The Ccr4–Not complex

Collart, Martine A.; Panasenko, Olesya O.

doi:10.1016/j.gene.2011.09.033

Cited by 261 publications

(329 citation statements)

References 180 publications

Supporting

Mentioning

322

Contrasting

Unclassified

Order By: Relevance

“…This hypothesis is confirmed by our observation that the second phase of CecA1 mRNA deadenylation occurs in polysomes and is accelerated by overexpressing dTIS11. In agreement with this observation, both the CCR4-CAF1-NOT complex and TTP have been detected in polysomes (38,39). Therefore, the polysomal deadenylation of ARE-containing mRNAs might represent the ancestral function of TIS11 family members, whereas new functions could have emerged in the course of evolution leading to the optimization of AMD.…”

Section: Discussionsupporting

confidence: 66%

dTIS11 Protein-dependent Polysomal Deadenylation Is the Key Step in AU-rich Element-mediated mRNA Decay in Drosophila Cells

Vindry

Lauwers

Hutin

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: TIS11 proteins control the degradation of mRNA containing AU-rich elements (ARE). Results: Drosophila dTIS11 activates the polysomal deadenylation of the ARE mRNA Cecropin A1. Conclusion: Drosophila dTIS11 controls fewer aspects of ARE mRNA decay as compared with its mammalian homologs. Significance: TIS11 proteins may have acquired additional functions to control mRNA decay during evolution from invertebrates to mammals.

show abstract

Section: Discussionsupporting

confidence: 66%

dTIS11 Protein-dependent Polysomal Deadenylation Is the Key Step in AU-rich Element-mediated mRNA Decay in Drosophila Cells

Vindry

Lauwers

Hutin

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…In (A) is shown a schematic representation of NOT1 as a scaffolding protein for a large, multiprotein complex, containing at least 2 deadenylases. This was modified from Collart and Panasenko (2012), with permission. (B) Shows the organization of the NOT1-binding domain in human TTP, and the TTPbinding domain of human NOT1, as identified by the indicated deletions and truncations of the respective fusion proteins.…”

Section: Viruses and Prokaryotesmentioning

confidence: 99%

“…In Fig. 1A, modified from Collart and Panasenko (2012), the central position of NOT1 as the ''scaffold'' of a large complex is shown, along with the known protein interactors, at least 2 of which are deadenylases that are capable of acting on the poly(A) tail. Figure 1B and C, taken from Fabian and others (2013), show the sites of interaction between human TTP and NOT1 (Fig.…”

Section: Introductionmentioning

confidence: 99%

Phylogenetic Distribution and Evolution of the Linked RNA-Binding and NOT1-Binding Domains in the Tristetraprolin Family of Tandem CCCH Zinc Finger Proteins

Blackshear

Perera

2014

Journal of Interferon & Cytokine Research

View full text Add to dashboard Cite

In humans, the tristetraprolin or TTP family of CCCH tandem zinc finger (TZF) proteins comprises 3 members, encoded by the genes ZFP36, ZFP36L1, and ZFP36L2. These proteins have direct orthologues in essentially all vertebrates studied, with the exception of birds, which appear to lack a version of ZFP36. Additional family members are found in rodents, amphibians, and fish. In general, the encoded proteins contain 2 critical macromolecular interaction domains: the CCCH TZF domain, which is necessary for high-affinity binding to AUrich elements in mRNA; and an extreme C-terminal domain that, in the case of TTP, interacts with NOT1, the scaffold of a large multi-protein complex that contains deadenylases. TTP and its related proteins act by first binding to AU-rich elements in mRNA, and then recruiting deadenylases to the mRNA, where they can processively remove the adenosine residues from the poly(A) tail. Highly conserved TZF domains have been found in unicellular eukaryotes such as yeasts, and these domains can bind AU-rich elements that resemble those bound by the mammalian proteins. However, certain fungi appear to lack proteins with intact TZF domains, and the TTP family proteins that are expressed in other fungi often lack the characteristic C-terminal NOT1 binding domain found in the mammalian proteins. For these reasons, we investigated the phylogenetic distribution of the relevant sequences in available databases. Both domains are present in family member proteins from most lineages of eukaryotes, suggesting their mutual presence in a common ancestor. However, the vertebrate type of NOT1-binding domain is missing in most fungi, and the TZF domain itself has disappeared or degenerated in recently evolved fungi. Nonetheless, both domains are present together in the proteins from several unicellular eukaryotes, including at least 1 fungus, and they seem to have remained together during the evolution of metazoans.

show abstract

“…This process is carried out by Pan2/3 and Ccr4 in yeast, with Ccr4 appearing to play the major role (9 -11). Ccr4 resides in a multisubunit complex called Ccr4-Not, which was first described as a transcriptional activator/ repressor (9,12). In addition to regulating the TATA-binding protein at the initiation stage, it directly associates with elongating RNA polymerase II (RNAPII) 2 and can reactivate arrested polymerase in vitro (13,14).…”

mentioning

confidence: 99%

The Rpb4/7 Module of RNA Polymerase II Is Required for Carbon Catabolite Repressor Protein 4-Negative on TATA (Ccr4-Not) Complex to Promote Elongation

Babbarwal

Reese

2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: mRNA transcription and decay are coordinated processes. Results: The Rpb4/7 module of RNA polymerase II is required for the transcription and mRNA decay factor Ccr4-Not to associate with elongation complexes. Conclusion: Association between these two entities is required for Ccr4-Not to promote transcription elongation. Significance: Our work provides molecular insights into how transcription and mRNA decay are linked.

show abstract

The Ccr4–Not complex

Cited by 261 publications

References 180 publications

dTIS11 Protein-dependent Polysomal Deadenylation Is the Key Step in AU-rich Element-mediated mRNA Decay in Drosophila Cells

dTIS11 Protein-dependent Polysomal Deadenylation Is the Key Step in AU-rich Element-mediated mRNA Decay in Drosophila Cells

Phylogenetic Distribution and Evolution of the Linked RNA-Binding and NOT1-Binding Domains in the Tristetraprolin Family of Tandem CCCH Zinc Finger Proteins

The Rpb4/7 Module of RNA Polymerase II Is Required for Carbon Catabolite Repressor Protein 4-Negative on TATA (Ccr4-Not) Complex to Promote Elongation

Contact Info

Product

Resources

About