Evidence map›Paper›PMID 27474797›Full record

ArticleeLife2016

Spatial control of translation repression and polarized growth by conserved NDR kinase Orb6 and RNA-binding protein Sts5.

Illyce Nuñez, Marbelys Rodriguez Pino, David J Wiley, Maitreyi E Das, Chuan Chen, Tetsuya Goshima, Kazunori Kume, Dai Hirata, Takashi Toda, Fulvia Verde

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

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  11. Role ofInternational journal of molecular sciences · 2021
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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

10 authors at 5 institutions in 3 countries.

Illyce NuñezMolecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, United States.
Marbelys Rodriguez PinoMolecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, United States.
David J WileyMolecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, United States.
Maitreyi E DasDepartment of Biochemistry and Cellular and Molecular Biology, The University of Tennessee, Knoxville, United States.
Chuan ChenMolecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, United States.
Tetsuya GoshimaNational Research Institute of Brewing, Higashi-Hiroshima, Japan.
Kazunori KumeDepartment of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima, Japan.
Dai HirataDepartment of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima, Japan.
Takashi TodaDepartment of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima, Japan.
Fulvia VerdeMolecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, United States.ORCID 0000-0002-2575-0823
University of Miami · USHiroshima University · JPMarine Biological Laboratory · USNational Research Institute of Brewing · JPUniversity of Tennessee at Knoxville · US

Funding

Control of cell morphogenesis and cell growth by conserved NDR kinase Orb6R01GM095867 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI VERDE, FULVIA · 2011 to 2015
$1.4M
Cancer Research UKNIGMS NIH HHS R01 GM095867
6 · The paper itself

Abstract

RNA-binding proteins contribute to the formation of ribonucleoprotein (RNP) granules by phase transition, but regulatory mechanisms are not fully understood. Conserved fission yeast NDR (Nuclear Dbf2-Related) kinase Orb6 governs cell morphogenesis in part by spatially controlling Cdc42 GTPase. Here we describe a novel, independent function for Orb6 kinase in negatively regulating the recruitment of RNA-binding protein Sts5 into RNPs to promote polarized cell growth. We find that Orb6 kinase inhibits Sts5 recruitment into granules, its association with processing (P) bodies, and degradation of Sts5-bound mRNAs by promoting Sts5 interaction with 14-3-3 protein Rad24. Many Sts5-bound mRNAs encode essential factors for polarized cell growth, and Orb6 kinase spatially and temporally controls the extent of Sts5 granule formation. Disruption of this control system affects cell morphology and alters the pattern of polarized cell growth, revealing a role for Orb6 kinase in the spatial control of translational repression that enables normal cell morphogenesis.

Indexed as

Gene Expression Regulation, FungalProtein BiosynthesisCell Cycle ProteinsMicroscopy, FluorescenceProtein Serine-Threonine KinasesSchizosaccharomycesSchizosaccharomyces pombe ProteinsCell Cycle ProteinsOrb6 protein, S pombeProtein Serine-Threonine KinasesSchizosaccharomyces pombe ProteinsSTS5 protein, S pombe14-3-3 proteincell biologyNDR kinaseP-bodypolarized growthRNP granule assemblyS. pombetranslational repression

Identifiers

PMID27474797
PMCPMC5011436
OpenAlexW2488383711

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.