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Deadenylation and P-bodies.

Chen CY, Shyu AB.

Adv Exp Med Biol. 2013;768:183-95. doi: 10.1007/978-1-4614-5107-5_11. Review.


PUF3 acceleration of deadenylation in vivo can operate independently of CCR4 activity, possibly involving effects on the PAB1-mRNP structure.

Lee D, Ohn T, Chiang YC, Quigley G, Yao G, Liu Y, Denis CL.

J Mol Biol. 2010 Jun 18;399(4):562-75. doi: 10.1016/j.jmb.2010.04.034.


Relationship of GW/P-bodies with stress granules.

Stoecklin G, Kedersha N.

Adv Exp Med Biol. 2013;768:197-211. doi: 10.1007/978-1-4614-5107-5_12. Review.


Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases.

Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I, Tsujimoto M, Suzuki T, Katada T, Hoshino S.

Genes Dev. 2007 Dec 1;21(23):3135-48.


Deadenylation is a widespread effect of miRNA regulation.

Eulalio A, Huntzinger E, Nishihara T, Rehwinkel J, Fauser M, Izaurralde E.

RNA. 2009 Jan;15(1):21-32. doi: 10.1261/rna.1399509.


Cytoplasmic deadenylation: regulation of mRNA fate.

Wiederhold K, Passmore LA.

Biochem Soc Trans. 2010 Dec;38(6):1531-6. doi: 10.1042/BST0381531. Review.


Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells.

Zheng D, Ezzeddine N, Chen CY, Zhu W, He X, Shyu AB.

J Cell Biol. 2008 Jul 14;182(1):89-101. doi: 10.1083/jcb.200801196.


Relationship of other cytoplasmic ribonucleoprotein bodies (cRNPB) to GW/P bodies.

Moser JJ, Fritzler MJ.

Adv Exp Med Biol. 2013;768:213-42. doi: 10.1007/978-1-4614-5107-5_13. Review.


GW182 proteins cause PABP dissociation from silenced miRNA targets in the absence of deadenylation.

Zekri L, Kuzuoğlu-Öztürk D, Izaurralde E.

EMBO J. 2013 Apr 3;32(7):1052-65. doi: 10.1038/emboj.2013.44.


Stability control of MTL1 mRNA by the RNA-binding protein Khd1p in yeast.

Mauchi N, Ohtake Y, Irie K.

Cell Struct Funct. 2010;35(2):95-105.


The interactions of GW182 proteins with PABP and deadenylases are required for both translational repression and degradation of miRNA targets.

Huntzinger E, Kuzuoglu-Öztürk D, Braun JE, Eulalio A, Wohlbold L, Izaurralde E.

Nucleic Acids Res. 2013 Jan;41(2):978-94. doi: 10.1093/nar/gks1078.


Sbp1p affects translational repression and decapping in Saccharomyces cerevisiae.

Segal SP, Dunckley T, Parker R.

Mol Cell Biol. 2006 Jul;26(13):5120-30. Erratum in: Mol Cell Biol. 2007 Jan;27(2):789-90.


P-body formation is a consequence, not the cause, of RNA-mediated gene silencing.

Eulalio A, Behm-Ansmant I, Schweizer D, Izaurralde E.

Mol Cell Biol. 2007 Jun;27(11):3970-81.


mRNA decay proteins are targeted to poly(A)+ RNA and dsRNA-containing cytoplasmic foci that resemble P-bodies in Entamoeba histolytica.

López-Rosas I, Orozco E, Marchat LA, García-Rivera G, Guillen N, Weber C, Carrillo-Tapia E, Hernández de la Cruz O, Pérez-Plasencia C, López-Camarillo C.

PLoS One. 2012;7(9):e45966. doi: 10.1371/journal.pone.0045966.


dTIS11 Protein-dependent polysomal deadenylation is the key step in AU-rich element-mediated mRNA decay in Drosophila cells.

Vindry C, Lauwers A, Hutin D, Soin R, Wauquier C, Kruys V, Gueydan C.

J Biol Chem. 2012 Oct 12;287(42):35527-38. doi: 10.1074/jbc.M112.356188.


Quantifying Argonaute proteins in and out of GW/P-bodies: implications in microRNA activities.

Leung AK, Sharp PA.

Adv Exp Med Biol. 2013;768:165-82. doi: 10.1007/978-1-4614-5107-5_10. Review.


A complex containing the CCR4 and CAF1 proteins is involved in mRNA deadenylation in Drosophila.

Temme C, Zaessinger S, Meyer S, Simonelig M, Wahle E.

EMBO J. 2004 Jul 21;23(14):2862-71.

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