TRB3 interacts with CtIP and is overexpressed in certain cancers

Biochim Biophys Acta. 2007 Feb;1770(2):273-8. doi: 10.1016/j.bbagen.2006.09.025. Epub 2006 Oct 18.

Abstract

TRB3, a human homolog of Drosophila Tribbles, has been recently shown as a critical negative regulator of Akt and S6 kinase activation in a number of cellular processes. Here we found that TRB3 interacted with an important cell cycle regulator CtIP (CtBP-interacting protein) and the interaction involved the C-terminus of both proteins. Interestingly, TRB3 and CtIP co-localized to the nucleus in HeLa cells and exhibited a unique dot-like pattern. Finally, we demonstrated that TRB3 was overexpressed in multiple tumor tissues. Since CtIP plays important roles in cell cycle checkpoint control and it has been implicated in tumorigenesis, our data suggest that TRB3 may be involved in these biological processes through interacting with CtIP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • B-Lymphocytes
  • Base Sequence
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism*
  • Cell Cycle Proteins / genetics*
  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • DNA Primers
  • Endodeoxyribonucleases
  • Gene Expression Regulation, Enzymologic
  • Gene Expression Regulation, Neoplastic*
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Neoplasms / enzymology
  • Neoplasms / genetics
  • Nuclear Proteins / genetics*
  • Nuclear Proteins / metabolism*
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Plasmids
  • Polymerase Chain Reaction
  • Protein Serine-Threonine Kinases / genetics*
  • Protein Serine-Threonine Kinases / metabolism*
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism*
  • T-Lymphocytes
  • Transfection

Substances

  • Carrier Proteins
  • Cell Cycle Proteins
  • DNA Primers
  • Nuclear Proteins
  • Peptide Fragments
  • Repressor Proteins
  • TRIB3 protein, human
  • Protein Serine-Threonine Kinases
  • Endodeoxyribonucleases
  • RBBP8 protein, human