The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The gene/protein reviewed here is budding yeast Pop2/Caf1, a core subunit of the CCR4–NOT complex. Primary literature explicitly equates CAF1 with POP2 in S. cerevisiae and places it in the major cytoplasmic mRNA deadenylase complex with Ccr4 (tucker2001thetranscriptionfactor pages 2-3, ohn2007caf1playsan pages 1-1). The reviewed function and domains are consistent with UniProt P39008 as an RNase D/CAF1-family nuclease-module component (thore2003x‐raystructureand pages 2-4, basquin2012architectureofthe pages 1-2).
Pop2 (also called Caf1) is a conserved CAF1-family protein that functions within the CCR4–NOT complex, a central regulator of eukaryotic mRNA turnover and gene expression. In yeast, Pop2/Caf1 is part of the nuclease module that executes deadenylation, i.e., poly(A)-tail shortening that represses translation and promotes downstream mRNA decay steps (basquin2012architectureofthe pages 1-2, tucker2001thetranscriptionfactor pages 2-3).
Deadenylases are commonly described as 3′→5′ exoribonucleases that hydrolyze poly(A) tails and (in general description) lead to release of 5′-AMP, and they are often described as magnesium-dependent enzymes (review-level synthesis) (bartlam2010thestructuralbasis pages 3-4, hagkarim2020theregulatoryproperties pages 5-6). In CCR4–NOT, the two catalytic subunits are Ccr4 (EEP family) and Caf1/Pop2 (DEDD/RNase D family) (hagkarim2020theregulatoryproperties pages 5-6, basquin2012architectureofthe pages 1-2).
A classic yeast reporter pulse–chase study showed that CCR4 and CAF1 gene products are required for normal rates of deadenylation in vivo, and that they localize primarily to the cytoplasm where mRNA turnover occurs (tucker2001thetranscriptionfactor pages 2-3). Quantitatively, in wild-type cells the MFA2pG poly(A) tail shortens at ~13 nt/min, while in ccr4Δ and caf1Δ strains deadenylation proceeds at only ~2–3 nt/min, and the reporter mRNA is stabilized ~2–3-fold (tucker2001thetranscriptionfactor pages 2-3). These data support Pop2/Caf1 as an essential component for normal kinetics of cytoplasmic deadenylation.
Structural work on the yeast nuclease module established an architectural model in which Not1 is the scaffold, its central MIF4G-like domain binds Caf1, and Caf1 binds the LRR domain of Ccr4, thereby tethering the Ccr4 nuclease domain within the complex (basquin2012architectureofthe pages 1-2). This architecture explains why Pop2/Caf1 can have strong functional effects on deadenylation even when its own catalytic contribution is context-dependent.
A clear in vivo example of this “mediating/tethering” function is found in rDNA stability regulation: Pop2 presence (but not its catalytic activity) is required because Pop2 is needed for tethering Ccr4 to the complex, and pop2Δ causes the complex to lose both Pop2 and Ccr4 (hosoyamada2020theccr4notcomplex pages 3-4).
A high-impact structural/biochemical study solved the X-ray structure of the Pop2 RNase D domain and demonstrated that purified Pop2 displays in vitro RNase activity (thore2003x‐raystructureand pages 2-4). Substrate testing showed activity toward poly(A) and also poly(U) and poly(C), but not oligo(G), with competition assays indicating a subtle preference for poly(A); cleavage proceeded in a distributive manner (progressive appearance of shorter fragments) (thore2003x‐raystructureand pages 2-4).
Active-site residues: Mutation of residues S44A and E46A (within the DEDD-motif region described for the family/active site) abolished detectable activity in vitro, strongly linking the catalytic activity to the Pop2 RNase D domain (thore2003x‐raystructureand pages 2-4).
Metal-ion context: The Pop2 structure crystallized with two calcium ions, and the authors discuss the canonical DEDD mechanism (two-metal-ion catalysis in related nucleases) while also raising that Pop2 might bind only one metal under some conditions; the active-site magnesium is discussed as relevant for catalysis (thore2003x‐raystructureand pages 2-4).
Multiple sources highlight a tension: Pop2/Caf1 has measurable intrinsic nuclease activity in vitro (thore2003x‐raystructureand pages 2-4, ohn2007caf1playsan pages 1-2), yet multiple yeast genetic studies argue that Pop2 catalytic activity is not strictly required for key in vivo outputs, with Ccr4 being the primary catalytic deadenylase in budding yeast.
A coherent synthesis consistent with the above is that Pop2/CAF1 contributes both (i) architectural/assembly functions that enable Ccr4 action and targeting, and (ii) an intrinsic RNase activity whose quantitative contribution to in vivo poly(A) removal is condition- and substrate-dependent (basquin2012architectureofthe pages 1-2, ohn2007caf1playsan pages 1-2, hosoyamada2020theccr4notcomplex pages 3-4).
Ccr4p and Caf1p localize primarily to the cytoplasm, consistent with a direct role in cytoplasmic mRNA deadenylation and turnover (tucker2001thetranscriptionfactor pages 2-3).
Under stress, CCR4–NOT subunits including Ccr4 and Pop2 can relocalize to processing bodies (P-bodies), whereas they are not prominent P-body residents in unstressed cells (miller2012ccr4notcomplexthe pages 12-13). Deletion of CCR4 or POP2 causes only a minor reduction in P-body formation, suggesting recruitment but not strict necessity for foci assembly (miller2012ccr4notcomplexthe pages 12-13).
The canonical yeast model places deadenylation upstream of decapping and 5′→3′ decay. Recent work emphasizes that this coupling is not universal for all transcripts and is context-dependent.
A 2024 EMBO Journal study modeled yeast poly(A) tail kinetics and concluded that changes in poly(A)-tail length do not necessarily correlate with stability for most mRNAs, suggesting deadenylation may be critical for specific programs rather than globally rate-limiting (lena2024rnadegradationtriggered pages 1-2).
Complementarily, another 2024 EMBO Journal paper using nanopore direct RNA sequencing and modeling estimated a transcriptome-wide deadenylation rate of ~10 A/min and reported that deadenylation/decay relationships vary with functional groups and stress conditions; ribosomal protein mRNAs constitute ~40% of the transcriptome and show distinct behavior under heat stress (czarnockacieciura2024modelingofmrna pages 1-2).
Together, these 2024 studies represent a major development in the field: Pop2/Caf1-containing CCR4–NOT remains central to deadenylation, but the extent to which deadenylation dictates decay depends on transcript class and physiological state (lena2024rnadegradationtriggered pages 1-2, czarnockacieciura2024modelingofmrna pages 1-2).
A 2023 study reported that the Ccr4–Not complex in S. cerevisiae has bidirectional roles in autophagy across nutrient conditions. Under nutrient-rich conditions, Ccr4–Not directly targets ATG mRNAs in core autophagy machinery to promote their degradation through deadenylation, maintaining basal autophagy; after nitrogen starvation, it releases repression and promotes expression of a different ATG subset needed for induction (yin2023bidirectionalrolesof pages 1-2). Quantitatively, depletion of Ccr4 increased several ATG mRNAs by ~50% in the cited experiment (ATG1, ATG7, ATG9, ATG19) (yin2023bidirectionalrolesof pages 1-2). Because Pop2/Caf1 is explicitly part of the yeast Ccr4–Not deadenylase module, Pop2 is implicated as a necessary module component in this regulatory mode (yin2023bidirectionalrolesof pages 1-2, basquin2012architectureofthe pages 1-2).
A 2020 study identified pop2Δ as producing the highest level of extrachromosomal rDNA circles (ERCs) among tested mutants, with ERC accumulation ~50-fold above wild type and ~4-fold above sir2 (hosoyamada2020theccr4notcomplex pages 3-4). In pop2 mutants, E-pro noncoding transcripts accumulate, cohesin/condensin association is reduced, and rRNA amount is reduced to ~half of wild-type (hosoyamada2020theccr4notcomplex pages 3-4). Importantly, catalytic-dead Pop2 rescues rDNA instability, supporting a mediating role, whereas catalytic activity of Ccr4 is essential (hosoyamada2020theccr4notcomplex pages 3-4).
Genetic evidence links CCR4–NOT to transcription elongation phenotypes. A 2001 Genetics paper reported that caf1 mutations give rise to a 6-azauracil (6AU) phenotype, and ccr4, caf1, and not4 deletions confer mycophenolic acid sensitivity, both classic hallmarks of elongation-associated defects (denis2001geneticevidencesupports pages 2-3). These phenotypes can be rescued by excess guanine, consistent with the known mechanism of 6AU/MPA reducing nucleotide pools and stressing elongation (denis2001geneticevidencesupports pages 2-3).
Pop2/Caf1 is widely used as a functional entry point into:
* mRNA stability engineering (modulating deadenylation to tune transcript lifetimes) based on the established cytoplasmic deadenylase role of Ccr4/Caf1 (tucker2001thetranscriptionfactor pages 2-3).
* Stress granule/P-body biology and stress-regulated mRNA fate, given stress-dependent recruitment of Pop2/Ccr4 to P-bodies (miller2012ccr4notcomplexthe pages 12-13).
* Autophagy control mechanisms via post-transcriptional regulation of ATG gene expression (yin2023bidirectionalrolesof pages 1-2).
While these are primarily research implementations rather than industrial products, they represent real-world, routinely deployed experimental strategies in molecular biology.
The following table consolidates key functional-annotation claims, methods, quantitative data, and source metadata:
| Functional aspect | Key finding | Evidence type | Experimental/analysis approach | Quantitative data | Source (paper; year; publication date if available; URL) | Citation ID |
|---|---|---|---|---|---|---|
| Complex role | Pop2/Caf1 is a core subunit of the major cytoplasmic Ccr4-Not deadenylase, and both Ccr4p and Caf1p are required for normal deadenylation in vivo. | Primary | Reporter mRNA transcriptional pulse-chase; biochemical copurification | MFA2pG deadenylation in WT ~13 nt/min vs ~2–3 nt/min in ccr4Δ and caf1Δ; MFA2pG stabilized ~2–3-fold in mutants | Tucker et al., Cell, 2001, Feb; https://doi.org/10.1016/S0092-8674(01)00225-2 | (tucker2001thetranscriptionfactor pages 2-3) |
| Complex architecture | Not1 acts as scaffold; its central MIF4G-like domain binds Caf1, and Caf1 binds the Ccr4 LRR domain to tether the Ccr4 nuclease into the nuclease module. | Primary | Structural biology of yeast nuclease module | Multiprotein complex mass ~1 MDa noted; no catalytic rate reported | Basquin et al., Molecular Cell, 2012, Oct 26; https://doi.org/10.1016/j.molcel.2012.08.014 | (basquin2012architectureofthe pages 1-2) |
| Enzymatic activity | The Pop2 RNase D domain has intrinsic in vitro RNase activity, supporting its annotation as a poly(A) ribonuclease/deadenylase subunit. | Primary | X-ray crystallography plus in vitro RNase assays with purified domain | Structure solved at 2.3 Å; catalytic loss in S44A/E46A mutant | Thore et al., EMBO Reports, 2003, Dec; https://doi.org/10.1038/sj.embor.7400020 | (thore2003x‐raystructureand pages 4-6, thore2003x‐raystructureand pages 2-4) |
| Substrate specificity | Pop2 degrades poly(A) and also poly(U)/poly(C) in vitro, but not oligo(G), indicating preference for poly(A) with broader RNA reactivity than a strict poly(A)-only enzyme. | Primary | In vitro RNase substrate panel and competition assays | Active on poly(A), poly(U), poly(C); inactive on oligo(G); distributive cleavage pattern | Thore et al., EMBO Reports, 2003, Dec; https://doi.org/10.1038/sj.embor.7400020 | (thore2003x‐raystructureand pages 2-4) |
| Catalytic residues/domain | Pop2 belongs to the RNase D/DEDD family; mutating S44 and E46 in the active-site motif abolishes detectable RNase activity. | Primary | Structure-guided mutagenesis and enzymatic assay | S44A/E46A abolishes activity | Thore et al., EMBO Reports, 2003, Dec; https://doi.org/10.1038/sj.embor.7400020 | (thore2003x‐raystructureand pages 2-4, thore2003x‐raystructureand pages 4-6) |
| In vivo functional interpretation | Although Pop2 has intrinsic nuclease activity in vitro, genetic work in budding yeast suggests Ccr4 is the primary catalytic deadenylase in vivo and Pop2 also contributes through noncatalytic functions. | Primary | Mutagenesis, in vivo deadenylation assays, genetic interaction analysis | caf1Δ causes deadenylation defect but less severe than ccr4Δ; catalytic-site inactivation of CAF1 did not abolish in vivo function | Ohn et al., Nucleic Acids Research, 2007, Apr; https://doi.org/10.1093/nar/gkm196 | (ohn2007caf1playsan pages 1-1, ohn2007caf1playsan pages 1-2) |
| Localization | Ccr4p and Caf1p localize primarily to the cytoplasm, consistent with a direct role in cytoplasmic mRNA turnover. | Primary | Subcellular localization in yeast coupled to mRNA decay assays | No specific fraction percentage reported | Tucker et al., Cell, 2001, Feb; https://doi.org/10.1016/S0092-8674(01)00225-2 | (tucker2001thetranscriptionfactor pages 2-3) |
| Stress localization | Under stress, Ccr4-Not subunits including Pop2/Caf1 can relocalize to P-bodies, whereas in unstressed cells Pop2/Ccr4 are not prominent P-body residents during ongoing decay. | Review | Synthesis of microscopy/localization literature | Deletion of CCR4 or POP2 causes only minor reduction in P-body formation | Miller & Reese, Crit Rev Biochem Mol Biol, 2012, Jun; https://doi.org/10.3109/10409238.2012.667214 | (miller2012ccr4notcomplexthe pages 12-13) |
| Deadenylation mechanism | Expert synthesis indicates Caf1 acts mainly on exposed/naked poly(A), is blocked by Pab1, and cannot efficiently proceed past non-A residues, whereas Ccr4 trims Pab1-protected poly(A). | Review | Comparative biochemical/structural review | Pan2/Pan3 acts on tails >150 nt; combined Ccr4/Caf1 action yields ~27-nt periodic decrements | Hagkarim & Grand, Cells, 2020, Oct; https://doi.org/10.3390/cells9112379 | (hagkarim2020theregulatoryproperties pages 5-6) |
| Mutant phenotype: transcription elongation | caf1/pop2 mutants show 6-azauracil sensitivity and mycophenolic-acid sensitivity, supporting a genetic connection between CCR4-NOT and transcription elongation control. | Primary | Drug-sensitivity genetics | Qualitative 6AU and MPA sensitivity; rescue by excess guanine reported for CCR4-NOT defects | Denis et al., Genetics, 2001, Jun; https://doi.org/10.1093/genetics/158.2.627 | (denis2001geneticevidencesupports pages 2-3, denis2001geneticevidencesupports pages 1-2) |
| Mutant phenotype: rDNA stability | pop2Δ causes severe rDNA instability, accumulation of extrachromosomal rDNA circles, elevated E-pro noncoding RNA, and reduced rRNA, linking Pop2/Caf1 to rDNA maintenance. | Primary | PFGE, Southern/ERC assay, mutant reconstruction | ERCs ~50-fold above WT and ~4-fold above sir2; rRNA reduced to about half of WT | Hosoyamada et al., Molecular and Cellular Biology, 2020, Jan; https://doi.org/10.1128/MCB.00320-19 | (hosoyamada2020theccr4notcomplex pages 3-4) |
| Mediating/tethering role in rDNA pathway | In rDNA maintenance, Pop2 presence rather than Pop2 catalytic activity is needed because Pop2 tethers Ccr4 to the complex; pop2 deletion removes both Pop2 and Ccr4-associated deadenylase activity. | Primary | Catalytic-dead allele complementation with chromosomal phenotype readout | pop2 S44A,E46A complements rDNA instability, whereas ccr4 E556A does not | Hosoyamada et al., Molecular and Cellular Biology, 2020, Jan; https://doi.org/10.1128/MCB.00320-19 | (hosoyamada2020theccr4notcomplex pages 3-4) |
| Pathway role: autophagy | The yeast Ccr4-Not complex, containing Pop2/Caf1, directly deadenylates specific ATG mRNAs under nutrient-rich conditions to restrain basal autophagy and switches roles after nitrogen starvation to support induction. | Primary | Auxin-inducible depletion, ATG mRNA measurements, autophagy assays | Approx. 50% increase in ATG1, ATG7, ATG9, and ATG19 mRNAs upon Ccr4 depletion in the cited experiment | Yin et al., Autophagy, 2023, Feb; https://doi.org/10.1080/15548627.2022.2036476 | (yin2023bidirectionalrolesof pages 1-2) |
| Recent quantitative estimate | Transcriptome-wide direct RNA sequencing/modeling in yeast estimated a global cytoplasmic deadenylation rate of about 10 A/min, providing a current systems-level benchmark for Ccr4-Not/Pan2/3-driven deadenylation. | Primary | Nanopore direct RNA sequencing and mathematical modeling | Transcriptomic deadenylation rate estimated at 10 A/min; RPG mRNAs constitute ~40% of transcriptome | Czarnocka-Cieciura et al., The EMBO Journal, 2024, published online Oct 11; https://doi.org/10.1038/s44318-024-00258-3 | (czarnockacieciura2024modelingofmrna pages 1-2) |
| Recent systems-level reinterpretation | Rapid depletion experiments indicate that for many yeast mRNAs, poly(A)-tail perturbation does not correlate strongly with stability, implying Pop2/Caf1-mediated deadenylation is critical for selected regulatory programs rather than universally rate-limiting decay. | Primary | Rapid depletion of deadenylases/decapping enzymes; transcriptome-wide poly(A) and stability measurements | Oligoadenylated states can vary by up to ~1000-fold in degradation speed across mRNAs (reviewed in introduction/context) | Audebert et al., The EMBO Journal, 2024, published online Sep 25; https://doi.org/10.1038/s44318-024-00250-x | (lena2024rnadegradationtriggered pages 1-2) |
Table: This table compiles key functional annotation evidence for the Saccharomyces cerevisiae Pop2/Caf1 protein (UniProt P39008), covering its CCR4-NOT complex role, catalytic properties, localization, mutant phenotypes, pathway functions, and recent quantitative systems-level estimates. It is useful as a concise evidence map linking specific claims to experimental approaches and citable sources.
Primary molecular function: component of CCR4–NOT deadenylase; supports cytoplasmic poly(A)-tail shortening and mRNA turnover, acting as both (i) a nuclease-module component with intrinsic RNase D/DEDD-family activity, and (ii) a scaffold/tether enabling Ccr4 integration and function (tucker2001thetranscriptionfactor pages 2-3, basquin2012architectureofthe pages 1-2, thore2003x‐raystructureand pages 2-4, hosoyamada2020theccr4notcomplex pages 3-4).
Reaction and substrates: Pop2/Caf1 is associated with 3′→5′ deadenylation of poly(A) tails (general deadenylase mechanism described as Mg2+-dependent, producing 5′-AMP), and purified Pop2 shows in vitro RNase activity with preference for poly(A) but activity on poly(U)/poly(C) and not oligo(G) (bartlam2010thestructuralbasis pages 3-4, hagkarim2020theregulatoryproperties pages 5-6, thore2003x‐raystructureand pages 2-4).
Localization: primarily cytoplasmic; can accumulate in P-bodies under stress (tucker2001thetranscriptionfactor pages 2-3, miller2012ccr4notcomplexthe pages 12-13).
Pathways/processes: mRNA decay and translation-coupled regulation; autophagy control via ATG mRNA deadenylation; rDNA stability via repression of E-pro antisense transcripts; genetic linkage to transcription elongation stress (6AU/MPA sensitivity) (yin2023bidirectionalrolesof pages 1-2, hosoyamada2020theccr4notcomplex pages 3-4, denis2001geneticevidencesupports pages 2-3).
Some mechanistic uncertainty remains about how much Pop2’s intrinsic catalytic activity contributes to bulk poly(A) removal in vivo, because strong in vitro activity is observed for the RNase D domain and is abolished by S44A/E46A, yet multiple in vivo studies find Pop2 catalytic activity dispensable for at least some cellular phenotypes (mRNA poly(A) removal and rDNA maintenance), consistent with a dominant tethering/scaffold function and a primary catalytic role for Ccr4 in budding yeast (thore2003x‐raystructureand pages 2-4, ohn2007caf1playsan pages 1-2, hosoyamada2020theccr4notcomplex pages 3-4, bartlam2010thestructuralbasis pages 3-4).
References
(tucker2001thetranscriptionfactor pages 2-3): Morgan Tucker, Marco A Valencia-Sanchez, Robin R Staples, Junji Chen, Clyde L Denis, and Roy Parker. The transcription factor associated ccr4 and caf1 proteins are components of the major cytoplasmic mrna deadenylase in saccharomyces cerevisiae. Cell, 104:377-386, Feb 2001. URL: https://doi.org/10.1016/s0092-8674(01)00225-2, doi:10.1016/s0092-8674(01)00225-2. This article has 784 citations and is from a highest quality peer-reviewed journal.
(ohn2007caf1playsan pages 1-1): Takbum Ohn, Yueh-Chin Chiang, Darren J. Lee, Gang Yao, Chongxu Zhang, and Clyde L. Denis. Caf1 plays an important role in mrna deadenylation separate from its contact to ccr4. Nucleic Acids Research, 35:3002-3015, Apr 2007. URL: https://doi.org/10.1093/nar/gkm196, doi:10.1093/nar/gkm196. This article has 45 citations and is from a highest quality peer-reviewed journal.
(thore2003x‐raystructureand pages 2-4): Stéphane Thore, Fabienne Mauxion, Bertrand Séraphin, and Dietrich Suck. X‐ray structure and activity of the yeast pop2 protein: a nuclease subunit of the mrna deadenylase complex. The EMBO Reports, 4(12):1150-1155, Dec 2003. URL: https://doi.org/10.1038/sj.embor.7400020, doi:10.1038/sj.embor.7400020. This article has 151 citations.
(basquin2012architectureofthe pages 1-2): Jérôme Basquin, Vladimir V. Roudko, Michaela Rode, Claire Basquin, Bertrand Séraphin, and Elena Conti. Architecture of the nuclease module of the yeast ccr4-not complex: the not1-caf1-ccr4 interaction. Molecular cell, 48 2:207-18, Oct 2012. URL: https://doi.org/10.1016/j.molcel.2012.08.014, doi:10.1016/j.molcel.2012.08.014. This article has 198 citations and is from a highest quality peer-reviewed journal.
(bartlam2010thestructuralbasis pages 3-4): Mark Bartlam and Tadashi Yamamoto. The structural basis for deadenylation by the ccr4-not complex. Protein & Cell, 1:443-452, Jun 2010. URL: https://doi.org/10.1007/s13238-010-0060-8, doi:10.1007/s13238-010-0060-8. This article has 99 citations and is from a peer-reviewed journal.
(hagkarim2020theregulatoryproperties pages 5-6): Nafiseh Chalabi Hagkarim and Roger J. Grand. The regulatory properties of the ccr4–not complex. Cells, 9:2379, Oct 2020. URL: https://doi.org/10.3390/cells9112379, doi:10.3390/cells9112379. This article has 88 citations.
(hosoyamada2020theccr4notcomplex pages 3-4): Shun Hosoyamada, Mariko Sasaki, and Takehiko Kobayashi. The ccr4-not complex maintains stability and transcription of rrna genes by repressing antisense transcripts. Molecular and Cellular Biology, Jan 2020. URL: https://doi.org/10.1128/mcb.00320-19, doi:10.1128/mcb.00320-19. This article has 21 citations and is from a domain leading peer-reviewed journal.
(ohn2007caf1playsan pages 1-2): Takbum Ohn, Yueh-Chin Chiang, Darren J. Lee, Gang Yao, Chongxu Zhang, and Clyde L. Denis. Caf1 plays an important role in mrna deadenylation separate from its contact to ccr4. Nucleic Acids Research, 35:3002-3015, Apr 2007. URL: https://doi.org/10.1093/nar/gkm196, doi:10.1093/nar/gkm196. This article has 45 citations and is from a highest quality peer-reviewed journal.
(ohn2007caf1playsan pages 13-14): Takbum Ohn, Yueh-Chin Chiang, Darren J. Lee, Gang Yao, Chongxu Zhang, and Clyde L. Denis. Caf1 plays an important role in mrna deadenylation separate from its contact to ccr4. Nucleic Acids Research, 35:3002-3015, Apr 2007. URL: https://doi.org/10.1093/nar/gkm196, doi:10.1093/nar/gkm196. This article has 45 citations and is from a highest quality peer-reviewed journal.
(miller2012ccr4notcomplexthe pages 12-13): Jason E. Miller and Joseph C. Reese. Ccr4-not complex: the control freak of eukaryotic cells. Critical Reviews in Biochemistry and Molecular Biology, 47:315-333, Jun 2012. URL: https://doi.org/10.3109/10409238.2012.667214, doi:10.3109/10409238.2012.667214. This article has 222 citations and is from a peer-reviewed journal.
(lena2024rnadegradationtriggered pages 1-2): Léna Audebert, Frank Feuerbach, Mostafa Zedan, Alexandra P. Schürch, Laurence Decourty, Abdelkader Namane, Emmanuelle Permal, Karsten Weis, Gwenaël Badis, and Cosmin Saveanu. Rna degradation triggered by decapping is largely independent of initial deadenylation. The EMBO Journal, 43:6496-6524, Sep 2024. URL: https://doi.org/10.1038/s44318-024-00250-x, doi:10.1038/s44318-024-00250-x. This article has 12 citations.
(czarnockacieciura2024modelingofmrna pages 1-2): Agnieszka Czarnocka-Cieciura, Jarosław Poznański, Matti Turtola, Rafał Tomecki, Paweł S Krawczyk, Seweryn Mroczek, Wiktoria Orzeł, Upasana Saha, Torben Heick Jensen, Andrzej Dziembowski, and Agnieszka Tudek. Modeling of mrna deadenylation rates reveal a complex relationship between mrna deadenylation and decay. The EMBO Journal, 43:6525-6554, Oct 2024. URL: https://doi.org/10.1038/s44318-024-00258-3, doi:10.1038/s44318-024-00258-3. This article has 9 citations.
(yin2023bidirectionalrolesof pages 1-2): Zhangyuan Yin, Zhihai Zhang, Yuchen Lei, and Daniel J. Klionsky. Bidirectional roles of the ccr4-not complex in regulating autophagy before and after nitrogen starvation. Autophagy, 19:415-425, Feb 2023. URL: https://doi.org/10.1080/15548627.2022.2036476, doi:10.1080/15548627.2022.2036476. This article has 8 citations and is from a domain leading peer-reviewed journal.
(denis2001geneticevidencesupports pages 2-3): Clyde L Denis, Yueh-Chin Chiang, Yajun Cui, and Junji Chen. Genetic evidence supports a role for the yeast ccr4-not complex in transcriptional elongation. Genetics, 158:627-634, Jun 2001. URL: https://doi.org/10.1093/genetics/158.2.627, doi:10.1093/genetics/158.2.627. This article has 101 citations and is from a domain leading peer-reviewed journal.
(thore2003x‐raystructureand pages 4-6): Stéphane Thore, Fabienne Mauxion, Bertrand Séraphin, and Dietrich Suck. X‐ray structure and activity of the yeast pop2 protein: a nuclease subunit of the mrna deadenylase complex. The EMBO Reports, 4(12):1150-1155, Dec 2003. URL: https://doi.org/10.1038/sj.embor.7400020, doi:10.1038/sj.embor.7400020. This article has 151 citations.
(denis2001geneticevidencesupports pages 1-2): Clyde L Denis, Yueh-Chin Chiang, Yajun Cui, and Junji Chen. Genetic evidence supports a role for the yeast ccr4-not complex in transcriptional elongation. Genetics, 158:627-634, Jun 2001. URL: https://doi.org/10.1093/genetics/158.2.627, doi:10.1093/genetics/158.2.627. This article has 101 citations and is from a domain leading peer-reviewed journal.