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CREB-Binding Protein in Androgen Receptor-Mediated Signaling

Aarnisalo, Piia ; Palvimo, Jorma J. ; Janne, Olli A.

Proceedings of the National Academy of Sciences - PNAS, 1998-03, Vol.95 (5), p.2122-2127 [Periódico revisado por pares]

United States: National Academy of Sciences of the United States of America

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Título:
CREB-Binding Protein in Androgen Receptor-Mediated Signaling
Autor: Aarnisalo, Piia ; Palvimo, Jorma J. ; Janne, Olli A.
Assuntos: Androgens ; Animals ; Antibodies ; Binding Sites ; Biochemistry ; Biological Sciences ; Cell Line ; Cells ; COS Cells ; CREB-Binding Protein ; Deoxyribonucleic acid ; DNA ; Humans ; Kinetics ; Mutation ; Nuclear Proteins - chemistry ; Nuclear Proteins - metabolism ; Protein Engineering ; Proteins ; Rats ; Receptors ; Receptors, Androgen - chemistry ; Receptors, Androgen - metabolism ; Receptors, Glucocorticoid - biosynthesis ; Receptors, Glucocorticoid - metabolism ; Reporter genes ; Repression ; Sequence Deletion ; Signal Transduction ; Testosterone ; Trans-Activators ; Transactivation ; Transcription Factor AP-1 - biosynthesis ; Transcription Factors - chemistry ; Transcription Factors - metabolism ; Transcription, Genetic ; Transcriptional Activation ; Transfection
É parte de: Proceedings of the National Academy of Sciences - PNAS, 1998-03, Vol.95 (5), p.2122-2127
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
Edited by Elwood V. Jensen, University of Hamburg, Hamburg, Germany, and approved December 23, 1997
To whom reprint requests should be addressed at: Institute of Biomedicine, Department of Physiology, P.O. Box 9 (Siltavuorenpenger 20 J), FIN-00014 Helsinki, Finland. e-mail: olli.janne@helsinki.fi.
Descrição: CREB-binding protein (CBP) is a transcriptional coregulator that interacts with different DNA binding proteins and components of the general transcription machinery. CBP enhanced androgen receptor (AR)-dependent transcription under transient transfection conditions in CV-1 cells. The ligand binding domain (LBD) and residues 38-296 of the N-terminal region of AR are not required because the activity of a receptor mutant devoid of these domains was augmented by coexpressed CBP. There is physical interaction between AR and CBP in vivo, as judged by coimmunoprecipitation experiments from cell extracts. Consistent with the role of CBP as a coactivator for AR, the 12S E1A adenoviral protein that inactivates CBP function strongly inhibited AR-dependent transactivation. Exogenous CBP was also capable of overcoming the inhibitory effect of AR on AP-1 activity and diminished the mutual transcriptional repression between AR and NF-κ B (RelA). Collectively, these data imply that transcriptional interference between AR and AP-1 or NF-κ B is mediated, at least in part, through competition for intracellular CBP and that this coactivator serves as an integrator between androgen-mediated and other signaling pathways.
Editor: United States: National Academy of Sciences of the United States of America
Idioma: Inglês

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CREB-Binding Protein in Androgen Receptor-Mediated Signaling

Aarnisalo, Piia ; Palvimo, Jorma J. ; Janne, Olli A.

United States: National Academy of Sciences of the United States of America

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