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JAB1 interacts with both the progesterone receptor and SRC-1
A Chauchereau1, M Georgiakaki, M Perrin-Wolff
1INSERM U 135 Hormones, Genes et Reproduction, Hôpital de Bicêtre, 78 rue du Général Leclerc, 94275 Le Kremlin Bicêtre, France.
The Journal of Biological Chemistry
|March 18, 2000
Summary
Jun activation domain-binding protein-1 (JAB1) interacts with progesterone receptors and coactivators, stabilizing complexes and enhancing transcription factor activity. JAB1 is a key component of the COP9 signalosome, influencing nuclear receptor action.
Area of Science:
- Molecular Biology
- Cellular Biology
- Biochemistry
Background:
- Jun activation domain-binding protein-1 (JAB1) is known as a coactivator for the AP1 transcription factor.
- The COP9 signalosome is a large multiprotein complex involved in various cellular processes, including transcription regulation.
Purpose of the Study:
- To investigate the interaction of JAB1 with the progesterone receptor (PR) and steroid receptor coactivator 1 (SRC-1).
- To determine JAB1's role in the activity of transcription factors associated with SRC-1 and nuclear receptors.
Main Methods:
- Yeast and mammalian two-hybrid analyses were employed to study protein interactions.
- Pull-down experiments were conducted to confirm complex formation.
- The effects of JAB1 on transcription factor activity were assessed.
Main Results:
- JAB1 directly interacts with both the progesterone receptor (PR) and steroid receptor coactivator 1 (SRC-1).
- JAB1 stabilizes PR-SRC-1 complexes, enhancing the activity of transcription factors like nuclear receptors, AP1, and NF-κB without altering protein concentrations.
- JAB1, as part of the COP9 signalosome, plays a role in nuclear receptor and coactivator mechanisms.
Conclusions:
- JAB1 is a crucial regulator of nuclear receptor and coactivator function.
- The COP9 signalosome subunit JAB1 has a significant role in modulating transcription factor activity, particularly for nuclear receptors.