 , pp. 751-767
    • Stinski, M.1
  • 35
    • 0025909411 scopus 로고
    • Expression of the human cytomegalovirus UL36-38 immediate early region during permissive infection
    • Tenney D.J., Colberg-Poley AM. 1991. Expression of the human cytomegalovirus UL36-38 immediate early region during permissive infection. Virology 182: 199-210.
    • (1991) Virology , vol.182 , pp. 199-210
    • Tenney, D.J.1    Colberg-Poley, A.M.2
  • 38
    • 1842831274 scopus 로고    scopus 로고
    • Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells
    • Walsh D., Mohr I. 2004. Phosphorylation of eIF4E by Mnk-1 enhances HSV-1 translation and replication in quiescent cells. Genes Dev 18: 660-672.
    • (2004) Genes Dev , vol.18 , pp. 660-672
    • Walsh, D.1    Mohr, I.2
  • 39
    • 81255160914 scopus 로고    scopus 로고
    • Viral subversion of the host protein synthesis machinery
    • Walsh D., Mohr I. 2011. Viral subversion of the host protein synthesis machinery. Nat Rev Microbiol 9: 860-873.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 860-873
    • Walsh, D.1    Mohr, I.2
  • 40
    • 20744448501 scopus 로고    scopus 로고
    • Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells
    • Walsh D., Perez C, Notary J, Mohr I. 2005. Regulation of the translation initiation factor eIF4F by multiple mechanisms in human cytomegalovirus-infected cells. J Virol 79: 8057-8064.
    • (2005) J Virol , vol.79 , pp. 8057-8064
    • Walsh, D.1    Perez, C.2    Notary, J.3    Mohr, I.4
  • 41
    • 84870757284 scopus 로고    scopus 로고
    • Tinkering with translation: Protein synthesis in virus-infected cells
    • Walsh D., Mathews MB, Mohr I. 2013. Tinkering with translation: Protein synthesis in virus-infected cells. Cold Spring Harb Perspect Biol 5: a012351.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Walsh, D.1    Mathews, M.B.2    Mohr, I.3
  • 42
    • 0030041959 scopus 로고    scopus 로고
    • Overexpression of poly(A) binding protein prevents maturation-specific deadenylation and translational inactivation in Xenopus oocytes
    • Wormington M., Searfoss AM, Hurney CA. 1996. Overexpression of poly(A) binding protein prevents maturation-specific deadenylation and translational inactivation in Xenopus oocytes. EMBO J 15: 900-909.
    • (1996) EMBO J , vol.15 , pp. 900-909
    • Wormington, M.1    Searfoss, A.M.2    Hurney, C.A.3
  • 43
    • 0032545421 scopus 로고    scopus 로고
    • Negative control of the poly(A)-binding protein mRNA translation is mediated by the adenine-rich region of its 59-untranslated region
    • Wu J., Bag J. 1998. Negative control of the poly(A)-binding protein mRNA translation is mediated by the adenine-rich region of its 59-untranslated region. J Biol Chem 273: 34535-34542.
    • (1998) J Biol Chem , vol.273 , pp. 34535-34542
    • Wu, J.1    Bag, J.2
  • 44
    • 77956383157 scopus 로고    scopus 로고
    • The poly(A)-binding protein partner Paip2a controls translation during late spermatogenesis in mice
    • Yanagiya A., Delbes G, Svitkin YV, Robaire B, Sonenberg N. 2010. The poly(A)-binding protein partner Paip2a controls translation during late spermatogenesis in mice. J Clin Invest 120: 3389-3400.
    • (2010) J Clin Invest , vol.120 , pp. 3389-3400
    • Yanagiya, A.1    Delbes, G.2    Svitkin, Y.V.3    Robaire, B.4    Sonenberg, N.5


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