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Mater Sci Nanotechnol 2017 | Volume 1 Issue 2
allied
academies
Nanomaterials and Nanochemistry
November 29-30, 2017 | Atlanta, USA
International Conference on
T
o prevent genomic instability disorders, cells have
developed a DNA damage response. The response
involves various proteins that sense damaged DNA,
transduce damage signals, and effect DNA repair. Among
various types of DNA damage, double-stranded breaks are
highly toxic to genomic integrity. Homologous recombination
(HR) repair is an essential mechanism that fixes DNA damage
because of its high level of accuracy. Although factors in the
repair pathway are well established, pinpointing the exact
mechanisms of repair and devising therapeutic applications
requires more studies. RAP80 is one of key molecules in
DNA damage response pathway. This protein localizes to
sites of DNA insults to enhance the DNA-damage responses.
I identified TRAIP/RNF206 as a novel RAP80-interacting
protein and found that TRAIP is necessary for translocation
of RAP80 to DNA lesions. Biochemical analysis revealed that
the N terminus of TRAIP is crucial for RAP80 interaction, while
the C terminus of TRAIP is required for TRAIP localization
to sites of DNA damage through a direct interaction with
RNF20-RNF40. My research demonstrated that the novel
RAP80-binding partner TRAIP regulates recruitment of the
damage signaling machinery and promotes homologous
recombination.
e:
likej82@live.co.krIdentifying noble factors and their functions in DNA damage response pathway
Namsoo Lee
Sungkyunkwan University, South Korea