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Article

Phosphorylation of human vitamin D receptor serine-182 by PKA suppresses 1,25(OH)2D3-dependent transactivation.

Biochemical and biophysical research communications - 12 Nov 2004

Hsieh Jui-Cheng, Dang Hope T L, Galligan Michael A, Whitfield G Kerr, Haussler Carol A, Jurutka Peter W, Haussler Mark R

Abstract excerpt

The human vitamin D receptor (hVDR), which is a substrate for several protein kinases, mediates the actions of its 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) ligand to regulate gene expression. To determine the site, and functional impact, of cAMP-dependent protein kinase (PKA)-catalyzed phosphorylation of hVDR, we generated a series of C-terminally truncated and point mutant receptors. Incubation of mutant hVDRs...

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PMID: 15474498
DOI: 10.1016/j.bbrc.2004.09.139

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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