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Article

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

The Journal of steroid biochemistry and molecular biology - 1 Mar 2007

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

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 17368182
DOI: 10.1016/j.jsbmb.2006.12.021
PMCID: PMC3118558

Genes

VDR
SRC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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Phosphorylation at serine 208 of the 1alpha,25-dihydroxy Vitamin D3 receptor modulates the interaction with transcriptional coactivators.PMID 17368182Read ↗

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