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PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X

Mynol I Vhuiyan1, Magnolia L Pak1, Margaret A Park2

  • 1Faculty of Pharmaceutical Sciences, The University of British Columbia, Vancouver, BC V6T 1Z3, Canada.

Journal of Biochemistry
|January 7, 2017
PubMed

Insights

Protein arginine N-methyltransferase 2 (PRMT2) interacts with splicing factor SAM68, influencing BCL-X alternative splicing. This suggests PRMT2 plays a role in inflammation-related alternative splicing regulation.

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Protein arginine N-methyltransferase 2 (PRMT2) is involved in crucial cellular signaling pathways, including JAK-STAT and Wnt/β-catenin.
  • PRMT2 acts as a transcriptional co-activator and represses key transcription factors like NF-κB and E2F1, promoting apoptosis.
  • Previous research established PRMT2's interaction with and activation of PRMT1.

Purpose of the Study:

  • To investigate the interaction between PRMT2 and splicing factors.
  • To determine the role of PRMT2 in the regulation of BCL-X alternative splicing.
  • To explore PRMT2's function in inflammation-induced cellular processes.

Main Methods:

  • Proteomics was employed to identify proteins interacting with the PRMT2 SH3 domain.
  • Cellular interaction and subcellular localization of PRMT2 and SAM68 were analyzed.
  • The impact of PRMT2 expression on BCL-X alternative splicing was assessed in stimulated cells.

Main Results:

  • Proteomics revealed associations between the PRMT2 SH3 domain and splicing factors, notably SAM68.
  • PRMT2 was found to interact with SAM68 and regulate its subcellular localization.
  • Expression of wild-type PRMT2 increased the BCL-X(L)/BCL-X(s) ratio in TNF-α or LPS-stimulated cells.

Conclusions:

  • PRMT2 interacts with SAM68, a key regulator of BCL-X alternative splicing.
  • PRMT2's interaction with SAM68 and its effect on subcellular localization suggest a role in alternative splicing.
  • Active PRMT2 may contribute to alternative splicing regulation during inflammatory responses.
Keywords:
BCL-XPRMT2SAM68SH3 domainalternative splicing

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