Evidence map›Paper›PMID 29844170›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Structural basis for MTR4-ZCCHC8 interactions that stimulate the MTR4 helicase in the nuclear exosome-targeting complex.

M Rhyan Puno, Christopher D Lima

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

48 citing papers in PubMed, 66 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

2 authors at 1 institution in 1 country.

M Rhyan PunoStructural Biology Program, Sloan Kettering Institute, New York, NY 10065.
Christopher D LimaStructural Biology Program, Sloan Kettering Institute, New York, NY 10065; limac@mskcc.org.ORCID 0000-0002-9163-6092
Howard Hughes Medical Institute · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structural studies of RNA processing and ubiquitin-like protein modificationR35GM118080 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI CHRISTOPHER D. LIMA · 2016 to 2026
$5.0M
Structural and Functional Studies of Eukaryotic ExosomesR01GM079196 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI LIMA, CHRISTOPHER D. · 2008 to 2015
$2.5M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA008748NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM079196NIGMS NIH HHS R35 GM118080
6 · The paper itself

Abstract

The nuclear exosome-targeting (NEXT) complex functions as an RNA exosome cofactor and is involved in surveillance and turnover of aberrant transcripts and noncoding RNAs. NEXT is a ternary complex composed of the RNA-binding protein RBM7, the scaffold zinc-knuckle protein ZCCHC8, and the helicase MTR4. While RNA interactions with RBM7 are known, it remains unclear how NEXT subunits collaborate to recognize and prepare substrates for degradation. Here, we show that MTR4 helicase activity is enhanced when associated with RBM7 and ZCCHC8. While uridine-rich substrates interact with RBM7 and are preferred, optimal activity is observed when substrates include a polyadenylated 3' end. We identify a bipartite interaction of ZCCHC8 with MTR4 and uncover a role for the conserved C-terminal domain of ZCCHC8 in stimulating MTR4 helicase and ATPase activities. A crystal structure reveals that the ZCCHC8 C-terminal domain binds the helicase core in a manner that is distinct from that observed for

Indexed as

Cell NucleusDEAD-box RNA HelicasesExosome Multienzyme Ribonuclease ComplexExosomesModels, MolecularNuclear ProteinsProtein BindingRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDEAD-box RNA HelicasesExosome Multienzyme Ribonuclease ComplexMTR4 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsNEXT complexRBM7R-LOOPRNARNA decay

Identifiers

PMID29844170
PMCPMC6004480
OpenAlexW2807613466

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.