Evidence map›Paper›PMID 33574926›Full record

ArticleOncology letters2021

Akt regulates RSK2 to alter phosphorylation level of H2A.X in breast cancer.

Zhi-Feng Guo, Fan-Long Kong

Open access · diamondAbstract read
In one paragraph

Article in Oncology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
  3. Targeting RSK2 in Cancer Therapy: A Review of Natural Products.Anti-cancer agents in medicinal chemistry · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Association BetweenFrontiers in genetics · 2021
    Review
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

2 authors at 1 institution in 1 country.

Zhi-Feng GuoDepartment of Oncology, Section II, Chifeng Municipal Hospital, Chifeng, Inner Mongolia Autonomous Region 024000, P.R. China.
Fan-Long KongDepartment of Oncology, Section II, Chifeng Municipal Hospital, Chifeng, Inner Mongolia Autonomous Region 024000, P.R. China.
Chifeng Municipal Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone H2AX (H2A.X) is a variant of the histone H2A family. Phosphorylation of H2A.X is a marker of DNA strand breaks and the presence or absence of H2A.X is closely related to tumor susceptibility and drug resistance. The present study found that the activity of the serine/threonine kinase Akt was negatively associated with H2A.X phosphorylated at the Ser16 site (H2A.X S16ph), but the mechanism of the inverse relationship remains elusive. The aim of the present study was to elucidate the mechanism of action between Akt and H2A.X S16ph and the exact role of this mechanism. Western blot analysis was performed to detect the regulatory association between p-Akt and H2A.X S16ph/p-RSK2, and immunoprecipitation and chromatin immunoprecipitation were performed to prove that Akt, RSK2 and H2A.X combine and interact in human breast cancer cells. The changes of cellular proliferation and migration induced by the interaction of Akt, RSK2 and H2A.X was determined by MTT, soft agar colony formation and cell migration experiments. The effect of interaction of Akt, RSK2 and H2A.X on cancer-promoting genes, such as PSAT-1 was determined via reverse transcription-quantitative PCR analysis. The current study indicated that the serine/threonine kinase ribosomal S6 kinase 2 (RSK2) as a kinase of H2A.X could be phosphorylated by Akt at Ser19 site. Moreover, Akt positively regulated the phosphorylation of RSK2 to inhibit phosphorylation of H2A.X, thereby affecting the affinity between RSK2 and substrate histone, promoting the survival and migration of breast cancer cells. In conclusion, Akt-mediated phosphorylation of RSK2 regulated the phosphorylation of H2A.X, thereby promoting oncogenic activity. This finding provides new insights to understand the pathogenesis and treatment mechanisms of breast cancer.

Indexed as

Aktbreast cancerhistone H2AXphosphorylationserine/threonine kinase ribosomal S6 kinase 2

Identifiers

PMID33574926
PMCPMC7816342
OpenAlexW3119787732

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.