RACK1 mRNA translation is regulated via a rapamycin-sensitive pathway and coordinated with ribosomal protein synthesis

FEBS Letters

Volumn 579, Issue 25, 2005, Pages 5517-5520

  Loreni, Fabrizio ^a   Iadevaia, Valentina ^a   Tino, Elisa ^a   Caldarola, Sara ^a   Amaldi, Francesco ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

Author keywords

Growth control; Ribosome; TOP mRNA; Translational regulation

Indexed keywords

AMINO ACID; MESSENGER RNA; RAPAMYCIN; RECEPTOR FOR ACTIVATED C KINASE 1; RECEPTOR PROTEIN; RIBOSOME PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; FEMALE; HELA CELL; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN FUNCTION; REGULATORY MECHANISM; RIBOSOME; RNA SEQUENCE; RNA STRUCTURE; SERUM; STIMULATION; TERMINAL OLIGOPYRIMIDINE TRACT; TRANSLATION REGULATION;

AMINO ACIDS; GENE EXPRESSION REGULATION; GTP-BINDING PROTEINS; HELA CELLS; HUMANS; NEOPLASM PROTEINS; PROTEIN BIOSYNTHESIS; RECEPTORS, CELL SURFACE; RIBOSOMAL PROTEINS; RNA, MESSENGER; SIROLIMUS;

VERTEBRATA;

EID: 26844467327     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.09.016     Document Type: Article

References (29)

1. A. McCahill, J. Warwicker, G.B. Bolger, M.D. Houslay, and S.J. Yarwood The RACK1 scaffold protein: a dynamic cog in cell response mechanisms Mol Pharmacol 62 2002 1261 1273
2. F. Guillemot, A. Billault, and C. Auffray Physical linkage of a guanine nucleotide-binding protein-related gene to the chicken major histocompatibility complex Proc. Natl. Acad. Sci. USA 86 1989 4594 4598
3. D. Ron, Z. Jiang, L. Yao, A. Vagts, I. Diamond, and A. Gordon Coordinated movement of RACK1 with activated betaIIPKC J. Biol. Chem. 274 1999 27039 27046
4. B.Y. Chang, K.B. Conroy, E.M. Machleder, and C.A. Cartwright RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells Mol. Cell Biol. 18 1998 3245 3256
5. J. Liliental, and D.D. Chang Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit J. Biol. Chem. 273 1998 2379 2383
6. C.S. Buensuceso, D. Woodside, J.L. Huff, G.E. Plopper, and T.E. O'Toole The WD protein Rack1 mediates protein kinase C and integrin-dependent cell migration J. Cell Sci. 114 2001 1691 1698
7. A. Besson, T.L. Wilson, and V.W. Yong The anchoring protein RACK1 links protein kinase C epsilon to integrin beta chains. Requirements for adhesion and motility J. Biol. Chem. 277 2002 22073 22084
8. J. Nilsson, J. Sengupta, J. Frank, and P. Nissen Regulation of eukaryotic translation by the RACK1 protein: a platform for signalling molecules on the ribosome EMBO Rep. 5 2004 1137 1141
9. A.J. Link, J. Eng, D.M. Schieltz, E. Carmack, G.J. Mize, D.R. Morris, B.M. Garvik, and J.R. Yates 3rd Direct analysis of protein complexes using mass spectrometry Nat. Biotechnol. 17 1999 676 682
10. V.R. Gerbasi, C.M. Weaver, S. Hill, D.B. Friedman, and A.J. Link Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression Mol. Cell Biol. 24 2004 8276 8287
11. S. Baum, M. Bittins, S. Frey, and M. Seedorf Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes Biochem. J. 380 2004 823 830
12. B. Shor, J. Calaycay, J. Rushbrook, and M. McLeod Cpc2/RACK1 is a ribosome-associated protein that promotes efficient translation in Schizosaccharomyces pombe J. Biol. Chem. 278 2003 49119 49128
13. M. Ceci, C. Gaviraghi, C. Gorrini, L.A. Sala, N. Offenhauser, P.C. Marchisio, and S. Biffo Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly Nature 426 2003 579 584
14. O. Meyuhas, and E. Hornstein M.B. Mathews Translational control of gene expression 2000 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 671 693
15. M. Ledda Effect of 3′UTR length on the translational regulation of 5′-terminal oligopyrimidine mRNAs Gene 344 2005 213 220
16. F. Loreni, and F. Amaldi Translational regulation of ribosomal protein synthesis in Xenopus cultured cells: mRNA relocation between polysomes and RNP during nutritional shifts Eur. J. Biochem. 205 1992 1027 1032
17. J. Zhu, A. Hayakawa, T. Kakegawa, and R.L. Kaspar Binding of the La autoantigen to the 5′ untranslated region of a chimeric human translation elongation factor 1A reporter mRNA inhibits translation in vitro Biochim. Biophys. Acta 1521 2001 19 29
18. E.I. Schwartz, R.V. Intine, and R.J. Maraia CK2 is responsible for phosphorylation of human La protein serine-366 and can modulate rpL37 5′-terminal oligopyrimidine mRNA metabolism Mol. Cell Biol. 24 2004 9580 9591
19. C. Crosio, P.P. Boyl, F. Loreni, P. Pierandrei-Amaldi, and F. Amaldi La protein has a positive effect on the translation of TOP mRNAs in vivo Nucleic Acids Res. 28 2000 2927 2934
20. B. Cardinali, C. Carissimi, P. Gravina, and P. Pierandrei-Amaldi La protein is associated with terminal oligopyrimidine mRNAs in actively translating polysomes J. Biol. Chem. 278 2003 35145 35151
21. L. Pellizzoni, F. Lotti, B. Maras, and P. Pierandrei-Amaldi Cellular nucleic acid binding protein binds a conserved region of the 5′ UTR of Xenopus laevis ribosomal protein mRNAs J. Mol. Biol. 267 1997 264 275
22. S. Fumagalli, and G. Thomas N. Sonenberg J.W.B. Hershey M.B. Mathews Translational Control of Gene Expression 2000 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 695 717
23. M. Pende S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5′-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway Mol. Cell Biol. 24 2004 3112 3124
24. M. Stolovich, H. Tang, E. Hornstein, G. Levy, R. Cohen, S.S. Bae, M.J. Birnbaum, and O. Meyuhas Transduction of growth or mitogenic signals into translational activation of TOP mRNAs is fully reliant on the phosphatidylinositol 3-kinase-mediated pathway but requires neither S6K1 nor rpS6 phosphorylation Mol. Cell Biol. 22 2002 8101 8113
25. H. Tang, E. Hornstein, M. Stolovich, G. Levy, M. Livingstone, D. Templeton, J. Avruch, and O. Meyuhas Amino acid-induced translation of TOP mRNAs is fully dependent on phosphatidylinositol 3-kinase-mediated signaling, is partially inhibited by rapamycin, and is independent of S6K1 and rpS6 phosphorylation Mol. Cell Biol. 21 2001 8671 8683
26. S. Caldarola, F. Amaldi, C.G. Proud, and F. Loreni Translational regulation of terminal oligopyrimidine mRNAs induced by serum and amino acids involves distinct signaling events J. Biol. Chem. 279 2004 13522 13531
27. Sambrook, J., Fritsch, E.F. and Maniatia, T. (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
28. R.A. Zimmermann The double life of ribosomal proteins Cell 115 2003 130 132
29. I.G. Wool Extraribosomal functions of ribosomal proteins Trends Biochem. Sci. 21 1996 164 165