ArticleRNA (New York, N.Y.)2015
Xenopus CAF1 requires NOT1-mediated interaction with 4E-T to repress translation in vivo.
Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- Remodeling of Germ Cell mRNPs for Translational Control.Biology · 2025Review
- Optimized Analysis of Proteins from Xenopus Oocytes and Embryos by Immunoblotting.Journal of visualized experiments : JoVE · 2025Article
- Translational repression by 4E-T is crucial to maintain the prophase-I arrest in vertebrate oocytes.Nature communications · 2025Article
- Condensate-forming eIF4ET ensures adequate levels of meiotic proteins to support oocyte storage.Life science alliance · 2025Article
- RNA-binding proteins DND1 and NANOS3 cooperatively suppress the entry of germ cell lineage.Nature communications · 2025Article
- Roles of the CCR4-Not complex in translation and dynamics of co-translation events.Wiley interdisciplinary reviews. RNA · 2023Review
- RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system.Nucleic acids research · 2023Article
- RNF219 regulates CCR4-NOT function in mRNA translation and deadenylation.Scientific reports · 2022Article
- Human Pumilio proteins directly bind the CCR4-NOT deadenylase complex to regulate the transcriptome.RNA (New York, N.Y.) · 2021Article
- Differential processing and localization of human Nocturnin controls metabolism of mRNA and nicotinamide adenine dinucleotide cofactors.The Journal of biological chemistry · 2020Article
- 4E-T-bound mRNAs are stored in a silenced and deadenylated form.Genes & development · 2020Article
- Unique repression domains of Pumilio utilize deadenylation and decapping factors to accelerate destruction of target mRNAs.Nucleic acids research · 2020Article
- Regulation of Germ Cell mRNPs by eIF4E:4EIP Complexes: Multiple Mechanisms, One Goal.Frontiers in cell and developmental biology · 2020Review
- Mechanistic Insights into MicroRNA-Mediated Gene Silencing.Cold Spring Harbor perspectives in biology · 2019Review
- The structure of human Nocturnin reveals a conserved ribonuclease domain that represses target transcript translation and abundance in cells.Nucleic acids research · 2018Article
- MicroRNAs from plants to animals, do they define a new messenger for communication?Nutrition & metabolism · 2018Review
- Combinatorial control of messenger RNAs by Pumilio, Nanos and Brain Tumor Proteins.RNA biology · 2017Article
- Translational repression of theRNA (New York, N.Y.) · 2017Article
- Alternative splicing of CNOT7 diversifies CCR4-NOT functions.Nucleic acids research · 2017Article
- Cap-binding protein 4EHP effects translation silencing by microRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
RNA-regulatory factors bound to 3' UTRs control translation and stability. Repression often is associated with poly(A) removal. The deadenylase CAF1 is a core component of the CCR4-NOT complex. Our prior studies established that CAF1 represses translation independent of deadenylation. We sought the mechanism of its deadenylation-independent repression in Xenopus oocytes. Our data reveal a chain of interacting proteins that links CAF1 to CCR4-NOT and to Xp54 and 4E-T. Association of CAF1 with NOT1, the major subunit of CCR4-NOT, is required for repression by CAF1 tethered to a reporter mRNA. Affinity purification-mass spectrometry and coimmunoprecipitation revealed that at least five members of the CCR4-NOT complex were recruited by CAF1. The recruitment of these proteins required NOT1, as did the ability of tethered CAF1 to repress translation. In turn, NOT1 was needed to recruit Xp54 and 4E-T. We examined the role of 4E-T in repression using mutations that disrupted either eIF4E-dependent or -independent mechanisms. Expression of a 4E-T truncation that still bound eIF4E alleviated repression by tethered CAF1, NOT1, and Xp54. In contrast, a mutant 4E-T that failed to bind eIF4E did not. Repression of global translation was affected only by the eIF4E-dependent mechanism. Reporters bearing IRES elements revealed that repression via tethered CAF1 and Xp54 is cap- and eIF4E-independent, but requires one or more of eIF4A, eIF4B, and eIF4G. We propose that RNA-binding proteins, and perhaps miRNAs, repress translation through an analogous chain of interactions that begin with the 3' UTR-bound repressor and end with the noncanonical activity of 4E-T.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.