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(Received for publication, July 16, 1997)
From the Genetisches Institut der Justus-Liebig-Universität, The glucocorticoid receptor (GR) is a
ligand-dependent transcription factor that is able to
modulate gene activity by binding to its response element, interacting
with other transcription factors, and contacting several accessory
proteins such as coactivators. Here we show that GRIP120, one of the
factors we have identified to interact with the glucocorticoid
receptor, is identical to the heterogeneous nuclear ribonucleoprotein U
(hnRNP U), a nuclear matrix protein binding to RNA as well as to
scaffold attachment regions. GR·hnRNP U complexes were identified by
blotting and coimmunoprecipitation. The subnuclear distribution of GR
and hnRNP U was characterized by indirect immunofluorescent labeling
and confocal laser microscopy demonstrating a colocalization of both proteins. Using a nuclear transport-deficient deletion of hnRNP U,
nuclear translocation was seen to be dependent on GR and dexamethasone. Transient transfections were used to identify possible interaction domains. Overexpressed hnRNP U interfered with glucocorticoid induction, and the COOH-terminal domains of both proteins were sufficient in mediating the transcriptional interference. A possible functional role for this GR binding-protein in addition to its binding
to the nuclear matrix, to RNA, and to scaffold attachment regions is
discussed.
Volume 272, Number 45,
Issue of November 7, 1997
pp. 28471-28478
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
The Glucocorticoid Receptor Is Associated with the RNA-binding
Nuclear Matrix Protein hnRNP U
Institut
für Angewandte Physik,
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