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Vol. 18, Issue 6, 2274-2287, June 2007
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Department of Molecular and Cellular Biology and Howard Hughes Medical Institute, University of Arizona, Tucson, AZ 85721-0106; and *Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, 4099-003 Porto, Portugal
Submitted March 5, 2007;
Revised March 28, 2007;
Accepted March 30, 2007
Monitoring Editor: Thomas Fox
Recent experiments have defined cytoplasmic foci, referred to as processing bodies (P-bodies), that contain untranslating mRNAs in conjunction with proteins involved in translation repression and mRNA decapping and degradation. However, the order of protein assembly into P-bodies and the interactions that promote P-body assembly are unknown. To gain insight into how yeast P-bodies assemble, we examined the P-body accumulation of Dcp1p, Dcp2p, Edc3p, Dhh1p, Pat1p, Lsm1p, Xrn1p, Ccr4p, and Pop2p in deletion mutants lacking one or more P-body component. These experiments revealed that Dcp2p and Pat1p are required for recruitment of Dcp1p and of the Lsm1-7p complex to P-bodies, respectively. We also demonstrate that P-body assembly is redundant and no single known component of P-bodies is required for P-body assembly, although both Dcp2p and Pat1p contribute to P-body assembly. In addition, our results indicate that Pat1p can be a nuclear-cytoplasmic shuttling protein and acts early in P-body assembly. In contrast, the Lsm1-7p complex appears to primarily function in a rate limiting step after P-body assembly in triggering decapping. Taken together, these results provide insight both into the function of individual proteins involved in mRNA degradation and the mechanisms by which yeast P-bodies assemble.
Address correspondence to: Roy Parker (rrparker{at}u.arizona.edu).
This article has been cited by other articles:
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  M. A. M. Reijns, R. D. Alexander, M. P. Spiller, and J. D. Beggs A role for Q/N-rich aggregation-prone regions in P-body localization J. Cell Sci., August 1, 2008; 121(15): 2463 - 2472. [Abstract] [Full Text] [PDF]
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 D. Zheng, N. Ezzeddine, C.-Y. A. Chen, W. Zhu, X. He, and A.-B. Shyu Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells J. Cell Biol., July 14, 2008; 182(1): 89 - 101. [Abstract] [Full Text] [PDF]
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 C. Beckham, A. Hilliker, A.-M. Cziko, A. Noueiry, M. Ramaswami, and R. Parker The DEAD-Box RNA Helicase Ded1p Affects and Accumulates in Saccharomyces cerevisiae P-Bodies Mol. Biol. Cell, March 1, 2008; 19(3): 984 - 993. [Abstract] [Full Text] [PDF]
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 G. R. Pilkington and R. Parker Pat1 Contains Distinct Functional Domains That Promote P-Body Assembly and Activation of Decapping Mol. Cell. Biol., February 15, 2008; 28(4): 1298 - 1312. [Abstract] [Full Text] [PDF]
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C. J. Decker, D. Teixeira, and R. Parker Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae J. Cell Biol., November 5, 2007; 179(3): 437 - 449. [Abstract] [Full Text] [PDF]
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 C. J. Beckham, H. R. Light, T. Amar Nissan, P. Ahlquist, R. Parker, and A. Noueiry Interactions between Brome Mosaic Virus RNAs and Cytoplasmic Processing Bodies J. Virol., September 15, 2007; 81(18): 9759 - 9768. [Abstract] [Full Text] [PDF]
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M. Brengues and R. Parker Accumulation of Polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-Bodies in Saccharomyces cerevisiae Mol. Biol. Cell, July 1, 2007; 18(7): 2592 - 2602. [Abstract] [Full Text] [PDF]
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