Evidence map›Paper›PMID 22626544›Full record

ArticleThe Journal of steroid biochemistry and molecular biology2012

Discovery of novel vitamin D receptor interacting proteins that modulate 1,25-dihydroxyvitamin D3 signaling.

Pamela A Marshall, Zachary Hernandez, Ichiro Kaneko, Tim Widener, Christa Tabacaru, Izayadeth Aguayo, Peter W Jurutka

Abstract read
In one paragraph

Article in The Journal of steroid biochemistry and molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 32% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. CXXC5 is a ubiquitinated protein and is degraded by the ubiquitin-proteasome pathway.Protein science : a publication of the Protein Society · 2025
    Article
  4. Signal integrator function of CXXC5 in Cancer.Cell communication and signaling : CCS · 2025
    Review
  5. Article
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  8. Article
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  12. Review
  13. Article
  14. A brief history of rickets.Pediatric nephrology (Berlin, Germany) · 2020
    Review
  15. Article
  16. CXXC5: A novel regulator and coordinator of TGF-β, BMP and Wnt signaling.Journal of cellular and molecular medicine · 2019
    Review
  17. Article
  18. Article
  19. PTH and Vitamin D.Comprehensive Physiology · 2016
    Review
  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

7 authors at 2 institutions in 1 country.

Pamela A MarshallDivision of Mathematical and Natural Sciences, Arizona State University, Glendale, AZ 85306, United States.
Zachary Hernandez
Ichiro Kaneko
Tim Widener
Christa Tabacaru
Izayadeth Aguayo
Peter W Jurutka
Arizona State University · USUniversity of Arizona · US

Funding

Vitamin D Hormone Signaling in Bone Mineral HomeostasisR01DK033351 · NIDDK · UNIVERSITY OF ARIZONA · PI HAUSSLER, MARK R · 1986 to 2010
$2.8M
Howard Hughes Medical InstituteNIDDK NIH HHS R01 DK033351
6 · The paper itself

Abstract

The nuclear vitamin D receptor (VDR) modulates gene transcription in 1,25-dihydroxyvitamin D(3) (1,25D) target tissues such as kidney, intestine, and bone. VDR is also expressed in heart, and 1,25D deficiency may play a role in the acceleration of cardiovascular disease. Employing a yeast two-hybrid system and a human heart library, using both a 1,25D-independent and 1,25D-dependent screen, we discovered six candidate VDR interacting proteins (VIPs). These novel VIPs include CXXC5, FASTK, NR4A1, TPM2, MYL3 and XIRP1. Mammalian two-hybrid assays as well as GST pull-downs were used to confirm VIP-VDR interaction, and the combination of these two assays reveals that CXXC5, XIRP1, FASTK and NR4A1 interactions with VDR may be modulated by 1,25D. The functional effects of these VIPs on 1,25D-mediated gene expression were explored in transcriptional assays employing three separate and distinct 1,25D-responsive element (VDRE)-driven luciferase reporter genes in transfected Caco-2 and HEK-293 cells, and in a C2C12 myoblast line. FASTK and TPM2 activated expression in all cell line and promoter contexts, while CXXC5 and XIRP1 exhibited differing effects depending on the cell line and promoter employed, suggesting promoter and cell-specific effects of these unique VIPs on VDR signaling. Further evaluation of the interaction between CXXC5 and VDR revealed that CXXC5 acts in a dose-dependent manner to stimulate VDR-mediated transcription on select VDREs. Identification of novel heart VIPs and their influence on VDR activity may increase our understanding of how vitamin D impacts cardiac physiology and may facilitate development of VDR/VIP drug analogs to combat heart disease.

Indexed as

AnimalsCaco-2 CellsCarrier ProteinsCell LineDNA-Binding ProteinsHCT116 CellsHEK293 CellsHumansMiceMyocardiumNuclear ProteinsNuclear Receptor Subfamily 4, Group A, Member 1Protein Serine-Threonine KinasesReceptors, CalcitriolTranscription FactorsTropomyosinCarrier ProteinsCXXC5 protein, humandihydroxy-vitamin D3DNA-Binding ProteinsFASTK protein, humanNR4A1 protein, humanNuclear ProteinsNuclear Receptor Subfamily 4, Group A, Member 1Protein Serine-Threonine KinasesReceptors, CalcitriolTPM2 protein, humanTranscription FactorsTropomyosinVitamin DXIRP1 protein, human

Identifiers

PMID22626544
PMCPMC3408799
OpenAlexW1997180266

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.