Human Pat1b Connects Deadenylation with mRNA Decapping and Controls the Assembly of Processing Bodies

REFERENCES

• Andrei, M. A., D. Ingelfinger, R. Heintzmann, T. Achsel, R. Rivera-Pomar, and R. Luhrmann. 2005. A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies. RNA 11:717–727.
   PubMed Web of Science ®Google Scholar
• Bashkirov, V. I., H. Scherthan, J. A. Solinger, J. M. Buerstedde, and W. D. Heyer. 1997. A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J. Cell Biol. 136:761–773.
   PubMed Web of Science ®Google Scholar
• Bhattacharyya, S. N., R. Habermacher, U. Martine, E. I. Closs, and W. Filipowicz. 2006. Relief of microRNA-mediated translational repression in human cells subjected to stress. Cell 125:1111–1124.
   PubMed Web of Science ®Google Scholar
• Boag, P. R., A. Atalay, S. Robida, V. Reinke, and T. K. Blackwell. 2008. Protection of specific maternal messenger RNAs by the P body protein CGH-1 (Dhh1/RCK) during Caenorhabditis elegans oogenesis. J. Cell Biol. 182:543–557.
   PubMedGoogle Scholar
• Bonnerot, C., R. Boeck, and B. Lapeyre. 2000. The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p. Mol. Cell. Biol. 20:5939–5946.
   PubMedGoogle Scholar
• Bouveret, E., G. Rigaut, A. Shevchenko, M. Wilm, and B. Seraphin. 2000. A Sm-like protein complex that participates in mRNA degradation. EMBO J. 19:1661–1671.
   PubMedGoogle Scholar
• Chekulaeva, M., and W. Filipowicz. 2009. Mechanisms of miRNA-mediated post-transcriptional regulation in animal cells. Curr. Opin. Cell Biol. 21:452–460.
   PubMed Web of Science ®Google Scholar
• Chowdhury, A., J. Mukhopadhyay, and S. Tharun. 2007. The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs. RNA 13:998–1016.
   PubMedGoogle Scholar
• Coller, J., and R. Parker. 2005. General translational repression by activators of mRNA decapping. Cell 122:875–886.
   PubMed Web of Science ®Google Scholar
• Cougot, N., S. Babajko, and B. Seraphin. 2004. Cytoplasmic foci are sites of mRNA decay in human cells. J. Cell Biol. 165:31–40.
   PubMed Web of Science ®Google Scholar
• Decker, C. J., D. Teixeira, and R. Parker. 2007. Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. J. Cell Biol. 179:437–449.
   PubMed Web of Science ®Google Scholar
• Eulalio, A., I. Behm-Ansmant, D. Schweizer, and E. Izaurralde. 2007. P-body formation is a consequence, not the cause, of RNA-mediated gene silencing. Mol. Cell. Biol. 27:3970–3981.
   PubMed Web of Science ®Google Scholar
• Fenger-Gron, M., C. Fillman, B. Norrild, and J. Lykke-Andersen. 2005. Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol. Cell 20:905–915.
   PubMed Web of Science ®Google Scholar
• Franks, T. M., and J. Lykke-Andersen. 2007. TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes Dev. 21:719–735.
   PubMed Web of Science ®Google Scholar
• Garneau, N. L., J. Wilusz, and C. J. Wilusz. 2007. The highways and byways of mRNA decay. Nat. Rev. Mol. Cell Biol. 8:113–126.
   PubMed Web of Science ®Google Scholar
• Gilks, N., N. Kedersha, M. Ayodele, L. Shen, G. Stoecklin, L. M. Dember, and P. Anderson. 2004. Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol. Biol. Cell 15:5383–5398.
   PubMed Web of Science ®Google Scholar
• Haas, G., J. E. Braun, C. Igreja, F. Tritschler, T. Nishihara, and E. Izaurralde. 2010. HPat provides a link between deadenylation and decapping in metazoa. J. Cell Biol. 189:289–302.
   PubMedGoogle Scholar
• Hatfield, L., C. A. Beelman, A. Stevens, and R. Parker. 1996. Mutations in trans-acting factors affecting mRNA decapping in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:5830–5838.
   PubMedGoogle Scholar
• He, W., and R. Parker. 2001. The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3′ termini from partial degradation. Genetics 158:1445–1455.
   PubMedGoogle Scholar
• Hsu, C. L., and A. Stevens. 1993. Yeast cells lacking 5′→3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure. Mol. Cell. Biol. 13:4826–4835.
   PubMedGoogle Scholar
• Ingelfinger, D., D. J. Arndt-Jovin, R. Luhrmann, and T. Achsel. 2002. The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8:1489–1501.
   PubMed Web of Science ®Google Scholar
• Kedersha, N. L., M. Gupta, W. Li, I. Miller, and P. Anderson. 1999. RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J. Cell Biol. 147:1431–1442.
   PubMed Web of Science ®Google Scholar
• Lim, F., T. P. Downey, and D. S. Peabody. 2001. Translational repression and specific RNA binding by the coat protein of the Pseudomonas phage PP7. J. Biol. Chem. 276:22507–22513.
   PubMed Web of Science ®Google Scholar
• Liu, J., M. A. Valencia-Sanchez, G. J. Hannon, and R. Parker. 2005. MicroRNA-dependent localization of targeted mRNAs to mammalian P-bodies. Nat. Cell Biol. 7:719–723.
   PubMed Web of Science ®Google Scholar
• Lykke-Andersen, J., and E. Wagner. 2005. Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1. Genes Dev. 19:351–361.
   PubMed Web of Science ®Google Scholar
• Muhlrad, D., C. J. Decker, and R. Parker. 1994. Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′→3′ digestion of the transcript. Genes Dev. 8:855–866.
   PubMed Web of Science ®Google Scholar
• Muhlrad, D., and R. Parker. 2005. The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p. EMBO J. 24:1033–1045.
   PubMedGoogle Scholar
• Nakamura, Y., K. J. Tanaka, M. Miyauchi, L. Huang, M. Tsujimoto, and K. Matsumoto. 21 May 2010. Translational repression by the oocyte-specific protein P100 in Xenopus. Dev. Biol. [Epub ahead of print.] 10.1016/j.ydbio.2010.05.006.
   Google Scholar
• Parker, R., and H. Song. 2004. The enzymes and control of eukaryotic mRNA turnover. Nat. Struct. Mol. Biol. 11:121–127.
   PubMed Web of Science ®Google Scholar
• Pilkington, G. R., and R. Parker. 2008. Pat1 contains distinct functional domains that promote P-body assembly and activation of decapping. Mol. Cell. Biol. 28:1298–1312.
   PubMed Web of Science ®Google Scholar
• Pillai, R. S., S. N. Bhattacharyya, C. G. Artus, T. Zoller, N. Cougot, E. Basyuk, E. Bertrand, and W. Filipowicz. 2005. Inhibition of translational initiation by Let-7 microRNA in human cells. Science 309:1573–1576.
   PubMed Web of Science ®Google Scholar
• Reijns, M. A., R. D. Alexander, M. P. Spiller, and J. D. Beggs. 2008. A role for Q/N-rich aggregation-prone regions in P-body localization. J. Cell Sci. 121:2463–2472.
   PubMed Web of Science ®Google Scholar
• Rothbauer, U., K. Zolghadr, S. Muyldermans, A. Schepers, M. C. Cardoso, and H. Leonhardt. 2008. A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins. Mol. Cell. Proteomics 7:282–289.
   PubMed Web of Science ®Google Scholar
• Scheller, N., P. Resa-Infante, S. de la Luna, R. P. Galao, M. Albrecht, L. Kaestner, P. Lipp, T. Lengauer, A. Meyerhans, and J. Diez. 2007. Identification of PatL1, a human homolog to yeast P body component Pat1. Biochim. Biophys. Acta 1773:1786–1792.
   PubMedGoogle Scholar
• Sheth, U., and R. Parker. 2003. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300:805–808.
   PubMed Web of Science ®Google Scholar
• Shorter, J., and S. Lindquist. 2005. Prions as adaptive conduits of memory and inheritance. Nat. Rev. Genet. 6:435–450.
   PubMed Web of Science ®Google Scholar
• Stoecklin, G., and P. Anderson. 2006. Posttranscriptional mechanisms regulating the inflammatory response. Adv. Immunol. 89:1–37.
   PubMedGoogle Scholar
• Stoecklin, G., T. Mayo, and P. Anderson. 2006. ARE-mRNA degradation requires the 5′-3′ decay pathway. EMBO Rep. 7:72–77.
   PubMed Web of Science ®Google Scholar
• Stoecklin, G., P. Stoeckle, M. Lu, O. Muehlemann, and C. Moroni. 2001. Cellular mutants define a common mRNA degradation pathway targeting cytokine AU-rich elements. RNA 7:1578–1588.
   PubMed Web of Science ®Google Scholar
• Teixeira, D., and R. Parker. 2007. Analysis of P-body assembly in Saccharomyces cerevisiae. Mol. Biol. Cell 18:2274–2287.
   PubMed Web of Science ®Google Scholar
• Temme, C., S. Zaessinger, S. Meyer, M. Simonelig, and E. Wahle. 2004. A complex containing the CCR4 and CAF1 proteins is involved in mRNA deadenylation in Drosophila. EMBO J. 23:2862–2871.
   PubMed Web of Science ®Google Scholar
• Tharun, S., and R. Parker. 2001. Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol. Cell 8:1075–1083.
   PubMedGoogle Scholar
• van Dijk, E., N. Cougot, S. Meyer, S. Babajko, E. Wahle, and B. Seraphin. 2002. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21:6915–6924.
   PubMed Web of Science ®Google Scholar
• Wang, Z., X. Jiao, A. Carr-Schmid, and M. Kiledjian. 2002. The hDcp2 protein is a mammalian mRNA decapping enzyme. Proc. Natl. Acad. Sci. U. S. A. 99:12663–12668.
   PubMed Web of Science ®Google Scholar
• Winkler, G. S., K. W. Mulder, V. J. Bardwell, E. Kalkhoven, and H. T. Timmers. 2006. Human Ccr4-Not complex is a ligand-dependent repressor of nuclear receptor-mediated transcription. EMBO J. 25:3089–3099.
   PubMed Web of Science ®Google Scholar
• Yamasaki, S., G. Stoecklin, N. Kedersha, M. Simarro, and P. Anderson. 2007. T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs. J. Biol. Chem. 282:30070–30077.
   PubMed Web of Science ®Google Scholar
• Zheng, D., N. Ezzeddine, C. Y. Chen, W. Zhu, X. He, and A. B. Shyu. 2008. Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells. J. Cell Biol. 182:89–101.
   PubMed Web of Science ®Google Scholar