Evidence map›Paper›PMID 20807815›Full record

ArticleCancer research2010

Cyclin-dependent kinase-mediated phosphorylation plays a critical role in the oncogenic functions of PELP1.

Binoj C Nair, Sujit S Nair, Dimple Chakravarty, Rambabu Challa, Bramanandam Manavathi, P Renee Yew, Rakesh Kumar, Rajeshwar Rao Tekmal, Ratna K Vadlamudi

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
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  11. Overexpression of PELP1 in Lung Adenocarcinoma Promoted EPathology oncology research : POR · 2021
    Article
  12. Article
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  14. Review
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  18. Minireview: Deciphering the Cellular Functions of PELP1.Molecular endocrinology (Baltimore, Md.) · 2015
    Review
  19. Article
  20. 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

9 authors at 3 institutions in 2 countries.

Binoj C NairDepartment of Obstetrics and Gynecology, University of Texas Health Science Center, 7703 Floyd Curl Drive, Mail Code 7836, San Antonio, TX 78229-3900, USA.
Sujit S Nair
Dimple Chakravarty
Rambabu Challa
Bramanandam Manavathi
P Renee Yew
Rakesh Kumar
Rajeshwar Rao Tekmal
Ratna K Vadlamudi
The University of Texas Health Science Center at San Antonio · USUniversity of Hyderabad · INWashington University Medical Center · US

Funding

PELP1, a Novel Regulator of Estrogen ReceptorR01CA095681 · NCI · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI VADLAMUDI, RATNA K · 2003 to 2013
$2.5M
NCI NIH HHS CA0095681NCI NIH HHS R01 CA095681
6 · The paper itself

Abstract

Estrogen receptor (ER) signaling plays an important role in breast cancer progression, and ER functions are influenced by coregulatory proteins. PELP1 (proline-, glutamic acid-, and leucine-rich protein 1) is a nuclear receptor coregulator that plays an important role in ER signaling. Its expression is deregulated in hormonal cancers. We identified PELP1 as a novel cyclin-dependent kinase (CDK) substrate. Using site-directed mutagenesis and in vitro kinase assays, we identified Ser(477) and Ser(991) of PELP1 as CDK phosphorylation sites. Using the PELP1 Ser(991) phospho-specific antibody, we show that PELP1 is hyperphosphorylated during cell cycle progression. Model cells stably expressing the PELP1 mutant that lack CDK sites had defects in estradiol (E2)-mediated cell cycle progression and significantly affected PELP1-mediated oncogenic functions in vivo. Mechanistic studies showed that PELP1 modulates transcription factor E2F1 transactivation functions, that PELP1 is recruited to pRb/E2F target genes, and that PELP1 facilitates ER signaling cross talk with cell cycle machinery. We conclude that PELP1 is a novel substrate of interphase CDKs and that its phosphorylation is important for the proper function of PELP1 in modulating hormone-driven cell cycle progression and also for optimal E2F transactivation function. Because the expression of both PELP1 and CDKs is deregulated in breast tumors, CDK-PELP1 interactions will have implications in breast cancer progression.

Indexed as

AnimalsBreast NeoplasmsCell CycleCell Line, TumorCo-Repressor ProteinsCyclin-Dependent Kinase 2Cyclin-Dependent KinasesE2F Transcription FactorsFemaleHumansMiceMice, NudeMutationNIH 3T3 CellsPhosphorylationTrans-ActivatorsCo-Repressor ProteinsCyclin-Dependent Kinase 2Cyclin-Dependent KinasesE2F Transcription FactorsPELP1 protein, humanTrans-ActivatorsTranscription Factors

Identifiers

PMID20807815
PMCPMC3058498
OpenAlexW2154478723

What OpenQuestion holds

Textmetadata
LicenceTDM
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.