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53BP1 promotes ATM activity through direct interactions with the MRN complex.

Ji-Hoon Lee¹, Aaron A Goodarzi, Penny A Jeggo

¹Howard Hughes Medical Institute and the Department of Molecular Genetics and Microbiology, The University of Texas at Austin, Austin, TX 78712, USA.

The EMBO Journal

|December 17, 2009

Summary

Mediator proteins 53BP1 and BRCA1 amplify DNA double-strand break (DSB) signaling by the MRN complex and ATM kinase. Their interaction with MRN is crucial for ATM activation and DNA repair.

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Area of Science:

Molecular Biology
Genetics
Cell Biology

Background:

The Mre11/Rad50/Nbs1 (MRN) complex is critical for activating ATM kinase at DNA double-strand break (DSB) sites.
Efficient ATM signaling also requires mediator proteins like 53BP1 and BRCA1 in human cells.

Purpose of the Study:

To investigate the role of 53BP1 and BRCA1 in ATM activation.
To understand how these mediator proteins influence MRN-ATM interactions and DNA repair.

Main Methods:

Investigated protein interactions between MRN, 53BP1, and BRCA1.
Analyzed the impact of 53BP1 and BRCA1 on ATM kinase activation and substrate phosphorylation.
Assessed DNA DSB repair in mammalian cells.

Main Results:

53BP1 and BRCA1 amplify MRN-mediated ATM activation, especially when MRN-ATM interactions are impaired.
A direct interaction between MRN and 53BP1's BRCT repeats is essential for this amplification.
This interaction leads to hyper-phosphorylation of Nbs1 and 53BP1, and affects 53BP1 multimer structure, promoting ATM substrate phosphorylation and DNA repair.

Conclusions:

53BP1 and BRCA1 act as crucial amplifiers of the MRN-ATM DNA damage response pathway.
The structural integrity of 53BP1, influenced by its BRCT domains, is vital for efficient DNA repair and ATM signaling.