DARPP-32 binds to tra2-beta1 and influences alternative splicing

Biochim Biophys Acta. 2010 May-Jun;1799(5-6):448-53. doi: 10.1016/j.bbagrm.2010.01.003. Epub 2010 Jan 13.

Abstract

The majority of human genes undergo alternative splicing, which is frequently altered in response to physiological stimuli. DARPP-32 (dopamine and cAMP regulated phosphoprotein, 32kDa) is a component of PKA-dependent signaling pathways. Here we show that DARPP-32 binds directly to the splicing factor tra2-beta1 (transformer 2). DARPP-32 changes the usage of tra2-beta1 dependent alternative exons in a concentration-dependent manner, suggesting that the DARPP-32:tra2-beta1 interaction is a molecular link between signaling pathways and pre-mRNA processing.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing*
  • Animals
  • Cell Line
  • Cells, Cultured
  • Dopamine and cAMP-Regulated Phosphoprotein 32 / antagonists & inhibitors
  • Dopamine and cAMP-Regulated Phosphoprotein 32 / genetics
  • Dopamine and cAMP-Regulated Phosphoprotein 32 / metabolism*
  • Exons
  • Humans
  • In Vitro Techniques
  • Models, Biological
  • Nerve Tissue Proteins / metabolism*
  • Neurons / metabolism
  • Protein Binding
  • Protein Phosphatase 1 / metabolism
  • RNA Precursors / genetics
  • RNA Precursors / metabolism
  • RNA Processing, Post-Transcriptional
  • RNA, Small Interfering / genetics
  • RNA-Binding Proteins / metabolism*
  • Rats
  • Serine-Arginine Splicing Factors
  • Signal Transduction

Substances

  • Dopamine and cAMP-Regulated Phosphoprotein 32
  • Nerve Tissue Proteins
  • PPP1R1B protein, human
  • RNA Precursors
  • RNA, Small Interfering
  • RNA-Binding Proteins
  • TRA2B protein, human
  • Serine-Arginine Splicing Factors
  • Protein Phosphatase 1