Evidence map›Paper›PMID 32175694›Full record

ArticleMolecular systems biology2020

Isoform-resolved correlation analysis between mRNA abundance regulation and protein level degradation.

Barbora Salovska, Hongwen Zhu, Tejas Gandhi, Max Frank, Wenxue Li, George Rosenberger, Chongde Wu, Pierre-Luc Germain, Hu Zhou, Zdenek Hodny and 2 more

Open access · goldAbstract read
In one paragraph

Article in Molecular systems biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

49 citing papers in PubMed, 75 citations in OpenAlex.

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  17. Impact of protein degradation and cell growth on mammalian proteomes.bioRxiv : the preprint server for biology · 2025
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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

12 authors at 7 institutions in 5 countries.

Barbora SalovskaYale Cancer Biology Institute, Yale University, West Haven, CT, USA.ORCID 0000-0002-7093-4576
Hongwen ZhuDepartment of Analytical Chemistry and CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Tejas GandhiBiognosys, Zurich-Schlieren, Switzerland.ORCID 0000-0001-7412-0484
Max FrankEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Wenxue LiYale Cancer Biology Institute, Yale University, West Haven, CT, USA.
George RosenbergerDepartment of Systems Biology, Columbia University, New York, NY, USA.ORCID 0000-0002-1655-6789
Chongde WuYale Cancer Biology Institute, Yale University, West Haven, CT, USA.
Pierre-Luc GermainInstitute for Neuroscience, D-HEST, ETH Zurich, Zurich, Switzerland.ORCID 0000-0003-3418-4218
Hu ZhouDepartment of Analytical Chemistry and CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0001-7006-4737
Zdenek HodnyDepartment of Genome Integrity, Institute of Molecular Genetics of the Czech Academy of Sciences, Prague, Czech Republic.
Lukas ReiterBiognosys, Zurich-Schlieren, Switzerland.ORCID 0000-0001-5751-3139
Yansheng LiuYale Cancer Biology Institute, Yale University, West Haven, CT, USA.ORCID 0000-0002-2626-3912
Yale Cancer Center · USBiognosys (Switzerland) · CHChinese Academy of Sciences · CNColumbia University · USCzech Academy of Sciences, Institute of Molecular Genetics · CZEuropean Molecular Biology Laboratory · DEUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Profiling of biological relationships between different molecular layers dissects regulatory mechanisms that ultimately determine cellular function. To thoroughly assess the role of protein post-translational turnover, we devised a strategy combining pulse stable isotope-labeled amino acids in cells (pSILAC), data-independent acquisition mass spectrometry (DIA-MS), and a novel data analysis framework that resolves protein degradation rate on the level of mRNA alternative splicing isoforms and isoform groups. We demonstrated our approach by the genome-wide correlation analysis between mRNA amounts and protein degradation across different strains of HeLa cells that harbor a high grade of gene dosage variation. The dataset revealed that specific biological processes, cellular organelles, spatial compartments of organelles, and individual protein isoforms of the same genes could have distinctive degradation rate. The protein degradation diversity thus dissects the corresponding buffering or concerting protein turnover control across cancer cell lines. The data further indicate that specific mRNA splicing events such as intron retention significantly impact the protein abundance levels. Our findings support the tight association between transcriptome variability and proteostasis and provide a methodological foundation for studying functional protein degradation.

Indexed as

Alternative SplicingGene Expression Regulation, NeoplasticHeLa CellsHumansIsotope LabelingMass SpectrometryProtein IsoformsProteinsProteolysisProteomicsRNA IsoformsRNA, MessengerWorkflowProtein IsoformsProteinsRNA IsoformsRNA, Messengeralternative splicingDIA mass spectrometryprotein turnoverproteomicspulsed SILAC

Identifiers

PMID32175694
PMCPMC7073818
OpenAlexW3011977430

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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.