Polypyrimidine tract-binding protein 1 regulates the alternative splicing of dopamine receptor D2

Toshikazu Sasabe, Eugene Futai, Shoichi Ishiura

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


Dopamine receptor D2 (DRD2) has two splicing isoforms, a long form (D2L) and short form (D2S), which have distinct functions in the dopaminergic system. However, the regulatory mechanism of the alternative splicing of DRD2 is unknown. In this study, we examined which splicing factors regulate the expression of D2L and D2S by over-expressing several RNA-binding proteins in HEK293 cells. In a cellular splicing assay, the over-expression of polypyrimidine tract-binding protein 1 (PTBP1) reduced the expression of D2S, whereas the knockdown of PTBP1 increased the expression of D2S. We also identified the regions of DRD2 that are responsive to PTBP1 using heterologous minigenes and deletion mutants. Our results indicate that PTBP1 regulates the alternative splicing of DRD2. Considering that DRD2 inhibits cAMP-dependent protein kinase A, which modulates the intracellular localization of PTBP1, PTBP1 may contribute to the autoregulation of DRD2 by regulating the expression of its isoforms.

Original languageEnglish
Pages (from-to)76-81
Number of pages6
JournalJournal of Neurochemistry
Issue number1
Publication statusPublished - 2011 Jan
Externally publishedYes


  • PTBP1
  • alternative splicing
  • dopamine
  • dopamine receptor D

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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