Evidence map›Paper›PMID 28510697›Full record

ArticleJournal of molecular cell biology2017

BCCIPβ modulates the ribosomal and extraribosomal function of S7 through a direct interaction.

Qian Ba, Xiaoguang Li, Chao Huang, Junyang Li, Yijing Fu, Peizhan Chen, Juan Duan, Miao Hao, Yinghua Zhang, Jingquan Li and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Roles of BCCIP deficiency in mammary tumorigenesis.Breast cancer research : BCR · 2017
    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

16 authors at 5 institutions in 2 countries.

Qian BaSchool of Public Health, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
Xiaoguang LiSchool of Public Health, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
Chao HuangKey Laboratory of Food Safety Research, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Junyang LiKey Laboratory of Food Safety Research, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Yijing FuKey Laboratory of Food Safety Research, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Peizhan ChenSchool of Public Health, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
Juan DuanKey Laboratory of Food Safety Research, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Miao HaoKey Laboratory of Food Safety Research, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Yinghua ZhangKey Laboratory of Food Safety Research, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Jingquan LiSchool of Public Health, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
Chuanqi SunInstitute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Hao YingKey Laboratory of Food Safety Research, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Haiyun SongKey Laboratory of Food Safety Research, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Ruiwen ZhangDepartment of Pharmaceutical Sciences, School of Pharmacy, Texas Tech University Health Sciences Center, Amarillo, TX 79106, USA.
Zhiyuan ShenRutgers Cancer Institute of New Jersey, Department of Radiation Oncology of Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, New Brunswick, NJ 08903, USA.
Hui WangSchool of Public Health, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
Chinese Academy of Sciences · CNShanghai Institutes for Biological Sciences · CNShanghai Jiao Tong University · CNRutgers, The State University of New Jersey · USTexas Tech University · US

Funding

Molecular modulators of radiation-induced chromosome instability and hematopoietic damageR01CA195612 · NCI · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI SHEN, ZHIYUAN · 2015 to 2025
$3.6M
Alternative Mechanisms to Inactivate p53 During OncogenesisR01CA156706 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI SHEN, ZHIYUAN · 2011 to 2015
$1.9M
NCI NIH HHS R01 CA156706NCI NIH HHS R01 CA195612
6 · The paper itself

Abstract

Extraribosomal functions of ribosomal proteins (RPs) have gained much attention for their implications in tumorigenesis and progression. However, the regulations for transition between the ribosomal and extraribosomal functions of RPs are rarely reported. Herein, we identified a ribosomal protein S7-interacting partner, BCCIPβ, which modulates the functional conversion of S7. Through the N-terminal acidic domain, BCCIPβ interacts with the central basic region in S7 and regulates the extraribosomal distribution of S7. BCCIPβ deficiency abrogates the ribosomal accumulation but enhances the ribosome-free location of S7. This translocation further impairs protein synthesis and triggers ribosomal stress. Consequently, BCCIPβ deficiency suppresses the ribosomal function and initiates the extraribosomal function of S7, resulting in restriction of cell proliferation. Moreover, clinically relevant S7 mutations were found to dampen the interaction with BCCIPβ and facilitate the functional transition of S7. In conclusion, BCCIPβ, as a S7 modulator, contributes to the regulation of ribosomal and extraribosomal functions of S7 and has implications in cell growth and tumor development.

Indexed as

Binding SitesCalcium-Binding ProteinsCell Cycle ProteinsHEK293 CellsHumansImmunoprecipitationMutationNeoplasmsNuclear ProteinsProtein Interaction MappingRibosomal ProteinsRibosomesSignal TransductionStatic ElectricityTumor Suppressor Protein p53BCCIP protein, humanCalcium-Binding ProteinsCell Cycle ProteinsNuclear ProteinsRibosomal Proteinsribosomal protein S7TP53 protein, humanTumor Suppressor Protein p53BCCIPβribosomal protein S7ribosomal stresstranslationtumor suppressor

Identifiers

PMID28510697
PMCPMC5907838
OpenAlexW2613734954

What OpenQuestion holds

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LicenceCC BY-NC
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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.