Evidence map›Paper›PMID 29510985›Full record

ArticleThe EMBO journal2018

Molecular architecture of LSM14 interactions involved in the assembly of mRNA silencing complexes.

Tobias Brandmann, Hana Fakim, Zoya Padamsi, Ji-Young Youn, Anne-Claude Gingras, Marc R Fabian, Martin Jinek

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

50 citing papers in PubMed, 87 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

Tobias BrandmannDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Hana FakimDepartment of Oncology, McGill University, Montreal, QC, Canada.ORCID 0000-0002-9751-7908
Zoya PadamsiDepartment of Oncology, McGill University, Montreal, QC, Canada.
Ji-Young YounLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada.
Anne-Claude GingrasLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada.
Marc R FabianDepartment of Oncology, McGill University, Montreal, QC, Canada marc.fabian@mcgill.ca jinek@bioc.uzh.ch.ORCID 0000-0003-3700-7604
Martin JinekDepartment of Biochemistry, University of Zurich, Zurich, Switzerland marc.fabian@mcgill.ca jinek@bioc.uzh.ch.ORCID 0000-0002-7601-210X
Jewish General Hospital · CAMount Sinai Hospital · CAUniversity of Zurich · CH

Funding

CIHR MOP‐130425Howard Hughes Medical Institute
6 · The paper itself

Abstract

The LSM domain-containing protein LSM14/Rap55 plays a role in mRNA decapping, translational repression, and RNA granule (P-body) assembly. How LSM14 interacts with the mRNA silencing machinery, including the eIF4E-binding protein 4E-T and the DEAD-box helicase DDX6, is poorly understood. Here we report the crystal structure of the LSM domain of LSM14 bound to a highly conserved C-terminal fragment of 4E-T. The 4E-T C-terminus forms a bi-partite motif that wraps around the N-terminal LSM domain of LSM14. We also determined the crystal structure of LSM14 bound to the C-terminal RecA-like domain of DDX6. LSM14 binds DDX6 via a unique non-contiguous motif with distinct directionality as compared to other DDX6-interacting proteins. Together with mutational and proteomic studies, the LSM14-DDX6 structure reveals that LSM14 has adopted a divergent mode of binding DDX6 in order to support the formation of mRNA silencing complexes and P-body assembly.

Indexed as

Protein Interaction Domains and MotifsAmino Acid SequenceAnimalsBinding SitesCaenorhabditis elegansCrystallography, X-RayDEAD-box RNA HelicasesDrosophila melanogasterEukaryotic Initiation Factor-4EHeLa CellsHumansHydrophobic and Hydrophilic InteractionsModels, MolecularMutationProtein BindingProtein ConformationDDX6 protein, humanDEAD-box RNA HelicasesEDC4 protein, humanEukaryotic Initiation Factor-4EProteinsProto-Oncogene ProteinsRec A RecombinasesRecombinant ProteinsRibonucleoproteinsRNA-associated protein 55, humanRNA, MessengermRNA decappingP‐bodiesprotein–protein interaction networksSLIMstranslational repression

Identifiers

PMID29510985
PMCPMC5881628
OpenAlexW2791043224

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.