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J Biol Chem, Vol. 273, Issue 40, 25654-25658, October 2, 1998
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From the The Src-like protein-tyrosine kinase Lyn is
activated by ionizing radiation and certain other DNA-damaging agents,
whereas the DNA-dependent protein kinase (DNA-PK),
consisting of the catalytic subunits (DNA-PKcs) and
Ku DNA-binding components, requires DNA double-stranded breaks for
activation. Here we demonstrate that Lyn associates constitutively with
DNA-PKcs. The SH3 domain of Lyn interacts directly with
DNA-PKcs near a leucine zipper homology domain. We also
show that Lyn phosphorylates DNA-PKcs but not Ku in
vitro. The interaction between Lyn and DNA-PKcs inhibits DNA-PKcs activity and the ability of DNA-PKcs
to form a complex with Ku/DNA. These results support the hypothesis
that there are functional interactions between Lyn and
DNA-PKcs in the response to DNA damage.
Department of Adult Oncology, Dana-Farber
Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, the ¶ Department of Radiation and Cellular Biology, University of
Chicago, Chicago, Illinois 60637, and the § Department of
Microbiology and Molecular Genetics, Harvard Medical School,
Boston, Massachusetts 02115
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