Evidence map›Paper›PMID 33796843›Full record

ArticleiScience2021

The nucleolus functions as the compartment for histone H2B protein degradation.

Yanping Liu, Yufei Wang, Lu Yang, Feng Sun, Sheng Li, Yequan Wang, Guo-An Zhang, Tingting Dong, Lei-Lei Zhang, Wanglin Duan and 3 more

Open access · goldAbstract read
In one paragraph

Article in iScience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

10 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Nucleolar stress: Friend or foe in cardiac function?Frontiers in cardiovascular medicine · 2022
    Review
  9. Review
  10. STAR protocols · 2021
    Article
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

13 authors at 4 institutions in 1 country.

Yanping LiuLaboratory of Molecular and Cellular Biology, School of Forensic Sciences, Xi'an Jiao Tong University Health Science Center, Xi'an, Shaanxi 710061, PR China.
Yufei WangLaboratory of Molecular and Cellular Biology, School of Forensic Sciences, Xi'an Jiao Tong University Health Science Center, Xi'an, Shaanxi 710061, PR China.
Lu YangLaboratory of Molecular and Cellular Biology, School of Forensic Sciences, Xi'an Jiao Tong University Health Science Center, Xi'an, Shaanxi 710061, PR China.
Feng SunResearch Center for Translational Medicine at East Hospital, School of Life Sciences and Technology, Tongji University, Shanghai, Shanghai 200092, PR China.
Sheng LiSchool of Forensic Sciences and Laboratory Medicine, Jining Medical University, Jining, Shandong 272067, PR China.
Yequan WangSchool of Forensic Sciences and Laboratory Medicine, Jining Medical University, Jining, Shandong 272067, PR China.
Guo-An ZhangSchool of Forensic Sciences and Laboratory Medicine, Jining Medical University, Jining, Shandong 272067, PR China.
Tingting DongSchool of Forensic Sciences and Laboratory Medicine, Jining Medical University, Jining, Shandong 272067, PR China.
Lei-Lei ZhangSchool of Forensic Sciences and Laboratory Medicine, Jining Medical University, Jining, Shandong 272067, PR China.
Wanglin DuanLaboratory of Molecular and Cellular Biology, School of Forensic Sciences, Xi'an Jiao Tong University Health Science Center, Xi'an, Shaanxi 710061, PR China.
Xiaojun ZhangDepartment of Science and Education, People's Hospital of Zunhua, Tangshan, Hebei 064200, PR China.
Wen CuiSchool of Forensic Sciences and Laboratory Medicine, Jining Medical University, Jining, Shandong 272067, PR China.
Su ChenLaboratory of Molecular and Cellular Biology, School of Forensic Sciences, Xi'an Jiao Tong University Health Science Center, Xi'an, Shaanxi 710061, PR China.
Jining Medical University · CNXi'an Jiaotong University · CNHenan University · CNShanghai East Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histones are main components of chromatin, and the protein levels of histones significantly affect chromatin assembly. However, how histone protein levels are regulated, especially whether and how histones are degraded, is largely unclear. Here, we found that histone H2B is mainly degraded through the proteasome-mediated pathway, and the lysine-120 site of H2B is essential for its K48-linked polyubiquitination and degradation. Moreover, the degradation-impaired H2BK120R mutant shows an increased nucleolus localization, and inhibition of the proteasome results in an elevated nucleolus distribution of wild-type H2B, which is similar to that of H2BK120R mutants. More importantly, the nucleolus fractions can ubiquitinate and degrade the purified H2B

Indexed as

BiochemistryCell Biology

Identifiers

PMID33796843
PMCPMC7995529
OpenAlexW3134540402

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.