Evidence map›Paper›PMID 26460970›Full record

ArticlePloS one2015

Proteomic Analysis of the Ubiquitin Landscape in the Drosophila Embryonic Nervous System and the Adult Photoreceptor Cells.

Juanma Ramirez, Aitor Martinez, Benoit Lectez, So Young Lee, Maribel Franco, Rosa Barrio, Gunnar Dittmar, Ugo Mayor

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. 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
1.5field-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

17 citing papers in PubMed, 31 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

8 authors at 5 institutions in 4 countries.

Juanma RamirezDepartment of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), Leioa, Bizkaia, Spain; Functional Genomics Unit, CIC bioGUNE, Derio, Spain.
Aitor MartinezDepartment of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), Leioa, Bizkaia, Spain; Functional Genomics Unit, CIC bioGUNE, Derio, Spain; Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool, United Kingdom.
Benoit LectezFunctional Genomics Unit, CIC bioGUNE, Derio, Spain; Mollecular Cell Biology, Turku Centre for Biotechnology, Turku, Finland.
So Young LeeFunctional Genomics Unit, CIC bioGUNE, Derio, Spain.
Maribel FrancoFunctional Genomics Unit, CIC bioGUNE, Derio, Spain; Developmental Neurobiology, Institute of Neurosciences, CSIC/UMH, Sant Joan d'Alacant, Alicante, Spain.
Rosa BarrioFunctional Genomics Unit, CIC bioGUNE, Derio, Spain.
Gunnar DittmarMax Delbrück Center for Molecular Medicine, Berlin, Germany.
Ugo MayorDepartment of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), Leioa, Bizkaia, Spain; Functional Genomics Unit, CIC bioGUNE, Derio, Spain; Ikerbasque, Basque Foundation for Science, Bilbao, Bizkaia, Spain.
CIC bioGUNE · ESIkerbasque · ESMax Delbrück Center · DETurku Centre for Biotechnology · FIUniversity of the Basque Country · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundUbiquitination is known to regulate physiological neuronal functions as well as to be involved in a number of neuronal diseases. Several ubiquitin proteomic approaches have been developed during the last decade but, as they have been mostly applied to non-neuronal cell culture, very little is yet known about neuronal ubiquitination pathways in vivo. METHODOLOGY/PRINCIPAL

findingsUsing an in vivo biotinylation strategy we have isolated and identified the ubiquitinated proteome in neurons both for the developing embryonic brain and for the adult eye of Drosophila melanogaster. Bioinformatic comparison of both datasets indicates a significant difference on the ubiquitin substrates, which logically correlates with the processes that are most active at each of the developmental stages. Detection within the isolated material of two ubiquitin E3 ligases, Parkin and Ube3a, indicates their ubiquitinating activity on the studied tissues. Further identification of the proteins that do accumulate upon interference with the proteasomal degradative pathway provides an indication of the proteins that are targeted for clearance in neurons. Last, we report the proof-of-principle validation of two lysine residues required for nSyb ubiquitination. CONCLUSIONS/SIGNIFICANCE: These data cast light on the differential and common ubiquitination pathways between the embryonic and adult neurons, and hence will contribute to the understanding of the mechanisms by which neuronal function is regulated. The in vivo biotinylation methodology described here complements other approaches for ubiquitome study and offers unique advantages, and is poised to provide further insight into disease mechanisms related to the ubiquitin proteasome system.

Indexed as

Amino Acid SequenceAnimalsBiotinylationBlotting, WesternCell LineDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianGreen Fluorescent ProteinsMass SpectrometryMolecular Sequence DataNervous SystemNeuronsPhotoreceptor Cells, InvertebrateProteasome Endopeptidase ComplexProteomicsDrosophila ProteinsGreen Fluorescent ProteinsProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID26460970
PMCPMC4604154
OpenAlexW2117633571

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Registered trials

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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.