Evidence map›Paper›PMID 17368182›Full record

ArticleThe Journal of steroid biochemistry and molecular biology2007

Phosphorylation at serine 208 of the 1alpha,25-dihydroxy Vitamin D3 receptor modulates the interaction with transcriptional coactivators.

Gloria Arriagada, Roberto Paredes, Juan Olate, Andre van Wijnen, Jane B Lian, Gary S Stein, Janet L Stein, Sergio Onate, Martin Montecino

Open access · greenAbstract read
In one paragraph

Article in The Journal of steroid biochemistry and molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Vitamin D Receptor Regulates the Expression of the Grainyhead-Like 1 Gene.International journal of molecular sciences · 2024
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The impact of VDR expression and regulation in vivo.The Journal of steroid biochemistry and molecular biology · 2018
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Glucocorticoid regulation of the vitamin D receptor.The Journal of steroid biochemistry and molecular biology · 2010
    Article
  17. Article
  18. 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.

Gloria ArriagadaDepartamento de Bioquimica y Biologia Molecular, Facultad de Ciencias Biologicas, Universidad de Concepcion, Casilla 160-C, Concepcion, Chile.
Roberto Paredes
Juan Olate
Andre van Wijnen
Jane B Lian
Gary S Stein
Janet L Stein
Sergio Onate
Martin Montecino
University of Concepción · CLUniversity of Massachusetts Chan Medical School · USRoswell Park Comprehensive Cancer Center · US

Funding

Subnuclear Integration of Regulatory Signals Controlling Bone Cell FunctionP01AR048818 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEIN, JANET L · 2002 to 2011
$14.0M
Molecular Control of Bone FormationR01AR049069 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI WESTENDORF, JENNIFER J · 2003 to 2021
$5.8M
NIAMS NIH HHS P01 AR048818NIAMS NIH HHS P01 AR 48818NIAMS NIH HHS R01 AR049069
6 · The paper itself

Abstract

Upon ligand binding the 1alpha,25-dihydroxy Vitamin D3 receptor (VDR) undergoes a conformational change that allows interaction with coactivator proteins including p160/SRC family members and the multimeric DRIP complex through the DRIP205 subunit. Casein kinase II (CKII) phosphorylates VDR both in vitro and in vivo at serine 208 within the hinge domain. This phosphorylation does not affect the ability of VDR to bind DNA, but increases its ability to transactivate target promoters. Here, we have analyzed whether phosphorylation of VDR by CKII modulates the ability of VDR to interact with coactivators in vitro. We find that both mutation of serine 208 to aspartic acid (VDRS208D) or phosphorylation of VDR by CKII enhance the interaction of VDR with DRIP205 in the presence of 1alpha,25-dihydroxy Vitamin D3. We also find that the mutation VDRS208D neither affects the ability of this protein to bind DNA nor to interact with SRC-1 and RXRalpha. Together, our results indicate that phosphorylation of VDR at serine 208 contributes to modulate the affinity of VDR for the DRIP complex and therefore may have a role in vivo regulating VDR-mediated transcriptional enhancement.

Indexed as

MutationPhosphoserineProtein BindingReceptors, CalcitriolTrans-ActivatorsPhosphoserineReceptors, CalcitriolTrans-Activators

Identifiers

PMID17368182
PMCPMC3118558
OpenAlexW2092445159

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.