analysis-nonhomologous-end-joining-homologous-recombination

Analysis of Nonhomologous End Joining and Homologous Recombination Efficiency in HEK-293T Cells Using GFP-Based Reporter Systems

DNA double-strand breaks (DSBs) represent the most perilous DNA lesions, capable of inducing substantial genetic information loss and cellular demise. In ...

Qiqihar Medical University

Cytoplasmic FAM21 works as a guiding protein in Wiskott-Aldrich Syndrome Protein and SCAR Homolog (WASH) complex by linking WASH complex to endosomes through its interaction with retromer. Recently, we have reported that nuclear WASH localizes to DNA double strand break (DSB) sites to promote DNA repair through non-homologous end-joining (NHEJ). However, whether FAM21, the close partner of WASH, is involved in the nuclear WASH localization and DNA repair remains to be clarified. Here, we show that FAM21 interacts with Ku and the interaction between C-terminal FAM21 and Ku is essential for its recruitment to DSB sites. Moreover, FAM21 depletion led to decreases in WASH recruitment to damaged DNA and repair capacity upon DNA damage. Taken together, these results reveal that FAM21 promotes DNA repair by orchestrating the recruitment of WASH to DSB sites, providing a mechanistic insight into WASH-dependent DNA DSB repair.

Tuo Tang

Laboratory of Protein Structure and Function,
Institute of Medicine and Pharmacy,
Laboratory of Protein Structure and Function, Institute of Medicine and Pharmacy

Qiqihar Medical University

Analysis of Nonhomologous End Joining and Homologous Recombination Efficiency in HEK-293T Cells Using GFP-Based Reporter Systems

Tuo Tang

Laboratory of Protein Structure and Function,Institute of Medicine and Pharmacy,Laboratory of Protein Structure and Function, Institute of Medicine and Pharmacy

Qiqihar Medical University

Analysis of Nonhomologous End Joining and Homologous Recombination Efficiency in HEK-293T Cells Using GFP-Based Reporter Systems

Laboratory of Protein Structure and Function,
Institute of Medicine and Pharmacy,
Laboratory of Protein Structure and Function, Institute of Medicine and Pharmacy