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Cell Growth and Development

The Drosophila Poly(A) Binding Protein-Interacting Protein, dPaip2, Is a Novel Effector of Cell Growth

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Pages 1143-1154 | Received 07 Aug 2003, Accepted 31 Oct 2003, Published online: 27 Mar 2023

REFERENCES

  • Adams, M. D., Celniker S. E., Holt R. A., Evans C. A., Gocayne J. D., Amanatides P. G., Scherer S. E., Li P. W., Hoskins R. A., Galle R. F., George R. A., Lewis S. E., Richards S., Ashburner M., Henderson S. N., et al. 2000. The genome sequence of Drosophila melanogaster. Science 287:2185–2195.
  • Brand, A. H., and Perrimon N.. 1993. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118:401–415.
  • Brasey, A., Lopez-Lastra M., Ohlmann T., Beerens N., Berkhout B., Darlix J. L., and Sonenberg N.. 2003. The leader of human immunodeficiency virus type 1 genomic RNA harbors an internal ribosome entry segment that is active during the G2/M phase of the cell cycle. J. Virol. 77:3939–3949.
  • Britton, J. S., and Edgar B. A.. 1998. Environmental control of the cell cycle in Drosophila: nutrition activates mitotic and endoreplicative cells by distinct mechanisms. Development 125:2149–2158.
  • Britton, J. S., Lockwood W. K., Li L., Cohen S. M., and Edgar B. A.. 2002. Drosophila's insulin/PI3-kinase pathway coordinates cellular metabolism with nutritional conditions. Dev. Cell 2:239–249.
  • Capdevila, J., and Guerrero I.. 1994. Targeted expression of the signaling molecule decapentaplegic induces pattern duplications and growth alterations in Drosophila wings. EMBO J. 13:4459–4468.
  • Chen, B. P., and Hai T.. 1994. Expression vectors for affinity purification and radiolabeling of proteins using Escherichia coli as host. Gene 139:73–75.
  • Craig, A. W., Haghighat A., Yu A. T., and Sonenberg N.. 1998. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392:520–523.
  • Datar, S. A., Jacobs H. W., de la Cruz A. F., Lehner C. F., and Edgar B. A.. 2000. The Drosophila cyclin D-Cdk4 complex promotes cellular growth. EMBO J. 19:4543–4554.
  • Deardorff, J. A., and Sachs A. B.. 1997. Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast poly(A)-binding protein. J. Mol. Biol. 269:67–81.
  • Deo, R. C., Sonenberg N., and Burley S. K.. 2001. X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein. Proc. Natl. Acad. Sci. USA 98:4414–4419.
  • Ellis, M. C., O'Neill E. M., and Rubin G. M.. 1993. Expression of Drosophila glass protein and evidence for negative regulation of its activity in non-neuronal cells by another DNA-binding protein. Development 119:855–865.
  • FlyBase Consortium. 1999. The FlyBase database of the Drosophila Genome Projects and community literature. Nucleic Acids Res. 27:85–88.
  • Freeman, M. 1996. Reiterative use of the EGF receptor triggers differentiation of all cell types in the Drosophila eye. Cell 87:651–660.
  • Gallie, D. R. 1991. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev. 5:2108–2116.
  • Gallie, D. R. 1998. A tale of two termini: a functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation. Gene 216:1–11.
  • Galloni, M., and Edgar B. A.. 1999. Cell-autonomous and non-autonomous growth-defective mutants of Drosophila melanogaster. Development 126:2365–2375.
  • Gingras, A.-C., Raught B., and Sonenberg N.. 1999. eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68:913–963.
  • Gray, N. K., and Wickens M.. 1998. Control of translation initiation in animals. Annu. Rev. Cell Dev. Biol. 14:399–458.
  • Hershey, J. W. B., and Merrick W. C.. 2000. Pathway and mechanism of initiation of protein synthesis, p. 33–88. In Sonenberg N., Hershey J. W. B., and Matthews M. B. (ed.), Translational control of gene expression. Cold Spring Harbor Laboratory Press, New York, N.Y.
  • Iizuka, N., Najita L., Franzusoff A., and Sarnow P.. 1994. Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae. Mol. Cell. Biol. 14:7322–7330.
  • Johnston, L. A., and Gallant P.. 2002. Control of growth and organ size in Drosophila. Bioessays 24:54–64.
  • Johnston, L. A., Prober D. A., Edgar B. A., Eisenman R. N., and Gallant P.. 1999. Drosophila myc regulates cellular growth during development. Cell 98:779–790.
  • Kahvejian, A., Roy G., and Sonenberg N.. 2001. The mRNA closed loop model: the function of PABP and PABP-interacting proteins in mRNA translation. Cold Spring Harbor Symp. Quant. Biol. 66:293–300.
  • Khaleghpour, K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y. V., Imataka H., O'Connor-McCourt M., and Sonenberg N.. 2001. Dual interactions of the translational repressor Paip2 with poly(A) binding protein. Mol. Cell. Biol. 21:5200–5213.
  • Khaleghpour, K., Pyronnet S., Gingras A. C., and Sonenberg N.. 1999. Translational homeostasis: eukaryotic translation initiation factor 4E control of 4E-binding protein 1 and p70 S6 kinase activities. Mol. Cell. Biol. 19:4302–4310.
  • Khaleghpour, K., Svitkin Y. V., Craig A. W., DeMaria C. T., Deo R. C., Burley S. K., and Sonenberg N.. 2001. Translational repression by a novel partner of human poly(A) binding protein, Paip2. Mol. Cell 7:205–216.
  • Kimball, S. R., and Jefferson L. S.. 2000. Regulation of translation initiation in mammalian cells by amino acids, p. 561–579. In Sonenberg N., Hershey J. W. B., and Matthews M. B. (ed.), Translational control of gene expression. Cold Spring Harbor Laboratory Press, New York, N.Y.
  • Kozlov, G., Trempe J. F., Khaleghpour K., Kahvejian A., Ekiel I., and Gehring K.. 2001. Structure and function of the C-terminal PABC domain of human poly(A)-binding protein. Proc. Natl. Acad. Sci. USA 98:4409–4413.
  • Kuhn, U., and Pieler T.. 1996. Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction. J. Mol. Biol. 256:20–30.
  • Lachance, P. E., Miron M., Raught B., Sonenberg N., and Lasko P.. 2002. Phosphorylation of eukaryotic translation initiation factor 4E is critical for growth. Mol. Cell. Biol. 22:1656–1663.
  • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.
  • Lambertsson, A. 1998. The minute genes in Drosophila and their molecular functions. Adv. Genet. 38:69–134.
  • Lasko, P. 2002. Diabetic flies? Using Drosophila melanogaster to understand the causes of monogenic and genetically complex diseases. Clin. Genet. 62:358–367.
  • Lefrère, V., Vincent A., and Amalric F.. 1990. Drosophila melanogaster poly(A)-binding protein: cDNA cloning reveals an unusually long 3′-untranslated region of the mRNA, also present in other eukaryotic species. Gene 96:219–225.
  • Meyer, C. A., Jacobs H. W., Datar S. A., Du W., Edgar B. A., and Lehner C. F.. 2000. Drosophila Cdk4 is required for normal growth and is dispensable for cell cycle progression. EMBO J. 19:4533–4542.
  • Miron, M., and Sonenberg N.. 2001. Regulation of translation via TOR signalling: insights from Drosophila melanogaster. J. Nutr. 131:2988S–2993S.
  • Miron, M., Verdu J., Lachance P. E., Birnbaum M. J., Lasko P. F., and Sonenberg N.. 2001. The translational inhibitor 4E-BP is an effector of PI(3)K/Akt signalling and cell growth in Drosophila. Nat. Cell Biol. 3:596–601.
  • Montagne, J., Stewart M. J., Stocker H., Hafen E., Kozma S. C., and Thomas G.. 1999. Drosophila S6 kinase: a regulator of cell size. Science 285:2126–2129.
  • Munroe, D., and Jacobson A.. 1990. mRNA poly(A) tail, a 3′ enhancer of translational initiation. Mol. Cell. Biol. 10:3441–3455.
  • Neufeld, T. P., de la Cruz A. F., Johnston L. A., and Edgar B. A.. 1998. Coordination of growth and cell division in the Drosophila wing. Cell 93:1183–1193.
  • Polymenis, M., and Schmidt E. V.. 1999. Coordination of cell growth with cell division. Curr. Opin. Genet. Dev. 9:76–80.
  • Rosenwald, I. B., Lazaris-Karatzas A., Sonenberg N., and Schmidt E. V.. 1993. Elevated levels of cyclin D1 protein in response to increased expression of eukaryotic initiation factor 4E. Mol. Cell. Biol. 13:7358–7363.
  • Rousseau, D., Kaspar R., Rosenwald I., Gehrke L., and Sonenberg N.. 1996. Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E. Proc. Natl. Acad. Sci. USA 93:1065–1070.
  • Roy, G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M., and Sonenberg N.. 2002. Paip1 interacts with poly(A) binding protein through two independent binding motifs. Mol. Cell. Biol. 22:3769–3782.
  • Rubin, G. M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., and Harvey D. A.. 2000. A Drosophila complementary DNA resource. Science 287:2222–2224.
  • Rubin, G. M., and Spradling A. C.. 1982. Genetic transformation of Drosophila with transposable element vectors. Science 218:348–353.
  • Sachs, A. 2000. Physical and functional interactions between the mRNA cap structure and the poly(A) tail, p. 447–466. In Sonenberg N., Hershey J. W. B., and Matthews M. B. (ed.), Translational control of gene expression. Cold Spring Harbor Laboratory Press, New York, N.Y.
  • Sachs, A. B., Davis R. W., and Kornberg R. D.. 1987. A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. Mol. Cell. Biol. 7:3268–3276.
  • Saucedo, L. J., and Edgar B. A.. 2002. Why size matters: altering cell size. Curr. Opin. Genet. Dev. 12:565–571.
  • Schneider, I. 1972. Cell lines derived from late embryonic stages of Drosophila melanogaster. J. Embryol. Exp. Morphol. 27:353–365.
  • Searfoss, A., Dever T. E., and Wickner R.. 2001. Linking the 3′ poly(A) tail to the subunit joining step of translation initiation: relations of Pab1p, eukaryotic translation initiation factor 5B (Fun12p), and Ski2p-Slh1p. Mol. Cell. Biol. 21:4900–4908.
  • Sigrist, S. J., Thiel P. R., Reiff D. F., Lachance P. E., Lasko P., and Schuster C. M.. 2000. Postsynaptic translation affects the efficacy and morphology of neuromuscular junctions. Nature 405:1062–1065.
  • Sonenberg, N., and Gingras A. C.. 1998. The mRNA 5′ cap-binding protein eIF4E and control of cell growth. Curr. Opin. Cell Biol. 10:268–275.
  • Soriano, E., Del Rio J. A., and Auladell C.. 1993. Characterization of the phenotype and birthdates of pyknotic dead cells in the nervous system by a combination of DNA staining and immunohistochemistry for 5′-bromodeoxyuridine and neural antigens. J. Histochem. Cytochem. 41:819–827.
  • Struhl, G., and Basler K.. 1993. Organizing activity of wingless protein in Drosophila. Cell 72:527–540.
  • Weinkove, D., and Leevers S. J.. 2000. The genetic control of organ growth: insights from Drosophila. Curr. Opin. Genet. Dev. 10:75–80.
  • Wickens, M. 1990. How the messenger got its tail: addition of poly(A) in the nucleus. Trends Biochem. Sci. 15:277–281.
  • Wolff, T. 2000. Histological techniques for the Drosophila eye. Part II: adult, p. 229–243. In Sullivan W., Ashburner M., and Hawley R. S. (ed.), Drosophila protocols. Cold Spring Harbor Laboratory Press, New York, N.Y.

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