Linked Life Data

21616089

Source:http://linkedlifedata.com/resource/pubmed/id/21616089

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-7-11
pubmed:abstractText
Dioxins, including 2,3,7,8 tetrachlorodibenzo-p-dioxin (TCDD), produce a wide range of toxic effects in mammals. Most, if not all, of these toxic effects are regulated by the aryl hydrocarbon receptor (AHR). The AHR is a ligand activated transcription factor that has been shown to interact with numerous proteins capable of influencing the receptor's function. The ability of secondary proteins to alter AHR-mediated transcriptional events, a necessary step for toxicity, led us to determine whether additional interacting proteins could be identified. To this end, we have employed tandem affinity purification (TAP) of the AHR in Hepa1c1c7 cells. TAP of the AHR, followed by mass spectrometry (MS) identified ATP5?1, a subunit of the ATP synthase complex, as a strong AHR interactor in the absence of ligand. The interaction was lost upon exposure to TCDD. The association was confirmed by co-immunoprecipitation in multiple cell lines. In addition, cell fractionation experiments showed that a fraction of the AHR is found in the mitochondria. To ascribe a potential functional role to the AHR:ATP5?1 interaction, TCDD was shown to induce a hyperpolarization of the mitochondrial membrane in an AHR-dependent and transcription-independent manner. These results suggest that a fraction of the total cellular AHR pool is localized to the mitochondria and contributes to the organelle's homeostasis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1096-0333
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
299-310
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed-meshheading:21616089-ATP Synthetase Complexes, pubmed-meshheading:21616089-Amino Acid Sequence, pubmed-meshheading:21616089-Animals, pubmed-meshheading:21616089-Cell Line, pubmed-meshheading:21616089-Cell Line, Tumor, pubmed-meshheading:21616089-Homeostasis, pubmed-meshheading:21616089-Mice, pubmed-meshheading:21616089-Mice, Knockout, pubmed-meshheading:21616089-Mitochondria, pubmed-meshheading:21616089-Mitochondrial Proteins, pubmed-meshheading:21616089-Mitochondrial Proton-Translocating ATPases, pubmed-meshheading:21616089-Molecular Sequence Data, pubmed-meshheading:21616089-Oxidative Phosphorylation Coupling Factors, pubmed-meshheading:21616089-Protein Binding, pubmed-meshheading:21616089-Protein Subunits, pubmed-meshheading:21616089-Receptors, Aryl Hydrocarbon, pubmed-meshheading:21616089-Tetrachlorodibenzodioxin
pubmed:year
2011
pubmed:articleTitle
The aryl hydrocarbon receptor interacts with ATP5?1, a subunit of the ATP synthase complex, and modulates mitochondrial function.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824-1319, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, N.I.H., Extramural