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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
Published on: August 7, 2021
Dishevelled3 is a novel arginine methyl transferase substrate
Rama Kamesh Bikkavilli1, Sreedevi Avasarala, Michelle Vanscoyk
1Division of Pulmonary Sciences and Critical Care, School of Medicine, Anschutz Medical Campus, University of Colorado Health Sciences Center, Aurora, Colorado 80045, USA. kamesh.bikkavilli@ucdenver.edu
Scientific Reports
|November 15, 2012
Summary
Arginine methylation regulates Dishevelled (Dvl) protein function in Wnt signaling. This study identifies protein arginine methyltransferases 1 and 7 as key enzymes, showing methylation acts as a switch for Wnt pathway activation.
Area of Science:
- Molecular Biology
- Cell Signaling
- Biochemistry
Background:
- Dishevelled (Dvl) is a crucial scaffold protein in Wnt-sensitive signaling pathways.
- Post-translational modifications of Dvl are critical for regulating its function.
- Understanding Dvl regulation is key to deciphering Wnt pathway dynamics.
Purpose of the Study:
- To investigate the role of arginine methylation in Dishevelled post-translational modification.
- To identify the enzymes responsible for Dishevelled methylation.
- To elucidate the impact of Dishevelled methylation on Wnt signaling activation.
Main Methods:
- In vitro and in vivo methylation assays of Dishevelled.
- Identification of protein arginine methyltransferases (PRMTs) catalyzing Dvl methylation.
- Analysis of Dishevelled localization and Wnt signaling activity using a methylation-deficient mutant (R271K) and Wnt3a stimulation in F9 teratocarcinoma cells.
Main Results:
- Dishevelled undergoes arginine methylation both in vitro and in vivo.
- Protein arginine methyltransferases 1 and 7 were identified as the primary enzymes responsible for Dishevelled methylation.
- Wnt3a stimulation led to decreased Dishevelled methylation, while a methylation-deficient mutant (R271K) showed constitutive membrane localization and enhanced Wnt signaling.
Conclusions:
- Arginine methylation serves as a critical regulatory switch for Dishevelled function.
- Differential methylation of Dishevelled plays a significant role in modulating Wnt signaling.
- This finding provides new insights into the post-translational control of Wnt pathway activity.
