Evidence map›Paper›PMID 10207052›Full record

ArticleMolecular and cellular biology1999

The C terminus of Ku80 activates the DNA-dependent protein kinase catalytic subunit.

B K Singleton, M I Torres-Arzayus, S T Rottinghaus, G E Taccioli, P A Jeggo

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

77 citing papers in PubMed, 182 citations in OpenAlex.

  1. Article
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  20. Review

17 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

B K SingletonMRC Cell Mutation Unit, University of Sussex, Brighton BN1 9RR, United Kingdom.
M I Torres-Arzayus
S T Rottinghaus
G E Taccioli
P A Jeggo
Boston University · USUniversity of Sussex · GBUniversity of Cambridge · GB

Funding

DNA REPAIR/V(D)J RECOMBINATION--FUNCTIONAL STUDYR01CA076409 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI TACCIOLI, GUILLERMO E · 1998 to 2001
$467k
NCI NIH HHS CA76409Wellcome Trust
6 · The paper itself

Abstract

Ku is a heterodimeric protein with double-stranded DNA end-binding activity that operates in the process of nonhomologous end joining. Ku is thought to target the DNA-dependent protein kinase (DNA-PK) complex to the DNA and, when DNA bound, can interact and activate the DNA-PK catalytic subunit (DNA-PKcs). We have carried out a 3' deletion analysis of Ku80, the larger subunit of Ku, and shown that the C-terminal 178 amino acid residues are dispensable for DNA end-binding activity but are required for efficient interaction of Ku with DNA-PKcs. Cells expressing Ku80 proteins that lack the terminal 178 residues have low DNA-PK activity, are radiation sensitive, and can recombine the signal junctions but not the coding junctions during V(D)J recombination. These cells have therefore acquired the phenotype of mouse SCID cells despite expressing DNA-PKcs protein, suggesting that an interaction between DNA-PKcs and Ku, involving the C-terminal region of Ku80, is required for DNA double-strand break rejoining and coding but not signal joint formation. To gain further insight into important domains in Ku80, we report a point mutational change in Ku80 in the defective xrs-2 cell line. This residue is conserved among species and lies outside of the previously reported Ku70-Ku80 interaction domain. The mutational change nonetheless abrogates the Ku70-Ku80 interaction and DNA end-binding activity.

Indexed as

Antigens, NuclearDNA HelicasesAnimalsCell SurvivalCHO CellsClone CellsCricetinaeDNA-Activated Protein KinaseDNA-Binding ProteinsEnzyme ActivationGene ExpressionHumansKu AutoantigenNuclear ProteinsPoint MutationProtein Serine-Threonine KinasesAntigens, NuclearDNA-Activated Protein KinaseDNA-Binding ProteinsDNA HelicasesKu AutoantigenNuclear ProteinsPRKDC protein, humanProtein Serine-Threonine KinasesXRCC5 protein, humanXrcc6 protein, humanXrcc6 protein, mouse

Identifiers

PMID10207052
PMCPMC84121
OpenAlexW2111802021

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.