ArticleProceedings of the National Academy of Sciences of the United States of America2017
A unique surface on Pat1 C-terminal domain directly interacts with Dcp2 decapping enzyme and Xrn1 5'-3' mRNA exonuclease in yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 67 citations in OpenAlex.
- The CCR4-NOT complex: a multifaceted sensor of molecular signals instructing eukaryotic mRNA translation and stability.Nucleic acids research · 2025Review
- Article
- RNA anchoring of Upf1 facilitates recruitment of Dcp2 in the NMD decapping complex.Nucleic acids research · 2025Article
- The ribosome as a platform to coordinate mRNA decay.Nucleic acids research · 2025Review
- Biochemical analysis of human eIF4E-DCP2 interaction: Implications for the relationship between translation initiation and decapping.PloS one · 2025Article
- Modeling of mRNA deadenylation rates reveal a complex relationship between mRNA deadenylation and decay.The EMBO journal · 2024Article
- Human DCP1 is crucial for mRNA decapping and possesses paralog-specific gene regulating functions.eLife · 2024Article
- Eukaryotic mRNA decapping factors: molecular mechanisms and activity.The FEBS journal · 2023Review
- mRNA decapping activators Pat1 and Dhh1 regulate transcript abundance and translation to tune cellular responses to nutrient availability.Nucleic acids research · 2023Article
- The mRNA decapping machinery targetsLife science alliance · 2023Article
- A unique mRNA decapping complex in trypanosomes.Nucleic acids research · 2023Article
- Article
- Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Decapping factor Dcp2 controls mRNA abundance and translation to adjust metabolism and filamentation to nutrient availability.bioRxiv : the preprint server for biology · 2023Article
- Structure and function of molecular machines involved in deadenylation-dependent 5'-3' mRNA degradation.Frontiers in genetics · 2023Review
- Dcp2 C-terminaleLife · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- Making ends meet: New functions of mRNA secondary structure.Wiley interdisciplinary reviews. RNA · 2021Review
- Pdc2/Pat1 increases the range of decay factors and RNA bound by the Lsm1-7 complex.RNA (New York, N.Y.) · 2020Article
- Pby1 is a direct partner of the Dcp2 decapping enzyme.Nucleic acids research · 2020Article
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Pat1 protein is a central player of eukaryotic mRNA decay that has also been implicated in translational control. It is commonly considered a central platform responsible for the recruitment of several RNA decay factors. We demonstrate here that a yeast-specific C-terminal region from Pat1 interacts with several short motifs, named helical leucine-rich motifs (HLMs), spread in the long C-terminal region of yeast Dcp2 decapping enzyme. Structures of Pat1-HLM complexes reveal the basis for HLM recognition by Pat1. We also identify a HLM present in yeast Xrn1, the main 5'-3' exonuclease involved in mRNA decay. We show further that the ability of yeast Pat1 to bind HLMs is required for efficient growth and normal mRNA decay. Overall, our analyses indicate that yeast Pat1 uses a single binding surface to successively recruit several mRNA decay factors and show that interaction between those factors is highly polymorphic between species.
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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.