The DNA-dependent protein kinase catalytic subunit phosphorylation sites in human Artemis (Q27919681)

2

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Michael R Lieber

6

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Klaus Schwarz

5

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Haihui Lu

3

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Doris Niewolik

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

7 October 2005

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published in

1 reference

The mechanism and regulation of chromosomal V(D)J recombination

PubMed

volume

280

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issue

40

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page(s)

33839-46

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cites work

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Human severe combined immune deficiency and DNA repair

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The RAG proteins and V(D)J recombination: complexes, ends, and transposition

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Unraveling V(D)J recombination; insights into gene regulation

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The mechanism of vertebrate nonhomologous DNA end joining and its role in V(D)J recombination

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The role of the non-homologous end-joining pathway in lymphocyte development

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Artemis, a novel DNA double-strand break repair/V(D)J recombination protein, is mutated in human severe combined immune deficiency.

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Leaky Scid phenotype associated with defective V(D)J coding end processing in Artemis-deficient mice

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Defective DNA repair and increased genomic instability in Artemis-deficient murine cells

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Functional and biochemical dissection of the structure-specific nuclease ARTEMIS

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The metallo-beta-lactamase/beta-CASP domain of Artemis constitutes the catalytic core for V(D)J recombination

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Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family

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The DNA-dependent protein kinase

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The DNA-dependent protein kinase: the director at the end.

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Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNA-dependent protein kinase

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Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair

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Non-homologous end joining requires that the DNA-PK complex undergo an autophosphorylation-dependent rearrangement at DNA ends.

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Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53.

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DNA-PK phosphorylation sites in XRCC4 are not required for survival after radiation or for V(D)J recombination

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Identification of DNA-PKcs phosphorylation sites in XRCC4 and effects of mutations at these sites on DNA end joining in a cell-free system

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Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response

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Phosphorylation of Artemis following irradiation-induced DNA damage

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A pathway of double-strand break rejoining dependent upon ATM, Artemis, and proteins locating to gamma-H2AX foci.

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Artemis deficiency confers a DNA double-strand break repair defect and Artemis phosphorylation status is altered by DNA damage and cell cycle progression

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Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in response to DNA damage.

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The DNA-dependent protein kinase interacts with DNA to form a protein-DNA complex that is disrupted by phosphorylation

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