Evidence map›Paper›PMID 18922467›Full record

ArticleMolecular cell2008

Essential phosphatases and a phospho-degron are critical for regulation of SRC-3/AIB1 coactivator function and turnover.

Chao Li, Yao-Yun Liang, Xin-Hua Feng, Sophia Y Tsai, Ming-Jer Tsai, Bert W O'Malley

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. SRC-3, a Steroid Receptor Coactivator: Implication in Cancer.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Steroid receptor coactivators as therapeutic targets in the female reproductive system.The Journal of steroid biochemistry and molecular biology · 2015
    Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Prostate cancer-associated mutations in speckle-type POZ protein (SPOP) regulate steroid receptor coactivator 3 protein turnover.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Chao LiDepartment of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Yao-Yun Liang
Xin-Hua Feng
Sophia Y Tsai
Ming-Jer Tsai
Bert W O'Malley
Baylor College of Medicine · US

Funding

ProteomicsU19DK062434 · NIDDK · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI MANGELSDORF, DAVID J · 2002 to 2011
$37.4M
REPRODUCTIVE HORMONES: BIOLOGICAL AND MOLECULAR ACTIONSR01HD008188 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI DAVID M LONARD, JOHN P LYDON · 1985 to 2026
$16.3M
RAT PUP HUDDLING: INTEGRATING MODELS AND EXPERIMENTSF32HD008188 · NICHD · INDIANA UNIVERSITY BLOOMINGTON · PI SCHANK, JEFFREY C · 1996 to 1998
–
NICHD NIH HHS F32 HD008188NICHD NIH HHS HD08818NICHD NIH HHS R01 HD008188NIDDK NIH HHS U19 DK062434
6 · The paper itself

Abstract

SRC-3/AIB1 is a master growth coactivator and oncogene, and phosphorylation activates it into a powerful coregulator. Dephosphorylation is a potential regulatory mechanism for SRC-3 function, but the identity of such phosphatases remains unexplored. Herein, we report that, using functional genomic screening of human Ser/Thr phosphatases targeting SRC-3's known phosphorylation sites, the phosphatases PDXP, PP1, and PP2A were identified to be key negative regulators of SRC-3 transcriptional coregulatory activity in steroid receptor signalings. PDXP and PP2A dephosphorylate SRC-3 and inhibit its ligand-dependent association with estrogen receptor. PP1 stabilizes SRC-3 protein by blocking its proteasome-dependent turnover through dephosphorylation of two previously unidentified phosphorylation sites (Ser101 and S102) required for activity. These two sites are located within a degron of SRC-3 and are primary determinants of SRC-3 turnover. Moreover, PP1 regulates the oncogenic cell proliferation and invasion functions of SRC-3 in breast cancer cells.

Indexed as

Breast NeoplasmsGene Expression RegulationGenomeHeLa CellsHumansNuclear Receptor Coactivator 3Phosphoprotein PhosphatasesPhosphoproteinsPhosphoric Monoester HydrolasesPhosphorylationPhosphoserineProteasome Endopeptidase ComplexProtein BindingProtein Phosphatase 1Protein Phosphatase 2Receptors, EstrogenNuclear Receptor Coactivator 3PDXP protein, humanPhosphoprotein PhosphatasesPhosphoproteinsPhosphoric Monoester HydrolasesPhosphoserineProteasome Endopeptidase ComplexProtein Phosphatase 1Protein Phosphatase 2Receptors, EstrogenRNA, Small InterferingTranscription Factors

Identifiers

PMID18922467
PMCPMC2597059
OpenAlexW2089722059

What OpenQuestion holds

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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.