Unknown

Dataset Information

0

The DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosis.


ABSTRACT: The DNA-dependent protein kinase (DNA-PK) is a serine/threonine protein kinase composed of a large catalytic subunit (DNA-PKcs) and the Ku70/80 heterodimer. Over the past two decades, significant progress has been made in elucidating the role of DNA-PK in non-homologous end joining (NHEJ), the major pathway for repair of ionizing radiation-induced DNA double strand breaks in human cells and recently, additional roles for DNA-PK have been reported. In this review, we will describe the biochemistry, structure and function of DNA-PK, its roles in DNA double strand break repair and its newly described roles in mitosis and other cellular processes.

SUBMITTER: Jette N 

PROVIDER: S-EPMC4502593 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

The DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosis.

Jette Nicholas N   Lees-Miller Susan P SP  

Progress in biophysics and molecular biology 20141227 2-3


The DNA-dependent protein kinase (DNA-PK) is a serine/threonine protein kinase composed of a large catalytic subunit (DNA-PKcs) and the Ku70/80 heterodimer. Over the past two decades, significant progress has been made in elucidating the role of DNA-PK in non-homologous end joining (NHEJ), the major pathway for repair of ionizing radiation-induced DNA double strand breaks in human cells and recently, additional roles for DNA-PK have been reported. In this review, we will describe the biochemistr  ...[more]

Similar Datasets

| S-EPMC2867755 | biostudies-literature
| S-EPMC6218445 | biostudies-literature
| S-EPMC6398140 | biostudies-literature
| S-EPMC7457334 | biostudies-literature
| S-EPMC7337934 | biostudies-literature
| S-EPMC2861619 | biostudies-literature
| S-EPMC4178966 | biostudies-literature
| S-EPMC4282560 | biostudies-literature
| S-EPMC3540944 | biostudies-literature
| S-EPMC2519706 | biostudies-literature