In Vivo Association of the Stability Control Protein αCP with Actively Translating mRNAs

REFERENCES

• Andino, R., G. E. Rieckhof, P. L. Achacoso, and D. Baltimore. 1993. Poliovirus RNA synthesis utilizes an RNP complex formed around the 5′-end of viral RNA. EMBO J. 12: 3587–3598.
   PubMed Web of Science ®Google Scholar
• Ashley, C. T., K. D. Wilkinson, D. Reines, and S. T. Warren. 1993. FMR1 protein: conserved RNP family domains and selective RNA binding. Science 262: 563–566.
   PubMed Web of Science ®Google Scholar
• Atwater, J. A., R. Wisdom, and I. M. Verma. 1990. Regulated mRNA stability. Annu. Rev. Genet. 24: 519–541.
   PubMed Web of Science ®Google Scholar
• Bernstein, P. L., D. J. Herrick, R. D. Prokipcak, and J. Ross. 1992. Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant. Genes Dev. 6: 642–654.
   PubMed Web of Science ®Google Scholar
• Blobel, G., and D. Sabatini. 1971. Dissociation of mammalian polyribosomes into subunits by puromycin. Proc. Natl. Acad. Sci. USA 68: 390–394.
   PubMedGoogle Scholar
• Brown, V., P. Jin, S. Ceman, J. C. Darnell, W. T. O'Donnell, S. A. Tenenbaum, X. Jin, Y. Feng, K. D. Wilkinson, J. D. Keene, R. B. Darnell, and S. T. Warren. 2001. Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome. Cell 107: 477–487.
   PubMed Web of Science ®Google Scholar
• Chkheidze, A. N., D. L. Lyakhov, A. V. Makeyev, J. Morales, J. Kong, and S. A. Liebhaber. 1999. Assembly of the alpha-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3′ untranslated region determinant and poly(C) binding protein αCP. Mol. Cell. Biol. 19: 4572–4781.
   PubMed Web of Science ®Google Scholar
• Clegg, J. B., D. J. Weatherall, and P. F. Milner. 1971. Haemoglobin Constant Spring—a chain termination mutant? Nature 234: 337–340.
   PubMed Web of Science ®Google Scholar
• Corbin, F., M. Bouillon, A. Fortin, S. Morin, F. Rousseau, and E. W. Khandjian. 1997. The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes. Hum. Mol. Genet. 6: 1465–1472.
   PubMed Web of Science ®Google Scholar
• Darnell, J. C., K. B. Jensen, P. Jin, V. Brown, S. T. Warren, and R. B. Darnell. 2001. Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Cell 107: 489–499.
   PubMed Web of Science ®Google Scholar
• Doyle, G. A., N. A. Betz, P. F. Leeds, A. J. Fleisig, R. D. Prokipcak, and J. Ross. 1998. The c-myc coding region determinant-binding protein: a member of a family of KH domain RNA-binding proteins. Nucleic Acids Res. 26: 5036–5044.
   PubMed Web of Science ®Google Scholar
• Feng, Y., D. Absher, D. E. Eberhart, V. Brown, H. Malter, and S. T. Warren. 1997. FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association. Mol. Cell 1: 109–118.
   PubMed Web of Science ®Google Scholar
• Frey, S., M. Pool, and M. Seedorf. 2001. Scp160p, an RNA-binding, polysome-associated protein, localizes to the endoplasmic reticulum of Saccharomyces cerevisiae in a microtubule-dependent manner. J. Biol. Chem. 276: 15905–15912.
   PubMedGoogle Scholar
• Funke, B., B. Zuleger, R. Benavente, T. Schuster, M. Goller, J. Stevenin, and I. Horak. 1996. The mouse poly(C)-binding protein exists in multiple isoforms and interacts with several RNA-binding proteins. Nucleic Acids Res. 24: 3821–3828.
   PubMedGoogle Scholar
• Gamarnik, A. V., and R. Andino. 1997. Two functional complexes formed by KH domain containing proteins with the 5′ noncoding region of poliovirus RNA. RNA 3: 882–892.
   PubMed Web of Science ®Google Scholar
• Hazelrigg, T. 1998. The destinies and destinations of RNAs. Cell 95: 451–460.
   PubMedGoogle Scholar
• Hohne, M., B. J. Thiele, S. Prehn, E. Giessmann, B. Nack, and S. M. Rapoport. 1988. Activation of translationally inactive lipoxygenase mRNP particles from rabbit reticulocytes. Biomed. Biochim. Acta 47: 75–78.
   PubMedGoogle Scholar
• Holcik, M., and S. A. Liebhaber. 1997. Four highly stable eukaryotic mRNAs assemble 3′ untranslated region RNA-protein complexes sharing cis and trans components. Proc. Natl. Acad. Sci. USA 94: 2410–2414.
   PubMed Web of Science ®Google Scholar
• Kaytor, M. D., and H. T. Orr. 2001. RNA targets of the fragile X protein. Cell 107: 555–557.
   PubMedGoogle Scholar
• Kiledjian, M., X. Wang, and S. A. Liebhaber. 1995. Identification of two KH domain proteins in the alpha-globin mRNP stability complex. EMBO J. 14: 4357–4364.
   PubMed Web of Science ®Google Scholar
• Kong, J., et al. Mol. Cell. Biol., in press.
   Google Scholar
• Lang, B. D., A. M. Li, H. D. Black-Brewster, and J. L. Fridovich-Keil. 2001. The brefeldin A resistance protein Bfr1p is a component of polyribosome-associated mRNP complexes in yeast. Nucleic Acids Res. 29: 2567–2574.
   PubMedGoogle Scholar
• Leffers, H., K. Dejgaard, and J. E. Celis. 1995. Characterization of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains. Eur. J. Biochem. 230: 447–453.
   PubMedGoogle Scholar
• Liebhaber, S. A. 1997. mRNA stability and the control of gene expression. Nucleic Acids Symp. Ser. 36: 29–32.
   Google Scholar
• Liebhaber, S. A., and Y. W. Kan. 1981. Differentiation of the mRNA transcripts originating from the α1- and α2-globin loci in normals and alpha-thalassemics. J. Clin. Investig. 68: 439–446.
   PubMed Web of Science ®Google Scholar
• Liebhaber, S. A., Z. Wang, F. E. Cash, B. Monks, and J. E. Russell. 1996. Developmental silencing of the embryonic ζ-globin gene: concerted action of the promoter and the 3′-flanking region combined with stage-specific silencing by the transcribed segment. Mol. Cell. Biol. 16: 2637–2646.
   PubMedGoogle Scholar
• Makeyev, A. V., and S. A. Liebhaber. 2000. Identification of two novel mammalian genes establishes a subfamily of KH-domain RNA-binding proteins. Genomics 67: 301–316.
   PubMed Web of Science ®Google Scholar
• Makeyev, A. V., and S. A. Liebhaber. 2002. The poly(C)-binding proteins: a multiplicity of functions and a search for mechanisms. RNA 8: 265–278.
   PubMed Web of Science ®Google Scholar
• Matunis, M. J., W. M. Michael, and G. Dreyfuss. 1992. Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein. Mol. Cell. Biol. 12: 164–171.
   PubMed Web of Science ®Google Scholar
• Milner, P. F., J. B. Clegg, and D. J. Weatherall. 1971. Haemoglobin-H disease due to a unique haemoglobin variant with an elongated alpha-chain. Lancet i: 729–732.
   Google Scholar
• Morales, J., J. E. Russell, and S. A. Liebhaber. 1997. Destabilization of human alpha-globin mRNA by translation anti-termination is controlled during erythroid differentiation and is paralleled by phased shortening of the poly(A) tail. J. Biol. Chem. 272: 6607–6613.
   PubMed Web of Science ®Google Scholar
• Ostareck, D. H., A. Ostareck-Lederer, M. Wilm, B. J. Thiele, M. Mann, and M. W. Hentze. 1997. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell 89: 597–606.
   PubMed Web of Science ®Google Scholar
• Ostareck, D. H., A. Ostareck-Lederer, I. N. Shatsky, and M. W. Hentze. 2001. Lipoxygenase mRNA silencing in erythroid differentiation: the 3′UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104: 281–290.
   PubMed Web of Science ®Google Scholar
• Ostareck-Lederer, A., D. H. Ostareck, N. Standart, and B. J. Thiele. 1994. Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region. EMBO J. 13: 1476–1481.
   PubMed Web of Science ®Google Scholar
• Paulding, W. R., and M. F. Czyzyk-Krzeska. 2000. Hypoxia-induced regulation of mRNA stability. Adv. Exp. Med. Biol. 475: 111–121.
   PubMedGoogle Scholar
• Ross, J. 1995. mRNA stability in mammalian cells. Microbiol. Rev. 59: 423–450.
   PubMedGoogle Scholar
• Russell, J. E., J. Morales, and S. A. Liebhaber. 1997. The role of mRNA stability in the control of globin gene expression. Prog. Nucleic Acids Res. Mol. Biol. 57: 249–287.
   Google Scholar
• Siomi, H., M. J. Matunis, W. M. Michael, and G. Dreyfuss. 1993. The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res. 21: 1193–1198.
   PubMed Web of Science ®Google Scholar
• Stefanovic, B., C. Hellerbrand, M. Holcik, M. A. Briendl, S. A. Liebhaber, and D. A. Brenner. 1997. Posttranscriptional regulation of collagen α1(I) mRNA in hepatic stellate cells. Mol. Cell. Biol. 17: 5201–5209.
   PubMed Web of Science ®Google Scholar
• Surdej, P., A. Riedl, and M. Jacobs-Lorena. 1994. Regulation of mRNA stability in development. Annu. Rev. Genet. 28: 263–282.
   PubMedGoogle Scholar
• Thiele, B. J., H. Andree, M. Hohne, and S. M. Rapoport. 1981. Regulation of the synthesis of lipoxygenase in erythroid cells. Acta Biol. Med. Ger. 40: 597–602.
   PubMedGoogle Scholar
• Thiele, B. J., H. Andree, M. Hohne, and S. M. Rapoport. 1982. Lipoxygenase mRNA in rabbit reticulocytes. Its isolation, characterization and translational repression. Eur. J. Biochem. 129: 133–141.
   PubMedGoogle Scholar
• Wang, X., M. Kiledjian, I. M. Weiss, and S. A. Liebhaber. 1995. Detection and characterization of a 3′ untranslated region ribonucleoprotein complex associated with human α-globin mRNA stability. Mol. Cell. Biol. 15: 1769–1777.
   PubMedGoogle Scholar
• Wang, Z., N. Day, P. Trifillis, and M. Kiledjian. 1999. An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro. Mol. Cell. Biol. 19: 4552–4560.
   PubMed Web of Science ®Google Scholar
• Weiss, I. M., and S. A. Liebhaber. 1994. Erythroid cell-specific determinants of α-globin mRNA stability. Mol. Cell. Biol. 14: 8123–8132.
   PubMed Web of Science ®Google Scholar
• Weiss, I. M., and S. A. Liebhaber. 1995. Erythroid cell-specific mRNA stability elements in the α2-globin 3′ nontranslated region. Mol. Cell. Biol. 15: 2457–2465.
   PubMed Web of Science ®Google Scholar
• Welfle, H., B. Henkel, and H. Bielka. 1976. Ionic interactions in eukaryotic ribosomes: splitting of the subunits of rat liver ribosomes by treatment with monovalent cations. Acta Biol. Med. Ger. 35: 401–411.
   PubMedGoogle Scholar
• Ziemiecki, A., R. G. Muller, X. C. Fu, N. E. Hynes, and S. Kozma. 1990. Oncogenic activation of the human trk proto-oncogene by recombination with the ribosomal large subunit protein L7a. EMBO J. 9: 191–196.
   PubMed Web of Science ®Google Scholar