Evidence map›Paper›PMID 22990868›Full record

ArticleNature communications2012

Enhanced HSP70 lysine methylation promotes proliferation of cancer cells through activation of Aurora kinase B.

Hyun-Soo Cho, Tadahiro Shimazu, Gouji Toyokawa, Yataro Daigo, Yoshihiko Maehara, Shinya Hayami, Akihiro Ito, Ken Masuda, Noriko Ikawa, Helen I Field and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

72 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 9 institutions in 3 countries.

Hyun-Soo ChoLaboratory of Molecular Medicine, Human Genome Center, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo, Japan.
Tadahiro Shimazu
Gouji Toyokawa
Yataro Daigo
Yoshihiko Maehara
Shinya Hayami
Akihiro Ito
Ken Masuda
Noriko Ikawa
Helen I Field
Eiju Tsuchiya
Shin-ichi Ohnuma
Bruce A J Ponder
Minoru Yoshida
Yusuke Nakamura
Ryuji Hamamoto
The University of Tokyo · JPRIKEN Advanced Science Institute · JPKyushu University · JPTokyo University of Science · JPCancer Research UK · GBSaitama Cancer Center · JPShiga University of Medical Science · JPUniversity College London · GBUniversity of Cambridge · GB

Funding

Cancer Research UK 19275
6 · The paper itself

Abstract

Although heat-shock protein 70 (HSP70), an evolutionarily highly conserved molecular chaperone, is known to be post-translationally modified in various ways such as phosphorylation, ubiquitination and glycosylation, physiological significance of lysine methylation has never been elucidated. Here we identify dimethylation of HSP70 at Lys-561 by SETD1A. Enhanced HSP70 methylation was detected in various types of human cancer by immunohistochemical analysis, although the methylation was barely detectable in corresponding non-neoplastic tissues. Interestingly, methylated HSP70 predominantly localizes to the nucleus of cancer cells, whereas most of the HSP70 protein locates to the cytoplasm. Nuclear HSP70 directly interacts with Aurora kinase B (AURKB) in a methylation-dependent manner and promotes AURKB activity in vitro and in vivo. We also find that methylated HSP70 has a growth-promoting effect in cancer cells. Our findings demonstrate a crucial role of HSP70 methylation in human carcinogenesis.

Indexed as

AnimalsAurora Kinase BAurora KinasesBlotting, WesternCell Line, TumorCell ProliferationChlorocebus aethiopsCOS CellsHSP70 Heat-Shock ProteinsHumansImmunohistochemistryImmunoprecipitationLysineMethylationProtein BindingProtein Serine-Threonine KinasesAURKB protein, humanAurora Kinase BAurora KinasesHSP70 Heat-Shock ProteinsLysineProtein Serine-Threonine Kinases

Identifiers

PMID22990868
PMCPMC3658001
OpenAlexW1996315419

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.