Evidence map›Paper›PMID 31113955›Full record

ArticleNature communications2019

Ubiquitylome study identifies increased histone 2A ubiquitylation as an evolutionarily conserved aging biomarker.

Lu Yang, Zaijun Ma, Han Wang, Kongyan Niu, Ye Cao, Le Sun, Yang Geng, Bo Yang, Feng Gao, Zuolong Chen and 9 more

Abstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

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  17. MicroRNA biogenesis pathway alterations in aging.Extracellular vesicles and circulating nucleic acids · 2023
    Review
  18. Review
  19. Article
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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

19 authors.

Lu YangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Zaijun MaInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Han WangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Kongyan NiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Ye CaoInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Le SunInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Yang GengInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Bo YangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Feng GaoNeurodegenerative Disorder Research Center, University of Science and Technology of China, No.96, JinZhai Road Baohe District, Hefei, Anhui, 230026, China.
Zuolong ChenNeurodegenerative Disorder Research Center, University of Science and Technology of China, No.96, JinZhai Road Baohe District, Hefei, Anhui, 230026, China.ORCID http://orcid.org/0000-0001-7558-6278
Zhen WuState Key Laboratory of Genetic Engineering, Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai, 200438, China.
Qingqing LiState Key Laboratory of Genetic Engineering, Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai, 200438, China.
Yong ShenNeurodegenerative Disorder Research Center, University of Science and Technology of China, No.96, JinZhai Road Baohe District, Hefei, Anhui, 230026, China.
Xumin ZhangState Key Laboratory of Genetic Engineering, Department of Biochemistry, School of Life Sciences, Fudan University, Shanghai, 200438, China.ORCID http://orcid.org/0000-0002-2810-6363
Hong JiangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Yelin ChenInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China.
Rui LiuSinglera Genomics, 781 Cailun Road, Rm 1208, Pudong, Shanghai, 201203, China.
Nan LiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China. liunan@sioc.ac.cn.
Yaoyang ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 26 Qiuyue Rd., Pudong, Shanghai, 201210, China. zyy@sioc.ac.cn.ORCID http://orcid.org/0000-0001-5363-9834

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31500665National Natural Science Foundation of China (National Science Foundation of China) 31530041National Natural Science Foundation of China (National Science Foundation of China) 31671428
6 · The paper itself

Abstract

The long-lived proteome constitutes a pool of exceptionally stable proteins with limited turnover. Previous studies on ubiquitin-mediated protein degradation primarily focused on relatively short-lived proteins; how ubiquitylation modifies the long-lived proteome and its regulatory effect on adult lifespan is unclear. Here we profile the age-dependent dynamics of long-lived proteomes in Drosophila by mass spectrometry using stable isotope switching coupled with antibody-enriched ubiquitylome analysis. Our data describe landscapes of long-lived proteins in somatic and reproductive tissues of Drosophila during adult lifespan, and reveal a preferential ubiquitylation of older long-lived proteins. We identify an age-modulated increase of ubiquitylation on long-lived histone 2A protein in Drosophila, which is evolutionarily conserved in mouse, monkey, and human. A reduction of ubiquitylated histone 2A in mutant flies is associated with longevity and healthy lifespan. Together, our data reveal an evolutionarily conserved biomarker of aging that links epigenetic modulation of the long-lived histone protein to lifespan.

Indexed as

AgingAnimalsAnimals, Genetically ModifiedBiomarkersBrainDrosophila melanogasterFemaleHistonesHumansLongevityMacaca mulattaMaleMiceProteomicsUbiquitinationBiomarkersHistones

Identifiers

PMID31113955
PMCPMC6529468

What OpenQuestion holds

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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.