MAP kinases couple multiple functions of human progesterone receptors: degradation, transcriptional synergy, and nuclear association (Q35207726)

7 August 2017

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title

MAP kinases couple multiple functions of human progesterone receptors: degradation, transcriptional synergy, and nuclear association (English)

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7 August 2017

2

Carol A Lange

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7 August 2017

Ming Qiu

1

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PubMed ID

12943699

7 August 2017

language of work or name

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1 June 2003

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The Journal of Steroid Biochemistry and Molecular Biology

7 August 2017

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7 August 2017

85

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7 August 2017

2-5

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7 August 2017

147-157

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Measurement of steroid hormone receptors in breast cancer patients on tamoxifen

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Convergence of progesterone and epidermal growth factor signaling in breast cancer. Potentiation of mitogen-activated protein kinase pathways

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Hypothesis: Progesterone primes breast cancer cells for cross-talk with proliferative or antiproliferative signals

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Ras-dependent growth factor regulation of MEK kinase in PC12 cells

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Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK

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Transcriptional hyperactivity of human progesterone receptors is coupled to their ligand-dependent down-regulation by mitogen-activated protein kinase-dependent phosphorylation of serine 294.

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Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase

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Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome

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Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites

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Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases

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Constitutive activation of the 41-/43-kDa mitogen-activated protein kinase signaling pathway in human tumors

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Hyperexpression of mitogen-activated protein kinase in human breast cancer

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A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf

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The human estrogen receptor-alpha is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators

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F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex

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p34Cdc28-mediated control of Cln3 cyclin degradation

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Cyclin is degraded by the ubiquitin pathway

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Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates

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Roles of ubiquitin-mediated proteolysis in cell cycle control

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Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin

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Mitogen-activated protein kinase regulates nuclear association of human progesterone receptors.

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A sequence in the 5' flanking region confers progestin responsiveness on the human c-myc gene

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Inhibition of transcription selectively reduces the level of ubiquitinated histone H2B in chromatin

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Regulation of transcriptional activation domain function by ubiquitin

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The 26S proteasome is required for estrogen receptor-alpha and coactivator turnover and for efficient estrogen receptor-alpha transactivation

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Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody

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Modulation of AP-1 activity by the human progesterone receptor in endometrial adenocarcinoma cells

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Heregulin induces transcriptional activation of the progesterone receptor by a mechanism that requires functional ErbB-2 and mitogen-activated protein kinase activation in breast cancer cells.

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Effect of hormone replacement therapy on breast cancer risk: estrogen versus estrogen plus progestin

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Identifiers

DOI

1 reference

7 August 2017

1 reference

PubMed ID

12943699