Human vitamin D receptor phosphorylation by casein kinase II at Ser-208 potentiates transcriptional activation (Q24567897)

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S Nakajima

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C A Haussler

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G K Whitfield

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M R Haussler

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

16 April 1996

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published in

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volume

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issue

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page(s)

3519-24

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cites work

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Transcription factor TFIIB and the vitamin D receptor cooperatively activate ligand-dependent transcription.

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Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor

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Mutation of serum response factor phosphorylation sites and the mechanism by which its DNA-binding activity is increased by casein kinase II.

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Casein kinase II is a predominantly nuclear enzyme

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Phosphorylation of serine 208 in the human vitamin D receptor. The predominant amino acid phosphorylated by casein kinase II, in vitro, and identification as a significant phosphorylation site in intact cells

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The vitamin D-responsive element in the rat bone Gla protein gene is an imperfect direct repeat that cooperates with other cis-elements in 1,25-dihydroxyvitamin D3- mediated transcriptional activation.

30 May 2018

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Phosphorylation on Tyrosine ofin VitroSynthesized Human Estrogen Receptor Activates Its Hormone Binding

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Phosphorylation selectively increases triiodothyronine receptor homodimer binding to DNA

28 November 2018

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12 December 2020

The c-erbA alpha-encoded thyroid hormone receptor is phosphorylated in its amino terminal domain by casein kinase II

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12 December 2020

Phosphorylation of the 1,25-dihydroxyvitamin D3 receptor. A primary event in 1,25-dihydroxyvitamin D3 action

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12 December 2020

Hormone-dependent androgen receptor phosphorylation is accompanied by receptor transformation in human lymph node carcinoma of the prostate cells

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12 December 2020

Vitamin D receptor phosphorylation in transfected ROS 17/2.8 cells is localized to the N-terminal region of the hormone-binding domain

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12 December 2020

The C-terminal region of the vitamin D receptor is essential to form a complex with a receptor auxiliary factor required for high affinity binding to the vitamin D-responsive element

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12 December 2020

Role of acidic and phosphorylated residues in gene activation by the glucocorticoid receptor

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12 December 2020