Evidence map›Paper›PMID 15806160›Full record

ArticleOncogene2005

Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells.

Brent W Sutherland, Jill Kucab, Joyce Wu, Cathy Lee, Maggie C U Cheang, Erika Yorida, Dmitry Turbin, Shoukat Dedhar, Colleen Nelson, Michael Pollak and 8 more

Abstract read
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In one paragraph

Article in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed
5.7field-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

154 citing papers in PubMed, 299 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Article
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  8. Article
  9. Y-box binding proteins in immunity and RNA virus infection.Microbiology and molecular biology reviews : MMBR · 2025
    Review
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94 more citing papers are in PubMed but not listed here.

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

18 authors at 8 institutions in 3 countries.

Brent W SutherlandClinical Research Division, Fred Hutchinson Cancer Center, Seattle, WA, USA.
Jill Kucab
Joyce Wu
Cathy Lee
Maggie C U Cheang
Erika Yorida
Dmitry Turbin
Shoukat Dedhar
Colleen Nelson
Michael Pollak
H Leighton Grimes
Kathy Miller
Sunil Badve
David Huntsman
C Blake-Gilks
Min Chen
Catherine J Pallen
Sandra E Dunn
BC Cancer Agency · CAChildren’s Health Research Institute · CAIndiana University Bloomington · USFred Hutch Cancer Center · USInstitute of Molecular and Cell Biology · SGMcGill University · CAVancouver General Hospital · CAVancouver Hospital and Health Sciences Centre · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Akt/PKB is a serine/threonine kinase that promotes tumor cell growth by phosphorylating transcription factors and cell cycle proteins. There is particular interest in finding tumor-specific substrates for Akt to understand how this protein functions in cancer and to provide new avenues for therapeutic targeting. Our laboratory sought to identify novel Akt substrates that are expressed in breast cancer. In this study, we determined that activated Akt is positively correlated with the protein expression of the transcription/translation factor Y-box binding protein-1 (YB-1) in primary breast cancer by screening tumor tissue microarrays. We therefore questioned whether Akt and YB-1 might be functionally linked. Herein, we illustrate that activated Akt binds to and phosphorylates the YB-1 cold shock domain at Ser102. We then addressed the functional significance of disrupting Ser102 by mutating it to Ala102. Following the stable expression of Flag:YB-1 and Flag:YB-1 (Ala102) in MCF-7 cells, we observed that disruption of the Akt phosphorylation site on YB-1 suppressed tumor cell growth in soft agar and in monolayer. This correlated with an inhibition of nuclear translocation by the YB-1(Ala102) mutant. In conclusion, YB-1 is a new Akt substrate and disruption of this specific site inhibits tumor cell growth.

Indexed as

Breast NeoplasmsCCAAT-Enhancer-Binding ProteinsCell AdhesionCell ProliferationDisease ProgressionFemaleHumansNFI Transcription FactorsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionTranscription FactorsY-Box-Binding Protein 1AKT1 protein, humanCCAAT-Enhancer-Binding ProteinsNFI Transcription FactorsProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktTranscription FactorsY-Box-Binding Protein 1

Identifiers

PMID15806160
OpenAlexW2132349803

What OpenQuestion holds

Textmetadata
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.