Multiple and cooperative trans-activation domains of the human glucocorticoid receptor

Hollenberg, Stanley M.; Evans, Ronald M.

doi:10.1016/0092-8674(88)90145-6

Cited by 676 publications

(373 citation statements)

References 40 publications

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“…This combination is known to provide constitutive, hormone-, and Hsp90-independent expression of the luciferase gene (Hollenberg et al, 1987;Hollenberg and Evans, 1988). When the DJA cochaperones were overexpressed, a pattern of luciferase activity was observed similar to that of the above-mentioned experiments.…”

Section: Dja Function In Cellsmentioning

confidence: 49%

“…The sequence encoding firefly luciferase was amplified by PCR from pGL3 (Promega) and inserted into pcDNA3.1 (Invitrogen) without a tag; the pSV40-␤-galactosidase vector was from Promega. The vectors pCAGGS-PiC-3HA, pGR-⌬LBD, and pMTV-luciferase (glucocorticoid responsive element [GRE]-luciferase) were as reported previously (Hollenberg et al, 1987;Hollenberg and Evans, 1988;Brychzy et al, 2003;Young et al, 2003).…”

Section: Plasmidsmentioning

confidence: 99%

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Multiple 40-kDa Heat-Shock Protein Chaperones Function in Tom70-dependent Mitochondrial Import

Bhangoo

Tzankov

Fan

et al. 2007

MBoC

107

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Mitochondrial preproteins that are imported via the translocase of the mitochondrial outer membrane (Tom)70 receptor are complexed with cytosolic chaperones before targeting to the mitochondrial outer membrane. The adenine nucleotide transporter (ANT) follows this pathway, and its purified mature form is identical to the preprotein. Purified ANT was reconstituted with chaperones in reticulocyte lysate, and bound proteins were identified by mass spectrometry. In addition to 70-kDa heat-shock cognate protein (Hsc70) and 90-kDa heat-shock protein (Hsp90), a specific subset of cochaperones were found, but no mitochondria-specific targeting factors were found. Interestingly, three different Hsp40-related J-domain proteins were identified: DJA1, DJA2, and DJA4. The DJAs bound preproteins to different extents through their C-terminal regions. DJA dominant-negative mutants lacking the N-terminal J-domains impaired mitochondrial import. The mutants blocked the binding of Hsc70 to preprotein, but with varying efficiency. The DJAs also showed significant differences in activation of the Hsc70 ATPase and Hsc70-dependent protein refolding. In HeLa cells, the DJAs increased new protein folding and mitochondrial import, although to different extents. No single DJA was superior to the others in all aspects, but each had a profile of partial specialization. The Hsp90 cochaperones p23 and Aha1 also regulated Hsp90 -preprotein interactions. We suggest that multiple cochaperones with similar yet partially specialized properties cooperate in optimal chaperone-preprotein complexes.

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Section: Dja Function In Cellsmentioning

confidence: 49%

Section: Plasmidsmentioning

confidence: 99%

Multiple 40-kDa Heat-Shock Protein Chaperones Function in Tom70-dependent Mitochondrial Import

Bhangoo

Tzankov

Fan

et al. 2007

MBoC

107

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“…Transactivational domains were identified in the C-terminal and N-terminal regions of the receptor (Giguere et al, 1986;Webster et al, 1988;Hollenberg and Evans, 1988;Pearce and Yamamoto, 1993). These domains are important determinants of the final transcriptional efficacy (Arriza et al, 1988).…”

Section: Primary Structurementioning

confidence: 99%

Mineralocorticoid and glucocorticoid receptors in the brain. Implications for ion permeability and transmitter systems

Joëls

Kloet

1994

Progress in Neurobiology

367

168

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“…Produced by the adrenal glands under the regulation of the hypothalamus-pituitary gland axis, corticosteroids were among the first hormones to be identified and later found to exert their effects through a specific DNA-binding protein, the glucocorticoid receptor (GR) [3]. It was subsequently shown that GR can act as a liganddependent transcription factor that positively regulates genes through interaction with DNA enhancer sequences, called glucocorticoid response elements (GRE) [4,5,6]. Molecular analysis of the anti-inflammatory actions of GR later revealed a second important mechanism of GR function in the nucleus.…”

Section: Introductionmentioning

confidence: 99%

Nontranscriptional actions of the glucocorticoid receptor

Limbourg

Liao

2003

J Mol Med

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Many cellular responses to corticosteroids involve the transcriptional modulation of target genes by a prototypical nuclear receptor, the glucocorticoid receptor (GR). In the classic model of steroid hormone action GR acts as ligand-dependent transcription factor by either activating or repressing gene expression through direct interactions with DNA or other transcription factors. Recent evidence suggests an important role for nontranscriptional effects of GR in the vascular system. The nontranscriptional actions of GR involve the rapid activation of protein kinases, such as phosphatidylinositol-3 kinase and Akt, leading to the activation of endothelial nitric oxide synthase. This novel pathway of steroid hormone action protects against ischemic injury by augmenting blood flow and decreasing vascular inflammation.

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Multiple and cooperative trans-activation domains of the human glucocorticoid receptor

Cited by 676 publications

References 40 publications

Multiple 40-kDa Heat-Shock Protein Chaperones Function in Tom70-dependent Mitochondrial Import

Multiple 40-kDa Heat-Shock Protein Chaperones Function in Tom70-dependent Mitochondrial Import

Mineralocorticoid and glucocorticoid receptors in the brain. Implications for ion permeability and transmitter systems

Nontranscriptional actions of the glucocorticoid receptor

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