Structural basis of γH2AX recognition by human PTIP BRCT5-BRCT6 domains in the DNA damage response pathway (Q24296259)

2

Zhenhua

Shao

1 reference

30 October 2023

Fudong Li

3

Fudong

Li

1 reference

30 October 2023

Maikun Teng

6

Maikun

Teng

1 reference

30 October 2023

Xu Li

7

Xu

Requirement of ATM-dependent phosphorylation of brca1 in the DNA damage response to double-strand breaks

Li

1 reference

30 October 2023

language of work or name

English

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publication date

15 December 2011

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published in

FEBS Letters

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volume

585

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issue

24

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page(s)

3874-9

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cites work

1 reference

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Structural and functional analysis of the Crb2-BRCT2 domain reveals distinct roles in checkpoint signaling and DNA damage repair

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PTIP, a novel BRCT domain-containing protein interacts with Pax2 and is associated with active chromatin

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The BRCT-domain containing protein PTIP links PAX2 to a histone H3, lysine 4 methyltransferase complex

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PTIP promotes DNA double-strand break repair through homologous recombination

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Human PTIP facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation

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Accumulation of Pax2 transactivation domain interaction protein (PTIP) at sites of DNA breaks via RNF8-dependent pathway is required for cell survival after DNA damage

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Phospho-epitope binding by the BRCT domains of hPTIP controls multiple aspects of the cellular response to DNA damage

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BRCT Repeats As Phosphopeptide-Binding Modules Involved in Protein Targeting

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Assembly of checkpoint and repair machineries at DNA damage sites

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Assembly and function of DNA double-strand break repair foci in mammalian cells

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PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex

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γH2A binds Brc1 to maintain genome integrity during S-phase

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The BRCT Domain Is a Phospho-Protein Binding Domain

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Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail

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MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks

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