The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks (Q24309142)

1

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Dana R Lilli

2

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Jeffrey Patterson-Fortin

3

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Kara A Coleman

4

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Devon E Morrissey

5

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Roger A Greenberg

Proceedings of the National Academy of Sciences of the United States of America

6

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language of work or name

English

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publication date

3 March 2009

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published in

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volume

106

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issue

9

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page(s)

3166-71

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cites work

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RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins

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The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair response

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Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response

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Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks

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Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

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Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks

7 April 2017

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Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage

27 September 2017

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Proteasome function is required for DNA damage response and fanconi anemia pathway activation

27 September 2017

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Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases.

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A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling

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27 September 2017

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gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair

27 September 2017

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ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation

27 September 2017

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Distinct spatiotemporal dynamics of mammalian checkpoint regulators induced by DNA damage

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Deubiquitination of FANCD2 is required for DNA crosslink repair

27 September 2017

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Inhibitors of the proteasome suppress homologous DNA recombination in mammalian cells.

30 May 2018

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Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0807485106

21 January 2018

Identifiers

DOI

10.1073/PNAS.0807485106

1 reference

2600143

ADS bibcode

2009PNAS..106.3166S

0 references

2600143

1 reference

1 reference

1 reference