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The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing.

The coactivator-associated arginine methyltransferase CARM1 is recruited by many different transcription factors as a positive regulator. To understand the mechanism by which CARM1 functions, we sought to isolate its substrates. We developed a small-pool screening approach for this purpose and identified CA150, SAP49, SmB, and U1C as splicing factors that are specifically methylated by CARM1. We further showed that CA150, a molecule that links transcription to splicing, interacts with the Tudor domain of the spinal muscular atrophy protein SMN in a CARM1-dependent fashion. Experiments with an exogenous splicing reporter and the endogenous CD44 gene revealed that CARM1 promotes exon skipping in an enzyme-dependent manner. The identification of splicing factors that are methylated by CARM1, and protein-protein interactions that are regulated by CARM1, strongly implicates this enzyme in the regulation of alternative splicing and points toward its involvement in spinal muscular atrophy pathogenesis.

Pubmed ID: 17218272


  • Cheng D
  • Côté J
  • Shaaban S
  • Bedford MT


Molecular cell

Publication Data

January 12, 2007

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK62248
  • Agency: NIEHS NIH HHS, Id: ES07784

Mesh Terms

  • Alternative Splicing
  • Amino Acid Motifs
  • Animals
  • Antibodies
  • Exons
  • Histones
  • Humans
  • Methylation
  • Mice
  • Nuclear Proteins
  • Protein Binding
  • Protein Methyltransferases
  • Protein Structure, Tertiary
  • Protein-Arginine N-Methyltransferases
  • RNA Processing, Post-Transcriptional
  • RNA, Messenger
  • Substrate Specificity
  • Transcription Factors
  • Transcription, Genetic