Estrogen Receptor β and Its Domains Interact with Casein Kinase 2, Phosphokinase C, and N-Myristoylation Sites of Mitochondrial and Nuclear Proteins in Mouse Brain

Paramanik, Vijay; Thakur, M. K.

doi:10.1074/jbc.m112.351262

Cited by 15 publications

(8 citation statements)

References 57 publications

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“…Studies have shown that mtERβ can increase mitochondrial DNA (mtDNA)–encoded transcription of cytochrome oxidase subunits I, III, and IV; increase respiration capacity; elevate antioxidant activity; and inhibit apoptosis . Using pull‐down assays and matrix‐assisted laser desorption ionization–mass spectroscopy, ERβ has been found in the mouse brain to interact with mitochondrial casein kinase 2 and phosphokinase C, which contribute to biogenesis of the mitochondrial translocase of the outer membrane and regulate ATP‐sensitive mitochondrial potassium channels, respectively . Additionally, it has been shown that mtERβ binds to estrogen response element (ERE)–like sequences in the D‐loop of mtDNA (Fig.…”

Section: Estrogen Acts Via the Estrogen Receptor Localized Within Mitmentioning

confidence: 99%

Estrogen receptor‐β in mitochondria: implications for mitochondrial bioenergetics and tumorigenesis

Liao

Tzeng

et al. 2015

Annals of the New York Academy of Sciences

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Estrogen enhances mitochondrial function by enhancing mitochondrial biogenesis and sustaining mitochondrial energy-transducing capacity. Shifts in mitochondrial bioenergetic pathways from oxidative phosphorylation to glycolysis have been hypothesized to be involved in estrogen-induced tumorigenesis. Studies have shown that mitochondria are an important target of estrogen. Estrogen receptor-β (ERβ) has been shown to localize to mitochondria in a ligand-dependent or -independent manner and can affect mitochondrial bioenergetics and anti-apoptotic signaling. However, the functional role of mitochondrial ERβ in tumorigenesis remains unclear. Clinical studies of ERβ-related tumorigenesis have shown that ERβ stimulates mitochondrial metabolism to meet the high energy demands of processes such as cell proliferation, cell survival, and transformation. Thus, in elucidating the precise role of mitochondrial ERβ in cell transformation and tumorigenesis, it will be particularly valuable to explore new approaches for the development of medical treatments targeting mitochondrial ERβ-mediated mitochondrial function and preventing apoptosis.

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Section: Estrogen Acts Via the Estrogen Receptor Localized Within Mitmentioning

confidence: 99%

Estrogen receptor‐β in mitochondria: implications for mitochondrial bioenergetics and tumorigenesis

Liao

Tzeng

et al. 2015

Annals of the New York Academy of Sciences

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“…3A ) and/or (ii) MR co-regulators directly. For other SHRs like ERβ and GR it has been established that SHR co-regulators are phosphorylated by CK2 and thereby modulating transcriptional SHR activity 24 , 25 . So far, it is not known whether i) CK2-induced phosphorylation of MR-S459 alters the interaction with MR co-regulators, ii) MR-caveolin signaling and/or iii) whether known MR co-activators are regulated by CK2-induced phosphorylation directly which will be investigated in further experiments.…”

Section: Discussionmentioning

confidence: 99%

Modulation of transcriptional mineralocorticoid receptor activity by casein kinase 2

Ruhs

Strätz

Quarch

et al. 2017

Sci Rep

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The pathogenesis of cardiovascular diseases is a multifunctional process in which the mineralocorticoid receptor (MR), a ligand-dependent transcription factor, is involved as proven by numerous clinical studies. The development of pathophysiological MR actions depends on the existence of additional factors e.g. inflammatory cytokines and seems to involve posttranslational MR modifications e.g. phosphorylation. Casein kinase 2 (CK2) is a ubiquitously expressed multifunctional serine/threonine kinase that can be activated under inflammatory conditions as the MR. Sequence analysis and inhibitor experiments revealed that CK2 acts as a positive modulator of MR activity by facilitating MR-DNA interaction with subsequent rapid MR degradation. Peptide microarrays and site-directed mutagenesis experiments identified the highly conserved S459 as a functionally relevant CK2 phosphorylation site of the MR. Moreover, MR-CK2 protein-protein interaction mediated by HSP90 was shown by co-immunoprecipitation. During inflammation, cytokine stimulation led to a CK2-dependent increased expression of proinflammatory genes. The additional MR activation by aldosterone during cytokine stimulation augmented CK2-dependent NFκB signaling which enhanced the expression of proinflammatory genes further. Overall, in an inflammatory environment the bidirectional CK2-MR interaction aggravate the existing pathophysiological cellular situation.

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“…The lack of further evidence associated with the diagnosis of breast cancer by MALDI TOF analysis of ERs highlights the issues associated with ER protein analysis in real biological samples. However, this method demonstrates excellent results for the visualization of protein expression ( 46 , 53 ), DNA methylation status ( 54 ), monitoring of ER interactions ( 55 , 56 ) and in searching for new biomarkers for breast cancer diagnosis ( 57 , 58 ).…”

Section: Maldi Tof As a Tool For Analysis Of Ersmentioning

confidence: 99%

Identification of estrogen receptor proteins in breast cancer cells using matrix-assisted laser desorption/ionization time of flight mass spectrometry (Review)

et al. 2014

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Estrogen receptors [ERs (subtypes α and β)], classified as a nuclear receptor super family, are intracellular proteins with an important biological role as the transcription factors for estrogen target genes. For ER-induced transcription, an interaction must exist between ligand and coregulators. Coregulators may stimulate (coactivators) or inhibit (corepressors) transcription, following binding with a specific region of the gene, called the estrogen response element. Misbalanced activity of coregulators or higher ligand concentrations may cause increased cell proliferation, resulting in specific types of cancer. These are exhibited as overexpression of ER proteins. Breast cancer currently ranks first in the incidence and second in the mortality of cancer in females worldwide. In addition, 70% of breast tumors are ERα positive and the importance of these proteins for diagnostic use is indisputable. Early diagnosis of the tumor and its classification has a large influence on the selection of appropriate therapy, as ER-positive tumors demonstrate a positive response to hormonal therapy. Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI TOF MS) has been hypothesized to have great potential, as it offers reliable, robust and efficient analysis methods for biomarker monitoring and identification. The present review discusses ER protein analysis by MALDI TOF MS, including the crucial step of protein separation.

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Estrogen Receptor β and Its Domains Interact with Casein Kinase 2, Phosphokinase C, and N-Myristoylation Sites of Mitochondrial and Nuclear Proteins in Mouse Brain

Cited by 15 publications

References 57 publications

Estrogen receptor‐β in mitochondria: implications for mitochondrial bioenergetics and tumorigenesis

Estrogen receptor‐β in mitochondria: implications for mitochondrial bioenergetics and tumorigenesis

Modulation of transcriptional mineralocorticoid receptor activity by casein kinase 2

Identification of estrogen receptor proteins in breast cancer cells using matrix-assisted laser desorption/ionization time of flight mass spectrometry (Review)

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