Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140 (Q24290971)

glucocorticoid receptor binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

J Zilliacus

1

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E Holter

2

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H Wakui

3

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H Tazawa

4

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E Treuter

5

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J A Gustafsson

Bcr and Raf form a complex in vivo via 14-3-3 proteins.

6

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language of work or name

English

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publication date

April 2001

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published in

Molecular Endocrinology

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volume

15

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page(s)

501-11

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issue

4

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cites work

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14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase

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Targets of activated steroid hormone receptors: basal transcription factors and receptor interacting proteins.

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The nuclear receptor superfamily: the second decade

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14-3-3 and its possible role in co-ordinating multiple signalling pathways.

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Increasing the complexity of coactivation in nuclear receptor signaling

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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The nuclear-receptor interacting protein (RIP) 140 binds to the human glucocorticoid receptor and modulates hormone-dependent transactivation

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Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein

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The CBP co-activator is a histone acetyltransferase

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14-3-3beta protein associates with insulin receptor substrate 1 and decreases insulin-stimulated phosphatidylinositol 3'-kinase activity in 3T3L1 adipocytes

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Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids

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