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J Biol Chem, Vol. 273, Issue 15, 8549-8552, April 10, 1998
From the Institute for Molecular Virology, St. Louis University
Health Sciences Center, St. Louis, Missouri 63110
Adenovirus E1A proteins immortalize primary
animal cells and cooperate with several other oncogenes in oncogenic
transformation. These activities are primarily determined by the
N-terminal half (exon 1) of E1A. Although the C-terminal half (exon 2)
is also essential for some of these activities, it is dispensable for cooperative transformation with the activated T24 ras
oncogene. Exon 2 negatively modulates in vitro
cooperative transformation with T24 ras as well as
the tumorigenic and metastatic potentials of transformed cells. A short
C-terminal sequence of E1A governs the oncogenesis-restraining activity
of exon 2. This region of E1A binds with a cellular phosphoprotein,
CtBP, through a 5-amino acid motif, PLDLS, conserved among the E1A
proteins of human adenoviruses. To understand the mechanism by which
interaction between E1A and CtBP results in tumorigenesis-restraining
activity, we searched for cellular proteins that complex with CtBP.
Here, we report the cloning and characterization of a 125-kDa protein,
CtIP, that binds with CtBP through the PLDLS motif. E1A exon 2 peptides
that contain the PLDLS motif disrupt the CtBP-CtIP complex. Our results suggest that the tumorigenesis-restraining activity of E1A exon 2 may
be related to the disruption of the CtBP-CtIP complex through the PLDLS
motif.
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