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Subunits of the Drosophila CCR4-NOT complex and their roles in mRNA deadenylation.

Temme C, Zhang L, Kremmer E, Ihling C, Chartier A, Sinz A, Simonelig M, Wahle E.

RNA. 2010 Jul;16(7):1356-70. doi: 10.1261/rna.2145110.


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.


NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain.

Bawankar P, Loh B, Wohlbold L, Schmidt S, Izaurralde E.

RNA Biol. 2013 Feb;10(2):228-44. doi: 10.4161/rna.23018.


The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex.

Petit AP, Wohlbold L, Bawankar P, Huntzinger E, Schmidt S, Izaurralde E, Weichenrieder O.

Nucleic Acids Res. 2012 Nov;40(21):11058-72. doi: 10.1093/nar/gks883.


Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex.

Chen J, Rappsilber J, Chiang YC, Russell P, Mann M, Denis CL.

J Mol Biol. 2001 Dec 7;314(4):683-94.


The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5.

Bai Y, Salvadore C, Chiang YC, Collart MA, Liu HY, Denis CL.

Mol Cell Biol. 1999 Oct;19(10):6642-51.


A role for Caf1 in mRNA deadenylation and decay in trypanosomes and human cells.

Schwede A, Ellis L, Luther J, Carrington M, Stoecklin G, Clayton C.

Nucleic Acids Res. 2008 Jun;36(10):3374-88. doi: 10.1093/nar/gkn108.


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.


Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits.

Albert TK, Lemaire M, van Berkum NL, Gentz R, Collart MA, Timmers HT.

Nucleic Acids Res. 2000 Feb 1;28(3):809-17.


CAF1 plays an important role in mRNA deadenylation separate from its contact to CCR4.

Ohn T, Chiang YC, Lee DJ, Yao G, Zhang C, Denis CL.

Nucleic Acids Res. 2007;35(9):3002-15.


Architecture of the nuclease module of the yeast Ccr4-not complex: the Not1-Caf1-Ccr4 interaction.

Basquin J, Roudko VV, Rode M, Basquin C, Séraphin B, Conti E.

Mol Cell. 2012 Oct 26;48(2):207-18. doi: 10.1016/j.molcel.2012.08.014.


Genome wide expression analysis of the CCR4-NOT complex indicates that it consists of three modules with the NOT module controlling SAGA-responsive genes.

Cui Y, Ramnarain DB, Chiang YC, Ding LH, McMahon JS, Denis CL.

Mol Genet Genomics. 2008 Apr;279(4):323-37. doi: 10.1007/s00438-007-0314-1.


GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets.

Braun JE, Huntzinger E, Fauser M, Izaurralde E.

Mol Cell. 2011 Oct 7;44(1):120-33. doi: 10.1016/j.molcel.2011.09.007.


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.


CCR4-NOT deadenylates mRNA associated with RNA-induced silencing complexes in human cells.

Piao X, Zhang X, Wu L, Belasco JG.

Mol Cell Biol. 2010 Mar;30(6):1486-94. doi: 10.1128/MCB.01481-09.


CUP promotes deadenylation and inhibits decapping of mRNA targets.

Igreja C, Izaurralde E.

Genes Dev. 2011 Sep 15;25(18):1955-67. doi: 10.1101/gad.17136311.


The enzyme activities of Caf1 and Ccr4 are both required for deadenylation by the human Ccr4-Not nuclease module.

Maryati M, Airhihen B, Winkler GS.

Biochem J. 2015 Jul 1;469(1):169-76. doi: 10.1042/BJ20150304.


Systematic mutagenesis of the leucine-rich repeat (LRR) domain of CCR4 reveals specific sites for binding to CAF1 and a separate critical role for the LRR in CCR4 deadenylase activity.

Clark LB, Viswanathan P, Quigley G, Chiang YC, McMahon JS, Yao G, Chen J, Nelsbach A, Denis CL.

J Biol Chem. 2004 Apr 2;279(14):13616-23.


Oskar allows nanos mRNA translation in Drosophila embryos by preventing its deadenylation by Smaug/CCR4.

Zaessinger S, Busseau I, Simonelig M.

Development. 2006 Nov;133(22):4573-83.


Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin.

Sandler H, Kreth J, Timmers HT, Stoecklin G.

Nucleic Acids Res. 2011 May;39(10):4373-86. doi: 10.1093/nar/gkr011.

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