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Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this binding by heregulin.

The processes by which ErbB-3, an inactive tyrosine kinase, exerts its biological effects are poorly understood. Using the yeast two-hybrid system, we have isolated an ErbB-3 binding protein (Ebp1) that interacts with the juxtamembrane domain of ErbB-3. This protein is identical to that predicted to be encoded for by the human PA2G4 gene. Ebp1 is the human homologue of a previously identified cell cycle-regulated mouse protein p38-2G4. Two transcripts of ebp1 mRNA (1.7 and 2.2 kb) were detected in several normal human organs. The interaction of Ebp1 with ErbB-3 was examined in vitro and in vivo. The first 15 amino acids of the juxtamembrane domain of ErbB-3 were essential for Ebp1 binding in vitro. Treatment of AU565 cells with the ErbB-3 ligand heregulin resulted in dissociation of Ebp1 from ErbB-3. Ebp1 translocated from the cytoplasm into the nucleus following heregulin stimulation. These findings suggest that Ebp1 may be a downstream member of an ErbB-3-regulated signal transduction pathway.

Pubmed ID: 10682683


  • Yoo JY
  • Wang XW
  • Rishi AK
  • Lessor T
  • Xia XM
  • Gustafson TA
  • Hamburger AW


British journal of cancer

Publication Data

February 2, 2000

Associated Grants

  • Agency: NCI NIH HHS, Id: F33CA63763
  • Agency: NCI NIH HHS, Id: R01CA 76047

Mesh Terms

  • Animals
  • Bacterial Proteins
  • Base Sequence
  • Biological Transport
  • Cell Line
  • Cell Nucleus
  • DNA Primers
  • Humans
  • Mice
  • Neuregulin-1
  • Protein Binding
  • RNA, Messenger
  • Receptor, Epidermal Growth Factor
  • Receptor, ErbB-3
  • Serine Endopeptidases
  • Two-Hybrid System Techniques