A dopamine-responsive domain in the N-terminal sequence of Pit-1. Transcriptional inhibition in endocrine cell types

J Biol Chem. 1995 Mar 31;270(13):7156-60. doi: 10.1074/jbc.270.13.7156.

Abstract

The POU transcription factor Pit-1 activates the prolactin gene in pituitary lactotrophs and may integrate responses of the gene to external signals. To study the role of Pit-1 in dopaminergic inhibition of the prolactin gene, we transiently transfected Pit-1 and dopamine D2 receptor vectors into a series of heterologous cell lines and examined dopamine regulation of the prolactin gene promoter. Regulation was Pit-1-dependent in all cell lines tested. Moreover, dopamine responsiveness was cell type-specific: stimulatory in fibroblasts (COS-7) and muscle-type cells (P19/Me2SO-induced) and inhibitory in pancreatic endocrine (RIN, InR1-G9) and neural-like (P19/retinoic acid-induced) cells. Because dopaminergic responses in Pit-1-transfected RIN cells paralleled those in pituitary GH4 cells, the islet cell line was used to test for sequences in Pit-1 that mediate negative hormone signals. Dopamine responsiveness of the Pit-1 transactivation domain (residues 8-80) was examined using a chimeric LexA construct. LxPit-1, LxSp1, and Lx-glucocorticoid receptor fusions all activated basal transcription, but only LxPit-1 was regulated by dopamine. Regulatory responses of LxPit-1 and full-length Pit-1 were quantitatively similar. In addition, gain-of-function G alpha mutants that inhibit Pit-1-dependent promoters in GH4 cells also suppressed selectively Pit-1- or LxPit-1-dependent promoters in RIN cells. This demonstrates that Pit-1 can function as a specific target for distinct inhibitory G protein signals. Interestingly, Pit-1 sequences N-terminal to the DNA-binding POU domain appear to be sufficient in mediating regulation by these pathways.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Cell Line
  • Chlorocebus aethiops
  • DNA-Binding Proteins / biosynthesis
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Dopamine / pharmacology*
  • Fibroblasts
  • Islets of Langerhans
  • Kidney
  • Luciferases / biosynthesis
  • Muscles
  • Pituitary Gland
  • Prolactin / biosynthesis*
  • Promoter Regions, Genetic* / drug effects
  • Rats
  • Receptors, Dopamine D2 / biosynthesis
  • Receptors, Dopamine D2 / metabolism*
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / metabolism
  • Serine Endopeptidases*
  • Transcription Factor Pit-1
  • Transcription Factors / biosynthesis
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • Transcription, Genetic / drug effects
  • Transfection

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • LexA protein, Bacteria
  • Pou1f1 protein, rat
  • Receptors, Dopamine D2
  • Recombinant Fusion Proteins
  • Transcription Factor Pit-1
  • Transcription Factors
  • Prolactin
  • Luciferases
  • Serine Endopeptidases
  • Dopamine