Evidence map›Paper›PMID 31825839›Full record

ArticleCell reports2019

On-Site Ribosome Remodeling by Locally Synthesized Ribosomal Proteins in Axons.

Toshiaki Shigeoka, Max Koppers, Hovy Ho-Wai Wong, Julie Qiaojin Lin, Roberta Cagnetta, Asha Dwivedy, Janaina de Freitas Nascimento, Francesca W van Tartwijk, Florian Ströhl, Jean-Michel Cioni and 6 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

111 citing papers in PubMed, 183 citations in OpenAlex.

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51 more citing papers are in PubMed but not listed here.

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

16 authors at 1 institution in 1 country.

Toshiaki ShigeokaDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK. Electronic address: ts561@cam.ac.uk.
Max KoppersDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Hovy Ho-Wai WongDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Julie Qiaojin LinDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Roberta CagnettaDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Asha DwivedyDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Janaina de Freitas NascimentoDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.
Francesca W van TartwijkDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK.
Florian StröhlDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK.
Jean-Michel CioniDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Julia SchaefferDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Mark CarringtonDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.
Clemens F KaminskiDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK.
Hosung JungDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
William A HarrisDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK.
Christine E HoltDepartment of Physiology, Development and Neuroscience, University of Cambridge, Downing Street, Cambridge CB2 3DY, UK. Electronic address: ceh33@cam.ac.uk.
University of Cambridge · GB

Funding

European Research Council 322817Medical Research Council MR/K015850/1Medical Research Council MR/K02292X/1Wellcome Trust 203249/Z/16/Z
6 · The paper itself

Abstract

Ribosome assembly occurs mainly in the nucleolus, yet recent studies have revealed robust enrichment and translation of mRNAs encoding many ribosomal proteins (RPs) in axons, far away from neuronal cell bodies. Here, we report a physical and functional interaction between locally synthesized RPs and ribosomes in the axon. We show that axonal RP translation is regulated through a sequence motif, CUIC, that forms an RNA-loop structure in the region immediately upstream of the initiation codon. Using imaging and subcellular proteomics techniques, we show that RPs synthesized in axons join axonal ribosomes in a nucleolus-independent fashion. Inhibition of axonal CUIC-regulated RP translation decreases local translation activity and reduces axon branching in the developing brain, revealing the physiological relevance of axonal RP synthesis in vivo. These results suggest that axonal translation supplies cytoplasmic RPs to maintain/modify local ribosomal function far from the nucleolus in neurons.

Indexed as

NeurogenesisAnimalsAxonsBrainCells, CulturedRegulatory Sequences, Ribonucleic AcidRibosomal ProteinsRibosomesRNA, MessengerXenopus laevisRegulatory Sequences, Ribonucleic AcidRibosomal ProteinsRNA, Messengeraxonaxonal protein synthesisaxon branchinglocal translationmRNAneural wiringribosomal proteinsribosomeribosome remodelingRps4x

Identifiers

PMID31825839
PMCPMC6915326
OpenAlexW2995312562

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.