Novel interaction between HMGA1a and StIP1 in murine terminally differentiated retina

Mol Cell Neurosci. 2006 Sep;33(1):81-7. doi: 10.1016/j.mcn.2006.06.009. Epub 2006 Jul 25.

Abstract

High mobility group protein A1a (HMGA1a) is expressed at high levels in embryonic cells and has been implicated in their transcriptional regulation. However, it has been reported that high levels of HMGA1a expression are normally detected in the photoreceptor of adult (terminally differentiated cells) murine retina. We showed that biochemical purification of the recombinant HMGA1a binding activity in nuclear fractions from murine retina, but not from hippocampus, resulted in STAT3 interacting protein 1 (StIP1) that formed a novel complex with HMGA1a, STAT3 and homeodomain-interacting protein kinase 2 (HIPK2). While StIP1 expressions in brain, liver, lung, heart, skeletal muscle, spleen and thymus have previously been demonstrated, this is the first report that StIP1 was expressed in nuclear fractions from murine retina, and that in murine retina there are several novel complexes of transcriptional regulators consisting of HMGA1a, StIP1, STAT3 and HIPK2.

MeSH terms

  • Animals
  • Carrier Proteins / metabolism
  • Cell Differentiation
  • Cell Line
  • Cell Nucleus / chemistry
  • Cell Nucleus / metabolism
  • HMGA1a Protein / genetics
  • HMGA1a Protein / metabolism*
  • Hippocampus / metabolism
  • Hypoxia
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Mice
  • Protein Serine-Threonine Kinases / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Retina / cytology*
  • Retina / growth & development
  • Retina / metabolism*

Substances

  • Carrier Proteins
  • Elp2 protein, mouse
  • Intracellular Signaling Peptides and Proteins
  • Recombinant Fusion Proteins
  • HMGA1a Protein
  • Hipk2 protein, mouse
  • Protein Serine-Threonine Kinases