Evidence map›Paper›PMID 15994929›Full record

ArticleCancer research2005

Proline-, glutamic acid-, and leucine-rich protein-1 is essential in growth factor regulation of signal transducers and activators of transcription 3 activation.

Bramanandam Manavathi, Sujit S Nair, Rui-An Wang, Rakesh Kumar, Ratna K Vadlamudi

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Altered Expression ofInternational journal of molecular sciences · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. STAT3 Interactors as Potential Therapeutic Targets for Cancer Treatment.International journal of molecular sciences · 2018
    Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. PELP1: a review of PELP1 interactions, signaling, and biology.Molecular and cellular endocrinology · 2014
    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

5 authors at 1 institution in 1 country.

Bramanandam ManavathiDepartment of Molecular and Cellular Oncology, The University of Texas M.D. Anderson Cancer Center, Houston, Texas, USA.
Sujit S Nair
Rui-An Wang
Rakesh Kumar
Ratna K Vadlamudi
The University of Texas MD Anderson Cancer Center · US

Funding

Role of Metastatic Tumor Antigen-1 in Mammary GlandR01CA098823 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI KUMAR, RAKESH · 2003 to 2013
$3.1M
PELP1, a Novel Regulator of Estrogen ReceptorR01CA095681 · NCI · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI VADLAMUDI, RATNA K · 2003 to 2013
$2.5M
SERM Regulation of PAK Pathway in Endometrial CancerR01CA109379 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI KUMAR, RAKESH · 2004 to 2008
$1.5M
NCI NIH HHS CA 095681NCI NIH HHS CA 098823NCI NIH HHS CA109379NCI NIH HHS R01 CA095681NCI NIH HHS R01 CA098823NCI NIH HHS R01 CA109379
6 · The paper itself

Abstract

Proline-, glutamic acid-, and leucine-rich protein-1 (PELP1) is a novel estrogen receptor coactivator that plays an important role in the genomic and nongenomic actions of estrogen receptor by interacting with histones and src-mitogen-activated protein kinase pathway, respectively. A great deal of information has emerged in recent years about the possible role of PELP1 in estrogen receptor signaling. However, the participation and significance of PELP1 in other cellular signaling pathways remains unknown. Using a yeast two-hybrid screen, we identified PELP1 as a novel interacting protein of signal transducers and activators of transcription 3 (STAT3) and found evidence of physiologic interaction between PELP1 and STAT3. We also found that these interactions played a mechanistic role in the positive regulation of STAT3 transcription from synthetic promoters and endogenous target genes such as cyclin D1, c-myc, and c-fos. Overexpression of PELP1 enhanced phosphorylation of STAT3 at Ser727 in a src-mitogen-activated protein kinase-sensitive manner and, conversely, down-regulation of PELP1 compromised growth factor-mediated induction of STAT3 target genes. We also discovered that PELP1 interacts with STAT3 in the nuclear compartment and down-regulation of PELP1 interfered with the recruitment of STAT3 to its target gene promoters. In summary, our results highlight a novel role for PELP1 in growth factor signaling and indicate that PELP1-mediated genomic and nongenomic functions play a role in the growth factor-mediated STAT3 transactivation functions. Such regulatory interactions of PELP1 may have important functional implications in the cross-talk of estrogen receptor and growth factor signaling.

Indexed as

AnimalsBreast NeoplasmsCell Line, TumorCell NucleusChlorocebus aethiopsCo-Repressor ProteinsCOS CellsDNA-Binding ProteinsErbB ReceptorsHeLa CellsHumansMAP Kinase Signaling SystemMicePhosphorylationsrc-Family KinasesSTAT3 Transcription FactorCo-Repressor ProteinsDNA-Binding ProteinsErbB ReceptorsPELP1 protein, humansrc-Family KinasesSTAT3 protein, humanStat3 protein, mouseSTAT3 Transcription FactorTrans-ActivatorsTranscription Factors

Identifiers

PMID15994929
PMCPMC1262663
OpenAlexW2147549133

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.