CREB-binding protein (CREBBP) and preeclampsia: a new promising target gene

2021 ◽  
Vol 48 (3) ◽  
pp. 2117-2122
Author(s):  
Hossein Sadeghi ◽  
Sahra Esmkhani ◽  
Reihaneh Pirjani ◽  
Mona Amin-Beidokhti ◽  
Milad Gholami ◽  
...  
Keyword(s):  
Target Gene ◽  
Binding Protein ◽  
Creb Binding Protein ◽  
Promising Target

scholarly journals The Hormonal Response of Estrogen Receptor β Is Decreased by the Phosphatidylinositol 3-Kinase/Akt Pathway via a Phosphorylation-dependent Release of CREB-binding Protein

2006 ◽  
Vol 282 (7) ◽  
pp. 4830-4840 ◽  
Author(s):  
Mélanie Sanchez ◽  
Karine Sauvé ◽  
Nathalie Picard ◽  
André Tremblay
Keyword(s):  
Target Gene ◽  
Binding Protein ◽  
Intrinsic Activity ◽  
Akt Pathway ◽  
Creb Binding Protein ◽  
Transcriptional Coactivator ◽  
Phosphatidylinositol 3 Kinase ◽  
Hormonal Response ◽  
Reduced Activity ◽  
Phosphatidylinositol 3

The hormonal response of estrogen receptors (ER) α and ERβ is controlled by a number of cofactors, including the general transcriptional coactivator CREB-binding protein (CBP). Growing evidence suggests that specific kinase signaling events also modulate the formation and activity of the ER coactivation complex. Here we show that ERβ activity and target gene expression are decreased upon activation of ErbB2/ErbB3 receptors despite the presence of CBP. This inhibition of ERβ involved activation of the phosphatidylinositol 3-kinase/Akt pathway, abrogating the potential of CBP to facilitate ERβ response to estrogen. Such reduced activity was associated with an impaired ability of ERβ to recruit CBP upon activation of Akt. Mutation of serine 255, an Akt consensus site contained in the hinge region of ERβ, prevented the release of CBP and rendered ERβ transcriptionally more responsive to CBP coactivation, suggesting that Ser-255 may serve as a regulatory site to restrain ERβ activity in Akt-activated cells. In contrast, we found that CBP intrinsic activity was increased by Akt through threonine 1872, a consensus site for Akt in the cysteine- and histidine-rich 3 domain of CBP, indicating that such enhanced transcriptional potential of CBP did not serve to activate ERβ. Interestingly, nuclear receptors sharing a conserved Akt consensus site with ERβ also exhibit a reduced ability to be coactivated by CBP, whereas others missing that site were able to benefit from the activation of CBP by Akt. These results therefore outline a regulatory mechanism by which the phosphatidylinositol 3-kinase/Akt pathway may discriminate nuclear receptor response through coactivator transcriptional competence.

scholarly journals EWS-ATF-1 chimeric protein in soft tissue clear cell sarcoma associates with CREB-binding protein and interferes with p53-mediated trans-activation function

Oncogene ◽  
2001 ◽  
Vol 20 (46) ◽  
pp. 6653-6659 ◽  
Author(s):  
Yasuo Fujimura ◽  
Habibur Siddique ◽  
Leo Lee ◽  
Veena N Rao ◽  
E Shyam P Reddy
Keyword(s):  
Soft Tissue ◽  
Clear Cell ◽  
Binding Protein ◽  
Chimeric Protein ◽  
Clear Cell Sarcoma ◽  
Activation Function ◽  
Creb Binding Protein ◽  
Cell Sarcoma

scholarly journals p300/cAMP-response-element-binding-protein ('CREB')-binding protein (CBP) modulates co-operation between myocyte enhancer factor 2A (MEF2A) and thyroid hormone receptor-retinoid X receptor

2003 ◽  
Vol 369 (3) ◽  
pp. 477-484 ◽  
Author(s):  
Antonio De LUCA ◽  
Anna SEVERINO ◽  
Paola De PAOLIS ◽  
Giuliano COTTONE ◽  
Luca De LUCA ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Binding Protein ◽  
Camp Response Element Binding ◽  
Creb Binding Protein ◽  
Camp Response Element ◽  
Response Element ◽  
Adenovirus E1a ◽  
Element Binding Protein ◽  
Enhancer Factor

Thyroid hormone receptors (TRs) and members of the myocyte enhancer factor 2 (MEF2) family are involved in the regulation of muscle-specific gene expression during myogenesis. Physical interaction between these two factors is required to synergistically activate gene transcription. p300/cAMP-response-element-binding-protein ('CREB')-binding protein (CBP) interacting with transcription factors is able to increase their activity on target gene promoters. We investigated the role of p300 in regulating the TR—MEF2A complex. To this end, we mapped the regions of these proteins involved in physical interactions and we evaluated the expression of a chloramphenicol acetyltransferase (CAT) reporter gene in U2OS cells under control of the α-myosin heavy chain promoter containing the thyroid hormone response element (TRE). Our results suggested a role of p300/CBP in mediating the transactivation effects of the TR—retenoid X receptor (RxR)—MEF2A complex. Our findings showed that the same C-terminal portion of p300 binds the N-terminal domains of both TR and MEF2A, and our in vivo studies demonstrated that TR, MEF2A and p300 form a ternary complex. Moreover, by the use of CAT assays, we demonstrated that adenovirus E1A inhibits activation of transcription by TR—RxR—MEF2A—p300 but not by TR—RxR—MEF2A. Our data suggested that p300 can bind and modulate the activity of TR—RxR—MEF2A at TRE. In addition, it is speculated that p300 might modulate the activity of the TR—RxR—MEF2A complex by recruiting a hypothetical endogenous inhibitor which may act like adenovirus E1A.

scholarly journals The CREB-binding protein affects the circadian regulation of behaviour

FEBS Letters ◽  
2016 ◽  
Vol 590 (18) ◽  
pp. 3213-3220 ◽  
Author(s):  
Christian Maurer ◽  
Tobias Winter ◽  
Siwei Chen ◽  
Hsiu-Cheng Hung ◽  
Frank Weber
Keyword(s):  
Binding Protein ◽  
Circadian Regulation ◽  
Creb Binding Protein

scholarly journals Acetylation of cAMP-responsive Element-binding Protein (CREB) by CREB-binding Protein Enhances CREB-dependent Transcription

2003 ◽  
Vol 278 (18) ◽  
pp. 15727-15734 ◽  
Author(s):  
Qing Lu ◽  
Amanda E. Hutchins ◽  
Colleen M. Doyle ◽  
James R. Lundblad ◽  
Roland P. S. Kwok
Keyword(s):  
Binding Protein ◽  
Creb Binding Protein ◽  
Element Binding Protein ◽  
Responsive Element ◽  
Camp Responsive Element Binding

scholarly journals p300/CREB Binding Protein-Related Protein p270 Is a Component of Mammalian SWI/SNF Complexes

1998 ◽  
Vol 18 (6) ◽  
pp. 3596-3603 ◽  
Author(s):  
Peter B. Dallas ◽  
Ian Wayne Cheney ◽  
Da-Wei Liao ◽  
Valerie Bowrin ◽  
Whitney Byam ◽  
...  
Keyword(s):  
Hormone Receptors ◽  
Binding Protein ◽  
Chromatin Modification ◽  
Cellular Protein ◽  
Cellular Proteins ◽  
Creb Binding Protein ◽  
Detailed Characterization ◽  
Molecular Masses ◽  
Histone Acetyltransferase Activity

ABSTRACT p300 and the closely related CREB binding protein (CBP) are transcriptional adaptors that are present in intracellular complexes with TATA binding protein (TBP) and bind to upstream activators including p53 and nuclear hormone receptors. They have intrinsic and associated histone acetyltransferase activity, suggesting that chromatin modification is an essential part of their role in regulating transcription. Detailed characterization of a panel of antibodies raised against p300/CBP has revealed the existence of a 270-kDa cellular protein, p270, distinct from p300 and CBP but sharing at least two independent epitopes with p300. The subset of p300/CBP-derived antibodies that cross-reacts with p270 consistently coprecipitates a series a cellular proteins with relative molecular masses ranging from 44 to 190 kDa. Purification and analysis of various proteins in this group reveals that they are components of the human SWI/SNF complex and that p270 is an integral member of this complex.

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