Posttranslational arginine methylation of lamin A/C during myoblast fusion

Su Jin Kim, Byong Chul Yoo, Chang Sub Uhm, Sang-Won Lee

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Protein arginine methylation is a major posttranslational modification that regulates various cellular functions, such as RNA processing and DNA repair. A recent report showed the involvement of protein arginine methyltransferase (PRMT) 4 in chromatin remodeling and gene expression during muscle differentiation in C2C12 cells. Because the fusion of myoblasts is a unique phenomenon observed in skeletal muscle differentiation, the present study focused on the expression and activities of PRMTs during myoblast fusion in primary rat skeletal muscle. NG, NG-asymmetric dimethylarginines (aDMA) and NG, N′G-symmetric dimethylarginines (sDMA) were both found consistently throughout myoblast fusion. However, PRMT1 exhibited the highest activity during myoblast fusion and maintained the elevated activity thereafter, whereas PRMT5 reached its highest activity only after myoblast fusion. To identify the proteins modified by such PRMTs, we conducted 2-dimensional electrophoresis (2-DE) of total proteins before and after myoblast fusion, and protein spots on the 2-DE gel immunoreactive for aDMA and sDMA were identified by mass spectrometric analysis. Among the proteins identified, lamin C2 was in particular observed to be dimethylated. Arginine methylation of lamin may therefore be important for muscle development and maintenance.

Original languageEnglish
Pages (from-to)308-317
Number of pages10
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1814
Issue number2
DOIs
Publication statusPublished - 2011 Feb 1

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Keywords

  • Lamin A/C
  • Mass spectrometry
  • Protein arginine methylation
  • Skeletal muscle differentiation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Analytical Chemistry
  • Molecular Biology

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