<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Okabe, Takashi</dc:creator>
  <dc:creator>Chavan, Rohit</dc:creator>
  <dc:creator>Costa, Sara S. Fonseca</dc:creator>
  <dc:creator>Brenna, Andrea</dc:creator>
  <dc:creator>Ripperger, Jürgen A.</dc:creator>
  <dc:creator>Albrecht, Urs</dc:creator>
  <dc:date>2016-11-01</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">REV-ERBα (encoded by Nr1d1) is a nuclear receptor that is part of the circadian clock  mechanism and regulates metabolism and inflammatory processes. The glucocorticoid  receptor (GR, encoded by Nr3c1) influences similar processes, but is not part of the  circadian clock, although glucocorticoid signaling affects resetting of the circadian  clock in peripheral tissues. Because of their similar impact on physiological processes,  we studied the interplay between these two nuclear receptors. We found that REV- ERBα binds to the C-terminal portion and GR to the N-terminal portion of HSP90α and  HSP90β, a chaperone responsible for the activation of proteins to ensure survival of a  cell. The presence of REV-ERBα influences the stability and nuclear localization of GR  by an unknown mechanism, thereby affecting expression of GR target genes, such as  IκBα (Nfkbia) and alcohol dehydrogenase 1 (Adh1). Our findings highlight an important  interplay between two nuclear receptors that influence the transcriptional potential of  each other. This indicates that the transcriptional landscape is strongly dependent on  dynamic processes at the protein level.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://folia.unifr.ch/global/documents/305235</dc:identifier>
  <dc:identifier>https://folia.unifr.ch/documents/305235/files/alb_ris.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.190959</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>License undefined</dc:rights>
  <dc:source>Journal of Cell Science. - 2016, vol. 129, no. 21, p. 4143–4154</dc:source>
  <dc:subject>info:eu-repo/classification/udc/57</dc:subject>
  <dc:title xmlns:ns1="xml" ns1:lang="en">REV-ERBα influences the stability and nuclear localization of the glucocorticoid receptor</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
