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Review
. 2007 Oct 22;179(2):183-6.
doi: 10.1083/jcb.200705106. Epub 2007 Oct 15.

DNA-dependent protein kinase in nonhomologous end joining: a lock with multiple keys?

Eric Weterings  1 , David J Chen
Affiliations
Review

DNA-dependent protein kinase in nonhomologous end joining: a lock with multiple keys?

Eric Weterings et al. J Cell Biol. .

Abstract

The DNA-dependent protein kinase (DNA-PK) is one of the central enzymes involved in DNA double-strand break (DSB) repair. It facilitates proper alignment of the two ends of the broken DNA molecule and coordinates access of other factors to the repair complex. We discuss the latest findings on DNA-PK phosphorylation and offer a working model for the regulation of DNA-PK during DSB repair.

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Figures

Figure 1.
Figure 1.
Schematic overview of the NHEJ process. (1) Recognition of a DSB by Ku 70/80. (2) Tethering of DNA ends by DNA-PKCS. (3) Processing of DNA ends. (4) Ligation of DNA ends.
Figure 2.
Figure 2.
Regulation of DNA end accessibility by DNA-PKCS phosphorylation. DNA-PKCS protects the DNA ends until trans-autophosphorylation induces a conformational change that enables DNA end processing and ligation. In addition to autophosphorylation, ATM-mediated phosphorylation of DNA-PKCS may play a role in this process.
Figure 3.
Figure 3.
Phosphorylation sites within the DNA-PKCS molecule. The 2609 cluster (Chan et al., 2002; Douglas et al., 2002), 2056 cluster (Chen et al., 2005; Cui et al., 2005), 3205 residue (Douglas et al., 2002), 3950 residue (Douglas et al., 2007), and 3821, 4026, and 4102 residues (Ma et al., 2005) are included. S, serine; T, threonine.
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