Protein arginine methylation of CRMP and tubulin in mouse cortical neurons

Abstract

Protein arginine methylation is a common post-translational modification where methyl groups are added to the arginine residues of peptide chains. It is carried out by a group of enzymes known as protein arginine methyltransferases in eukaryotic cells. Protein arginine methylation plays an important role in many cellular functions both in the nucleus and in the cytoplasm such as the regulation of signal transduction, RNA export, and cell proliferation. However, the exact role arginine methylation plays in neurons is not yet fully understood. Previously, CRMP-2 was suggested to be asymmetrically di-methylated in mouse primary cortical neurons during Honour study. Therefore, the major aim of this study was to explore the role of arginine methylation of CRMP-2 and its binding partner, tubulin. Another aim was to investigate the enzymes that are involved in the methylation of the identified proteins. The results showed that CRMP-2 and tubulin < and R are asymmetrically dimethylated using immunoprecipitation and Western blotting. Mass spectrometry analysis identified two methylated arginine residues in CRMP-2 (R63 and R173) along with one in CRMP-1 (R226) and two methylated arginines in CRMP-3 (R238 and R270) in primary cortical neurons. In addition, two novel methylated arginines in tubulin

Date of Award	2016
Original language	English