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Control of CBP co-activating activity by arginine methylation
Martine Chevillard-Briet1, Didier Trouche, Laurence Vandel
1Laboratoire de Biologie Moléculaire Eucaryote, UMR 5099 CNRS, Institut de Biologie Cellulaire et Génétique, 118 Route de Narbonne, 31062 Toulouse cedex, France.
The EMBO Journal
|October 11, 2002
Summary
Arginine methylation by CARM1 modifies CREB binding protein (CBP) in vitro and in vivo. This methylation is critical for GRIP-1-dependent and hormone-induced gene activation, highlighting its role in co-activator function.
Area of Science:
- Molecular Biology
- Epigenetics
- Gene Regulation
Background:
- Histone acetyltransferases CREB binding protein (CBP) and p300 are crucial transcriptional co-activators.
- Nuclear receptor activation involves p160 family co-activators (e.g., GRIP-1) that recruit other co-activators.
- Arginine methyltransferase CARM1 interacts with CBP and p300 proteins.
Purpose of the Study:
- To investigate the role of CARM1-mediated arginine methylation on CBP.
- To determine if CARM1 methylates CBP in vivo.
- To assess the functional significance of CARM1-mediated CBP methylation in transcriptional activation.
Main Methods:
- In vitro methylation assays using CARM1 and CBP domains.
- In vivo methylation analysis in cellular systems.
- Functional assays measuring GRIP-1-dependent and hormone-induced transcription.
Main Results:
- CARM1 specifically methylates arginine residues in a novel domain of CBP, both in vitro and in vivo.
- CARM1-mediated methylation of these arginine residues is essential for GRIP-1-dependent transcriptional activation.
- This methylation is also critical for hormone-induced gene activation.
Conclusions:
- Arginine methylation by CARM1 is an important regulatory mechanism for CBP.
- This post-translational modification modulates co-activator function in transcriptional regulation.
- Arginine methylation plays a key role in nuclear receptor signaling pathways.