Evidence map›Paper›PMID 31690658›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Pat1 activates late steps in mRNA decay by multiple mechanisms.

Joseph H Lobel, Ryan W Tibble, John D Gross

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. The mRNA decapping machinery targetsLife science alliance · 2023
    Article
  9. DNA topoisomerase 2-associated proteins PATL1 and PATL2 regulate the biogenesis of hERG KProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Review
  11. Dcp2 C-terminaleLife · 2022
    Article
  12. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Joseph H LobelChemistry and Chemical Biology Graduate Program, University of California, San Francisco, CA 94158.
Ryan W TibbleChemistry and Chemical Biology Graduate Program, University of California, San Francisco, CA 94158.ORCID 0000-0002-4188-3116
John D GrossDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158 jdgross@cgl.ucsf.edu.ORCID 0000-0002-1377-4705
University of California, San Francisco · US

Funding

RESEARCH TRAINING IN CHEMISTRY AND CHEMICAL BIOLOGYT32GM064337 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2002 to 2021
$7.8M
Structure and Function of the Decapping Enzyme ComplexR01GM078360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GROSS, JOHN D · 2009 to 2018
$2.5M
NIGMS NIH HHS R01 GM078360NIGMS NIH HHS T32 GM064337
6 · The paper itself

Abstract

Pat1 is a hub for mRNA metabolism, acting in pre-mRNA splicing, translation repression, and mRNA decay. A critical step in all 5'-3' mRNA decay pathways is removal of the 5' cap structure, which precedes and permits digestion of the RNA body by conserved exonucleases. During bulk 5'-3' decay, the Pat1/Lsm1-7 complex engages mRNA at the 3' end and promotes hydrolysis of the cap structure by Dcp1/Dcp2 at the 5' end through an unknown mechanism. We reconstitute Pat1 with 5' and 3' decay factors and show how it activates multiple steps in late mRNA decay. First, we find that Pat1 stabilizes binding of the Lsm1-7 complex to RNA using two conserved short-linear interaction motifs. Second, Pat1 directly activates decapping by binding elements in the disordered C-terminal extension of Dcp2, alleviating autoinhibition and promoting substrate binding. Our results uncover the molecular mechanism of how separate domains of Pat1 coordinate the assembly and activation of a decapping messenger ribonucleoprotein (mRNP) that promotes 5'-3' mRNA degradation.

Indexed as

RNA StabilityAmino Acid SequenceConserved SequenceModels, MolecularMultiprotein ComplexesNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationProtein DomainsProtein Interaction MappingProtein Serine-Threonine KinasesRecombinant ProteinsRNA-Binding ProteinsRNA CapsRNA, FungalRNA, MessengerDcp1 protein, S pombeDcp2 protein, S pombeMultiprotein ComplexesProtein Serine-Threonine Kinasesran1 protein, S pombeRecombinant ProteinsRNA-Binding ProteinsRNA CapsRNA, FungalRNA, MessengerSchizosaccharomyces pombe ProteinsDcp2decappingmRNA decayPat1short-linear interaction motifs

Identifiers

PMID31690658
PMCPMC6876151
OpenAlexW2985146793

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.